PIN1

UniProt ID: Q9C6B8
Organism: Arabidopsis thaliana
Review Status: DRAFT
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Gene Description

PIN1 (PIN-FORMED 1, AtPIN1) is a plasma-membrane-localized, polytopic (ten-transmembrane) secondary transporter of the auxin efflux carrier (PIN/AEC, TC 2.A.69.1) family that mediates cellular efflux of the phytohormone auxin (indole-3-acetic acid and related indolic auxins). The transmembrane domain adopts a NhaA fold composed of two inverted five-helix repeats, with an intracellular substrate-binding pocket that coordinates IAA, and PIN1 assembles as a homodimer. Auxin efflux activity is enhanced by AGC-kinase (e.g. D6PK) phosphorylation and competitively inhibited by the synthetic inhibitor N-1-naphthylphthalamic acid (NPA). The defining feature of PIN1 is its polar (apical or basal) localization within the plasma membrane, which is established and maintained by reversible phosphorylation of its central hydrophilic loop (by PINOID/PID and related AGC kinases, counteracted by PP2A/PP6-type phosphatases) and by GNOM-dependent endosomal recycling, together with MAB4/MEL adaptor proteins that limit lateral diffusion. Because the orientation of PIN1 in the membrane dictates the direction of intercellular (polar) auxin flow, PIN1 generates the local auxin gradients and maxima that pattern plant development. It controls vascular tissue formation, embryonic apical-basal axis and cotyledon formation, leaf shaping and venation, shoot apical meristem organ initiation and phyllotaxis, inflorescence and flower formation, gravitropism and photomorphogenic growth. Loss of PIN1 produces naked, pin-shaped inflorescences and broad defects in lateral organ number, size, shape and position.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0005886 plasma membrane
IEA
GO_REF:0000044
ACCEPT
Summary: PIN1 is an integral plasma-membrane auxin efflux carrier; the plasma membrane is its functional location. This UniProt subcellular-location mapping is fully consistent with experimental evidence.
Reason: The plasma membrane is the bona fide functional compartment of PIN1, confirmed by multiple experimental studies; this is a core localization.
Supporting Evidence:
PMID:33705718
PINs, MAB4/MELs, and AGC kinases interact in the same complex at the plasma membrane.
GO:0016020 membrane
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: Generic membrane localization from InterPro mapping. PIN1 is a multi-pass membrane protein, so the term is correct but far less informative than the plasma-membrane annotation.
Reason: Correct but a broad parent of the more specific (and experimentally supported) plasma membrane term; retained as non-core background.
Supporting Evidence:
PMID:35917925
The transmembrane domain of PIN1 has ten transmembrane segments (TM1 to TM10), with both N and C termini located extracellularly
GO:0055085 transmembrane transport
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: PIN1 mediates transmembrane transport of auxin across the plasma membrane. The term is correct but is a broad parent of the more specific auxin export and polar auxin transport terms.
Reason: Accurate but generic; the more precise auxin-transport terms capture the core function. Retained as a correct broad parent.
Supporting Evidence:
PMID:35917925
These results show that PIN1 mediates active auxin efflux when expressed in HEK293F cells, and is further activated by D6PK.
GO:0060918 auxin transport
IEA
GO_REF:0000117
ACCEPT
Summary: PIN1 is the founding auxin efflux carrier and a central mediator of auxin transport. This ARBA electronic annotation is well supported.
Reason: Core biological process; PIN1-mediated efflux is rate-limiting for cellular auxin transport.
Supporting Evidence:
PMID:9856939
Mutations affecting the PIN-FORMED (PIN1) gene diminish polar auxin transport in Arabidopsis thaliana inflorescence axes.
file:ARATH/PIN1/PIN1-deep-research-falcon.md
demonstrates PIN1-mediated auxin (IAA) efflux and inhibitor (NPA) binding, matching the UniProt record provided.
GO:0005515 protein binding
IPI
PMID:17237354
Interactions among PIN-FORMED and P-glycoprotein auxin trans...
MARK AS OVER ANNOTATED
Summary: IntAct interaction with ABCB19/PGP19 (Q9LJX0), a P-glycoprotein auxin transporter that co-acts with PIN1 in directional auxin transport. The bare protein binding term is uninformative about molecular function.
Reason: The interaction with ABCB19 is real and biologically relevant to auxin transport, but GO:0005515 is too generic to convey function; per curation guidance bare protein binding is not retained as a core molecular function.
Supporting Evidence:
PMID:17237354
Specific PGP–PIN interactions were seen in yeast two-hybrid and coimmunoprecipitation assays.
GO:0005515 protein binding
IPI
PMID:17889649
Antagonistic regulation of PIN phosphorylation by PP2A and P...
UNDECIDED
Summary: IntAct interaction with PINOID/PID (O64682), the AGC kinase that phosphorylates the PIN1 hydrophilic loop to control apical-basal polarity. The generic protein binding term is uninformative.
Reason: The cited publication (PMID:17889649) is available only as an abstract that describes PP2A/PINOID colocalization with and antagonistic phosphorylation of PINs; it does not report a direct physical PIN1-PID binding assay, so it does not substantiate this GO:0005515 (protein binding) IPI annotation. No verbatim supporting passage for a PIN1-PID interaction could be extracted.
GO:0005515 protein binding
IPI
PMID:20080776
PIN phosphorylation is sufficient to mediate PIN polarity an...
UNDECIDED
Summary: IntAct interaction with PID (O64682) in the context of phosphorylation directing PIN polarity. Generic protein binding term is uninformative.
Reason: The cited publication (PMID:20080776) characterizes a conserved phosphorylation site that controls PIN polarity and explicitly reports that its in vitro results do NOT support this site being a PID target; it does not report a direct physical PIN1-PID binding assay and therefore does not substantiate this GO:0005515 (protein binding) IPI annotation. No verbatim supporting passage for a PIN1-PID interaction could be extracted.
GO:0005886 plasma membrane
EXP
PMID:20439545
Differential auxin-transporting activities of PIN-FORMED pro...
ACCEPT
Summary: Experimental localization of PIN1 to the plasma membrane in root hair cells, consistent with its function as a PM auxin efflux carrier.
Reason: Direct experimental support for the core plasma-membrane localization.
Supporting Evidence:
PMID:20439545
those PINs were localized in the plasma membrane, where they likely export auxin to the apoplast
GO:0042802 identical protein binding
IDA
PMID:35917925
Structural insights into auxin recognition and efflux by Ara...
ACCEPT
Summary: Cryo-EM shows PIN1 forms a homodimer with a TM1/TM2/TM7 dimer interface. Identical protein binding (self-association) is directly demonstrated.
Reason: Directly supported by the structure; a genuine, informative molecular property (self-interaction), retained as a non-core but real activity.
Supporting Evidence:
PMID:35917925
we determined a dimeric structure of PIN1
GO:0042803 protein homodimerization activity
IDA
PMID:35917925
Structural insights into auxin recognition and efflux by Ara...
ACCEPT
Summary: PIN1 assembles as a homodimer in the cryo-EM structure, with TM1, TM2 and TM7 forming the dimer interface.
Reason: Structurally established homodimerization; an informative molecular function (more specific than identical protein binding).
Supporting Evidence:
PMID:35917925
TM1, TM2 and TM7 constitute the dimer interface, which consists mainly of hydrophobic residues
GO:0010315 auxin export across the plasma membrane
IDA
PMID:35917925
Structural insights into auxin recognition and efflux by Ara...
ACCEPT
Summary: PIN1 expressed in HEK293F cells mediates active IAA efflux across the plasma membrane (enhanced by D6PK, inhibited by NPA). This is the most precise biological-process term for the PIN1 efflux event.
Reason: Directly demonstrated auxin export across the PM; a core process.
Supporting Evidence:
PMID:35917925
These results show that PIN1 mediates active auxin efflux when expressed in HEK293F cells, and is further activated by D6PK. This PIN1-mediated auxin efflux is inhibited by NPA
file:ARATH/PIN1/PIN1-deep-research-falcon.md
that exports auxin from the cytosol toward the apoplast, thereby enabling
GO:0010329 auxin efflux transmembrane transporter activity
IDA
PMID:35917925
Structural insights into auxin recognition and efflux by Ara...
ACCEPT
Summary: Heterologous reconstitution plus cryo-EM with bound IAA establish PIN1 as a direct auxin efflux transmembrane transporter; IAA is coordinated in an intracellular pocket by conserved residues (V51, N112, N478, I582) and mutation of these residues impairs efflux activity. This is the core molecular function.
Reason: Strongest, most informative MF annotation; directly supported by structure-function evidence.
Supporting Evidence:
PMID:35917925
In the structure, IAA is coordinated through both hydrogen bonding and hydrophobic interactions
PMID:35917925
All interacting residues (V51, N112, N478 and I582) are highly conserved in PINs
file:ARATH/PIN1/PIN1-deep-research-falcon.md
Arabidopsis PIN1 was solved in multiple inward-facing conformations (apo, IAA-bound, NPA-bound), revealing a conserved transporter fold and a defined intracellular binding pocket that coordinates IAA.
file:ARATH/PIN1/PIN1-deep-research-falcon.md
this provides a molecular definition of PIN1’s substrate recognition.
GO:0005515 protein binding
IPI
PMID:33705718
AGC kinases and MAB4/MEL proteins maintain PIN polarity by l...
MARK AS OVER ANNOTATED
Summary: IntAct/UniProt interaction with NPY5/MEL1 (Q0WL52), a MAB4/MEL adaptor recruited to the plasma membrane by PIN1 to maintain polarity. Generic protein binding term is uninformative.
Reason: The PIN1-NPY5/MEL1 interaction is mechanistically important for polarity maintenance, but GO:0005515 conveys no specific function.
Supporting Evidence:
PMID:33705718
MAB4/MELs are recruited to the plasma membrane by the PINs and in concert with the AGC kinases maintain PIN polarity
GO:0071944 cell periphery
IDA
PMID:33705718
AGC kinases and MAB4/MEL proteins maintain PIN polarity by l...
KEEP AS NON CORE
Summary: PIN1 localizes to the cell periphery (plasma membrane and polar PM domains). Correct but a broad parent of the specific plasma-membrane term.
Reason: Accurate but generic relative to the plasma-membrane and polar-domain annotations; retained as non-core.
Supporting Evidence:
PMID:33705718
the polar subcellular plasma membrane (PM) localization of the PIN-FORMED (PIN) auxin efflux carriers
GO:0005886 plasma membrane
IDA
PMID:33705718
AGC kinases and MAB4/MEL proteins maintain PIN polarity by l...
ACCEPT
Summary: Direct experimental confirmation of PIN1 plasma-membrane localization within the PIN-MAB4/MEL-AGC kinase complex.
Reason: Core localization with direct experimental support.
Supporting Evidence:
PMID:33705718
we demonstrate that PINs, MAB4/MELs, and AGC kinases interact in the same complex at the plasma membrane
GO:0016324 apical plasma membrane
IDA
PMID:33705718
AGC kinases and MAB4/MEL proteins maintain PIN polarity by l...
KEEP AS NON CORE
Summary: PIN1 occupies polar (apical or basal) plasma-membrane domains; apical localization is observed in specific tissues and is phosphorylation-dependent. This polar PM subdomain is central to PIN1 directional function.
Reason: A real and functionally important polar PM subdomain; kept as non-core because the polarity (apical versus basal) is tissue- and phosphorylation-dependent rather than a fixed property, while plasma membrane is the core location.
Supporting Evidence:
PMID:20407025
The apical-basal polar localization of the PIN proteins that determines the direction of auxin flow is controlled by reversible phosphorylation of the PIN hydrophilic loop
GO:0045177 apical part of cell
IDA
PMID:33705718
AGC kinases and MAB4/MEL proteins maintain PIN polarity by l...
KEEP AS NON CORE
Summary: Reflects PIN1 apical polar localization. Correct but a broad cellular anatomical parent of apical plasma membrane.
Reason: Consistent with polar localization; generic relative to apical plasma membrane. Retained as non-core.
Supporting Evidence:
PMID:20407025
Conversely, phosphomimic PIN1:GFP (Ser to Glu) showed apical localization in the shoot apex but did not rescue pin1 inflorescence defects.
GO:0005515 protein binding
IPI
PMID:36226797
SUE4, a novel PIN1-interacting membrane protein, regulates a...
MARK AS OVER ANNOTATED
Summary: TAIR interaction with SUE4 (AT3G55880), a PIN1-interacting membrane protein that regulates acropetal auxin transport under sulfur deficiency. Generic protein binding term is uninformative.
Reason: Biologically relevant interaction but GO:0005515 conveys no specific molecular function.
Supporting Evidence:
PMID:36226797
SUE4, a novel plasma membrane-localized protein, interacts with the polar auxin transporter PIN1
GO:0010168 ER body
IDA
PMID:36398993
Mapping of the Classical Mutation rosette Highlights a Role ...
REMOVE
Summary: This annotation assigns PIN1 to an ER body. PMID:36398993 is a study of the tomato classical mutation rosette mapping to the BIG/UBR4 ortholog and the role of calcium in wound-induced rooting; the ER association it reports is for BIG, not for PIN1. PIN1 is a long PIN that resides at the plasma membrane, whereas only the short PINs (PIN5/PIN8) are ER-localized. There is no sound evidence that PIN1 is an ER-body resident protein.
Reason: Appears to be a mis-assignment; the cited paper does not support PIN1 ER-body localization, and PIN1 is an established plasma-membrane protein.
Supporting Evidence:
PMID:35917925
The short PINs are typically found at the endoplasmic reticulum, whereas the long PINs are at the plasma membrane and dynamically regulated by endocytosis and recycling
PMID:36398993
Subcellular localization of BIG suggests that, like its mammalian ortholog, it is associated with the endoplasmic reticulum.
GO:0048830 adventitious root development
IMP
PMID:36398993
Mapping of the Classical Mutation rosette Highlights a Role ...
KEEP AS NON CORE
Summary: PIN1-dependent auxin transport is implicated in wound-induced (adventitious) rooting; in the cited study PIN1 accumulation was sensitive to calcium levels in ro/big mutants, linking PIN1-mediated transport to wound-induced root formation. This is a downstream developmental output of auxin transport.
Reason: A pleiotropic downstream developmental process mediated via PIN1 auxin transport; evidence is indirect (a tomato BIG study). Retained as non-core.
Supporting Evidence:
PMID:36398993
accumulation of the auxin transporter PIN-FORMED1 (PIN1) was sensitive to calcium levels in the ro/big mutants
GO:0060918 auxin transport
IMP
PMID:36398993
Mapping of the Classical Mutation rosette Highlights a Role ...
ACCEPT
Summary: Genetic and physiological evidence that PIN1 contributes to auxin transport (reduced transport rates and NPA hypersensitivity in the relevant mutants). Consistent with PIN1 core role in auxin transport.
Reason: Core biological process, corroborated by the founding and structural studies.
Supporting Evidence:
PMID:36398993
ro mutants were severely inhibited in formation of wound-induced roots (WiRs) and had reduced auxin transport rates.
GO:0010262 somatic embryogenesis
IMP
PMID:36345646
Endogenous auxin maintains embryonic cell identity and promo...
KEEP AS NON CORE
Summary: Endogenous auxin (transported by PINs including PIN1) maintains embryonic cell identity and promotes somatic embryo development. This is a downstream developmental process patterned by PIN1-generated auxin gradients.
Reason: Pleiotropic developmental output acting via auxin transport; non-core.
Supporting Evidence:
PMID:36345646
polar auxin transport, with AUXIN/LIKE-AUX influx and PIN-FORMED1 efflux carriers as important drivers, is required for the transition of embryonic cells to proembryos
GO:0005737 cytoplasm
HDA
PMID:15610358
High-throughput protein localization in Arabidopsis using Ag...
UNDECIDED
Summary: High-throughput GFP-fusion localization. PIN1 cycles between the plasma membrane and endosomal compartments via GNOM-dependent recycling, so a cytoplasmic/endosomal signal is expected for trafficking intermediates, but the plasma membrane is the functional site.
Reason: The cited publication (PMID:15610358) is a generic high-throughput GFP-fusion localization methods paper; its available abstract does not mention PIN1 or report a cytoplasmic localization for PIN1 specifically, so it does not substantiate this GO:0005737 (cytoplasm) annotation. No verbatim PIN1-specific supporting passage could be extracted.
GO:0009506 plasmodesma
HDA
PMID:21533090
Arabidopsis plasmodesmal proteome.
UNDECIDED
Summary: PIN1 was detected in a plasmodesmal proteome. Plasmodesmal plasma membrane is continuous with the cell-surface PM, so detection here is plausible for a PM protein but does not indicate a distinct functional plasmodesmal role.
Reason: The cited publication (PMID:21533090) is the Arabidopsis plasmodesmal proteome paper, but its cached text does not mention PIN1 anywhere, so it does not substantiate plasmodesmal detection of PIN1 for this GO:0009506 (plasmodesma) annotation. No verbatim PIN1-specific supporting passage could be extracted.
GO:0005515 protein binding
IPI
PMID:22715043
A PP6-type phosphatase holoenzyme directly regulates PIN pho...
MARK AS OVER ANNOTATED
Summary: UniProt interactions with FYPP1 (Q9LHE7) and FYPP3 (Q9SX52), subunits of a PP6-type phosphatase holoenzyme that dephosphorylates PIN1 and regulates auxin efflux. Generic protein binding term is uninformative.
Reason: A real regulatory phosphatase interaction, but GO:0005515 conveys no specific molecular function.
Supporting Evidence:
PMID:22715043
FyPP1 and FyPP3 interact with a subset of PIN proteins and regulate PIN protein phosphorylation and targeting in vivo
GO:0010329 auxin efflux transmembrane transporter activity
IMP
PMID:9856939
Regulation of polar auxin transport by AtPIN1 in Arabidopsis...
ACCEPT
Summary: The founding study identified AtPIN1 as a transmembrane component of the auxin efflux carrier; pin1 mutants have diminished polar auxin transport. This mutant-phenotype evidence supports the core efflux transporter function.
Reason: Core molecular function, independently established here and later directly demonstrated structurally (PMID:35917925).
Supporting Evidence:
PMID:9856939
AtPIN1 may act as a transmembrane component of the auxin efflux carrier.
GO:0005515 protein binding
IPI
PMID:17586653
Ubiquitin lysine 63 chain forming ligases regulate apical do...
MARK AS OVER ANNOTATED
Summary: UniProt interaction (Q9LY87) in the context of K63 ubiquitin chain ligases regulating apical dominance. Generic protein binding term is uninformative about molecular function.
Reason: Interaction is recorded but GO:0005515 conveys no specific function.
Supporting Evidence:
PMID:17586653
RGLG2 and PIN1 can interact in the yeast two-hybrid system
GO:0009793 embryo development ending in seed dormancy
IMP
PMID:20407025
Phosphorylation of conserved PIN motifs directs Arabidopsis ...
KEEP AS NON CORE
Summary: Loss-of-phosphorylation PIN1 internalizes during embryogenesis causing strong embryo defects, demonstrating a PIN1 requirement in embryo development through proper polar auxin transport.
Reason: Important downstream developmental role mediated by PIN1 polar auxin transport; pleiotropic, non-core.
Supporting Evidence:
PMID:20407025
induced internalization of PIN1:GFP during embryogenesis, leading to strong embryo defects
GO:0005886 plasma membrane
IDA
PMID:18337510
Auxin transport inhibitors impair vesicle motility and actin...
UNDECIDED
Summary: This annotation cites PMID:18337510 for PIN1 plasma-membrane localization, but that paper studies how auxin transport inhibitors affect actin-dependent vesicle trafficking; its available text does not present PIN1-specific plasma-membrane localization data.
Reason: The cited publication (PMID:18337510) does not substantiate PIN1 plasma-membrane localization; its available abstract/discussion concern actin-stabilizing effects of auxin transport inhibitors on vesicle motility and do not localize PIN1 to the plasma membrane. No verbatim PIN1-specific supporting passage could be extracted. (PIN1 plasma-membrane localization remains well supported by other annotations here, e.g. PMID:33705718 and PMID:35917925.)
GO:0005886 plasma membrane
IDA
PMID:19825598
Plasma membrane-associated SCAR complex subunits promote cor...
UNDECIDED
Summary: This annotation cites PMID:19825598 for PIN1 plasma-membrane localization, but that paper concerns plasma-membrane localization of the SCAR complex subunits BRK1 and SCAR1 and cortical F-actin; its available text does not mention PIN1.
Reason: The cited publication (PMID:19825598) does not mention PIN1; it reports plasma-membrane localization of SCAR complex subunits (BRK1, SCAR1), not PIN1, so it does not substantiate this GO:0005886 (plasma membrane) annotation. No verbatim PIN1-specific supporting passage could be extracted. (PIN1 plasma-membrane localization remains well supported by other annotations here, e.g. PMID:33705718 and PMID:35917925.)
GO:0005886 plasma membrane
IDA
PMID:18539115
Differential expression of WOX genes mediates apical-basal a...
UNDECIDED
Summary: This annotation cites PMID:18539115 for PIN1 plasma-membrane localization, but that paper is a study of WOX gene expression in apical-basal axis formation; its abstract mentions PIN1 only as a reporter gene for auxin response and provides no PIN1 plasma-membrane localization data.
Reason: The cited publication (PMID:18539115) does not substantiate PIN1 plasma-membrane localization; its available text concerns WOX2/WOX8 cell-fate regulators and references a PIN1 reporter only in the context of auxin response maxima. No verbatim passage localizing PIN1 to the plasma membrane could be extracted. (PIN1 plasma-membrane localization is well supported by other annotations in this review, e.g. PMID:33705718 and PMID:35917925.)
GO:0009505 plant-type cell wall
IDA
PMID:18539115
Differential expression of WOX genes mediates apical-basal a...
MARK AS OVER ANNOTATED
Summary: PIN1 is an integral ten-pass plasma-membrane protein; assignment to the plant-type cell wall is not biologically meaningful for an auxin efflux carrier and likely reflects PM or apoplast-adjacent signal.
Reason: Inconsistent with PIN1 being an integral membrane transporter; the cell wall is not a functional compartment for PIN1.
Supporting Evidence:
PMID:35917925
The transmembrane domain of PIN1 has ten transmembrane segments (TM1 to TM10), with both N and C termini located extracellularly
GO:0048825 cotyledon development
IGI
PMID:15371311
PIN-FORMED1 and PINOID regulate boundary formation and cotyl...
KEEP AS NON CORE
Summary: PIN1 acts with PINOID to regulate boundary formation and cotyledon development during embryogenesis, via patterning of auxin distribution.
Reason: Downstream developmental output of PIN1 auxin transport; pleiotropic, non-core.
Supporting Evidence:
PMID:15371311
Single mutations in the PIN-FORMED1 (PIN1) and PINOID (PID) genes, which mediate auxin-dependent organ formation, moderately disrupt the symmetric patterning of cotyledons
GO:0009908 flower development
IMP
PMID:20407025
Phosphorylation of conserved PIN motifs directs Arabidopsis ...
KEEP AS NON CORE
Summary: PIN1-dependent polar auxin transport is required for flower formation at the shoot apex; defective PIN1 phosphorylation causes inflorescence and flower defects. pin1 mutants form pin-shaped naked inflorescences lacking flowers.
Reason: Downstream developmental process patterned by PIN1 auxin transport; pleiotropic, non-core.
Supporting Evidence:
PMID:20407025
Loss-of-phosphorylation PIN1:green fluorescent protein (GFP) (Ser to Ala) induced inflorescence defects
GO:0010229 inflorescence development
IMP
PMID:20407025
Phosphorylation of conserved PIN motifs directs Arabidopsis ...
KEEP AS NON CORE
Summary: PIN1 is required for normal inflorescence development; the defining pin1 phenotype is a naked, pin-shaped inflorescence resulting from failed organ initiation at the shoot apex.
Reason: Downstream developmental output of PIN1 polar auxin transport; non-core.
Supporting Evidence:
PMID:20407025
Loss-of-phosphorylation PIN1:green fluorescent protein (GFP) (Ser to Ala) induced inflorescence defects
file:ARATH/PIN1/PIN1-deep-research-falcon.md
pin1 mutants exhibit severe organ initiation failures, producing β€œpin-like” stems with reduced or absent flowers/organs, supporting a causal link between PIN1-mediated PAT and organogenesis.
GO:0048826 cotyledon morphogenesis
IMP
PMID:20407025
Phosphorylation of conserved PIN motifs directs Arabidopsis ...
KEEP AS NON CORE
Summary: PIN1-mediated auxin transport during embryogenesis shapes cotyledon formation; phosphorylation-deficient PIN1 produces embryo and cotyledon defects.
Reason: Downstream developmental output of PIN1 auxin transport; non-core.
Supporting Evidence:
PMID:20407025
induced internalization of PIN1:GFP during embryogenesis, leading to strong embryo defects
GO:0010358 leaf shaping
IMP
PMID:16971475
ASYMMETRIC LEAVES1 and auxin activities converge to repress ...
UNDECIDED
Summary: This annotation cites PMID:16971475 for a PIN1 role in leaf shaping, but that paper concerns AS1/KNOX (BREVIPEDICELLUS) interactions with auxin gradients in leaf development and does not mention PIN1 specifically.
Reason: The cited publication (PMID:16971475) does not mention PIN1 in its available text; it addresses ASYMMETRIC LEAVES1/KNOX and generic auxin gradients in leaf development, so it does not substantiate this PIN1 (IMP) GO:0010358 (leaf shaping) annotation. No verbatim PIN1-specific supporting passage could be extracted.
GO:0010051 xylem and phloem pattern formation
IMP
PMID:16943276
The HVE/CAND1 gene is required for the early patterning of l...
UNDECIDED
Summary: This annotation cites PMID:16943276 for a PIN1 role in xylem/phloem pattern formation, but that paper is about HVE/CAND1 and explicitly states its venation-patterning pathway does NOT involve PIN1, so the citation does not support a PIN1 function here. (PIN1-dependent auxin canalization in vascular patterning is a real concept but is not substantiated by this particular paper.)
Reason: The cited publication (PMID:16943276) does not substantiate a PIN1 role; it states the HVE/CAND1 venation-patterning pathway acts in a pathway that involves AXR1 'but not LOP1, PIN1, CVP1 or CVP2'. The citation therefore does not support this PIN1 (IMP) GO:0010051 annotation, and no supporting PIN1 passage exists in the text.
GO:0009630 gravitropism
IMP
PMID:16601150
PIN proteins perform a rate-limiting function in cellular au...
UNDECIDED
Summary: This annotation cites PMID:16601150 for a PIN1 role in gravitropism, but that paper establishes the rate-limiting auxin-efflux function of PINs in heterologous systems and does not address gravitropism or provide PIN1-specific gravitropic-phenotype evidence.
Reason: The cited publication (PMID:16601150) demonstrates that PINs catalyze rate-limiting cellular auxin efflux but does not mention gravitropism; it does not substantiate this PIN1 (IMP) GO:0009630 (gravitropism) annotation. No verbatim supporting passage linking PIN1 to gravitropism could be extracted.
GO:0009640 photomorphogenesis
TAS
PMID:16141452
Brassinosteroids stimulate plant tropisms through modulation...
UNDECIDED
Summary: This annotation cites PMID:16141452 for a PIN1 role in photomorphogenesis, but that paper examines brassinosteroid modulation of polar auxin transport and tropisms acting on the PIN2 protein; it does not provide PIN1-specific evidence for photomorphogenesis.
Reason: The cited publication (PMID:16141452) describes brassinosteroid effects on polar auxin transport and tropisms mediated at the protein level by PIN2 (PIN genes are only noted as transcriptionally regulated); it does not substantiate a specific PIN1 role in photomorphogenesis (GO:0009640). No verbatim PIN1-specific supporting passage could be extracted.
GO:0009925 basal plasma membrane
IDA
PMID:11959844
The Arabidopsis PILZ group genes encode tubulin-folding cofa...
KEEP AS NON CORE
Summary: PIN1 localizes to the basal plasma-membrane domain of vascular cells, the polar domain that directs basipetal (rootward) auxin flow. This basal polar domain is a defining feature of PIN1 in vascular tissue.
Reason: A real, functionally important polar PM subdomain; kept as non-core because apical-versus-basal polarity is tissue- and phosphorylation-dependent while plasma membrane is the core location.
Supporting Evidence:
PMID:9856939
the AtPIN1 protein was detected at the basal end of auxin transport-competent cells in vascular tissue
file:ARATH/PIN1/PIN1-deep-research-falcon.md
In vascular tissues and the root stele, PIN1 is frequently described as
GO:0009926 auxin polar transport
IMP
PMID:16601150
PIN proteins perform a rate-limiting function in cellular au...
ACCEPT
Summary: PIN proteins, including PIN1, perform the rate-limiting step of cellular auxin efflux that underlies directional polar auxin transport. This is a core biological process for PIN1.
Reason: Core biological process; PIN1 polarity dictates the direction of polar auxin transport.
Supporting Evidence:
PMID:16601150
PINs mediate auxin efflux from mammalian and yeast cells without needing additional plant-specific factors
PMID:9856939
Mutations affecting the PIN-FORMED (PIN1) gene diminish polar auxin transport in Arabidopsis thaliana inflorescence axes.
file:ARATH/PIN1/PIN1-deep-research-falcon.md
which determines the direction of auxin flow between neighboring cells.
GO:0045177 apical part of cell
IDA
PMID:16107478
The gene ENHANCER OF PINOID controls cotyledon development i...
KEEP AS NON CORE
Summary: PIN1 apical polar localization observed during cotyledon and embryo development. Correct but a broad anatomical parent of apical plasma membrane.
Reason: Consistent with PIN1 polar localization; generic relative to apical plasma membrane. Retained as non-core.
Supporting Evidence:
PMID:16107478
reversal of polarity of the PIN1 auxin transport facilitator in the apex is only occasional
GO:0048364 root development
IMP
PMID:9856939
Regulation of polar auxin transport by AtPIN1 in Arabidopsis...
KEEP AS NON CORE
Summary: PIN1-mediated polar auxin transport is required for normal root system development; pin1 mutants show broad organ-formation defects.
Reason: Downstream developmental output of PIN1 auxin transport; non-core.
Supporting Evidence:
PMID:9856939
abnormalities in the number, size, shape, and position of lateral organs
GO:0048367 shoot system development
IMP
PMID:11060241
PIN-FORMED 1 regulates cell fate at the periphery of the sho...
KEEP AS NON CORE
Summary: PIN1 regulates cell fate at the periphery of the shoot apical meristem, controlling organ initiation and overall shoot system development.
Reason: Downstream developmental output of PIN1 polar auxin transport; non-core.
Supporting Evidence:
PMID:11060241
Loss of function severely affects organ initiation, and pin1 mutants are characterised by an inflorescence meristem that does not initiate any flowers

Core Functions

Plasma-membrane auxin efflux transmembrane transporter that binds indolic auxins (notably IAA) in an intracellular pocket and exports them out of the cell; activity is enhanced by AGC-kinase (D6PK) phosphorylation and inhibited by NPA. PIN1 adopts a 10-TM NhaA fold and functions as a homodimer.

Supporting Evidence:
  • PMID:35917925
    These results show that PIN1 mediates active auxin efflux when expressed in HEK293F cells, and is further activated by D6PK. This PIN1-mediated auxin efflux is inhibited by NPA
  • PMID:35917925
    All interacting residues (V51, N112, N478 and I582) are highly conserved in PINs
  • file:ARATH/PIN1/PIN1-deep-research-falcon.md
    Arabidopsis PIN1 was solved in multiple inward-facing conformations (apo, IAA-bound, NPA-bound), revealing a conserved transporter fold and a defined intracellular binding pocket that coordinates IAA.

By localizing asymmetrically (apical or basal) within the plasma membrane, PIN1 sets the direction of intercellular (polar) auxin transport, performing the rate-limiting cellular efflux step that establishes the auxin gradients and maxima patterning plant development.

Supporting Evidence:
  • PMID:16601150
    PINs mediate auxin efflux from mammalian and yeast cells without needing additional plant-specific factors
  • PMID:9856939
    the AtPIN1 protein was detected at the basal end of auxin transport-competent cells in vascular tissue
  • file:ARATH/PIN1/PIN1-deep-research-falcon.md
    which determines the direction of auxin flow between neighboring cells.

Self-associates into a homodimer at the plasma membrane; the dimer (TM1/TM2/TM7 interface) is the assembled form observed in the cryo-EM structure.

Supporting Evidence:
  • PMID:35917925
    TM1, TM2 and TM7 constitute the dimer interface, which consists mainly of hydrophobic residues

References

Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
file:ARATH/PIN1/PIN1-deep-research-falcon.md
Falcon (Edison Scientific) deep research report for PIN1
PIN-FORMED 1 regulates cell fate at the periphery of the shoot apical meristem.
The Arabidopsis PILZ group genes encode tubulin-folding cofactor orthologs required for cell division but not cell growth.
PIN-FORMED1 and PINOID regulate boundary formation and cotyledon development in Arabidopsis embryogenesis.
High-throughput protein localization in Arabidopsis using Agrobacterium-mediated transient expression of GFP-ORF fusions.
The gene ENHANCER OF PINOID controls cotyledon development in the Arabidopsis embryo.
Brassinosteroids stimulate plant tropisms through modulation of polar auxin transport in Brassica and Arabidopsis.
PIN proteins perform a rate-limiting function in cellular auxin efflux.
The HVE/CAND1 gene is required for the early patterning of leaf venation in Arabidopsis.
ASYMMETRIC LEAVES1 and auxin activities converge to repress BREVIPEDICELLUS expression and promote leaf development in Arabidopsis.
Interactions among PIN-FORMED and P-glycoprotein auxin transporters in Arabidopsis.
Ubiquitin lysine 63 chain forming ligases regulate apical dominance in Arabidopsis.
Antagonistic regulation of PIN phosphorylation by PP2A and PINOID directs auxin flux.
Auxin transport inhibitors impair vesicle motility and actin cytoskeleton dynamics in diverse eukaryotes.
Differential expression of WOX genes mediates apical-basal axis formation in the Arabidopsis embryo.
Plasma membrane-associated SCAR complex subunits promote cortical F-actin accumulation and normal growth characteristics in Arabidopsis roots.
PIN phosphorylation is sufficient to mediate PIN polarity and direct auxin transport.
Phosphorylation of conserved PIN motifs directs Arabidopsis PIN1 polarity and auxin transport.
Differential auxin-transporting activities of PIN-FORMED proteins in Arabidopsis root hair cells.
Arabidopsis plasmodesmal proteome.
A PP6-type phosphatase holoenzyme directly regulates PIN phosphorylation and auxin efflux in Arabidopsis.
AGC kinases and MAB4/MEL proteins maintain PIN polarity by limiting lateral diffusion in plant cells.
Structural insights into auxin recognition and efflux by Arabidopsis PIN1.
SUE4, a novel PIN1-interacting membrane protein, regulates acropetal auxin transport in response to sulfur deficiency.
Endogenous auxin maintains embryonic cell identity and promotes somatic embryo development in Arabidopsis.
Mapping of the Classical Mutation rosette Highlights a Role for Calcium in Wound-Induced Rooting.
Regulation of polar auxin transport by AtPIN1 in Arabidopsis vascular tissue.

Deep Research

Falcon

(PIN1-deep-research-falcon.md)
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate. Falcon Edison Scientific Literature 29 citations 2 artifacts 2026-06-06T22:13:09.427150

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Research report: Functional annotation of Arabidopsis thaliana PIN1 (UniProt Q9C6B8, At1g73590)

0) Target verification (critical disambiguation)

The symbol PIN1 is highly ambiguous across biology; in animals it often denotes a prolyl isomerase. The present target is explicitly the Arabidopsis thaliana PIN-FORMED1 auxin transporter (auxin efflux carrier component 1). The 2022 cryo-EM structural/biochemical study of A. thaliana PIN1 explicitly references UniProt accession Q9C6B8, and demonstrates PIN1-mediated auxin (IAA) efflux and inhibitor (NPA) binding, matching the UniProt record provided. (yang2022structuralinsightsinto pages 1-2, yang2022structuralinsightsinto pages 4-5)

1) Key concepts and definitions (current understanding)

1.1 PIN1 as a canonical PIN auxin exporter

PIN1 is a canonical (long-loop) PIN-FORMED auxin efflux carrier that exports auxin from the cytosol toward the apoplast, thereby enabling polar auxin transport (PAT)β€”directional, cell-to-cell auxin movement that organizes plant development. Canonical long PINs (including PIN1) are predominantly plasma-membrane localized and can exhibit strongly asymmetric (polar) distribution across distinct plasma-membrane domains, which determines the direction of auxin flow between neighboring cells. (yang2022structuralinsightsinto pages 1-2, luschnig2024over25years pages 2-3)

1.2 Chemiosmotic framework for auxin movement

A widely used conceptual model is the chemiosmotic hypothesis: the apoplast is moderately acidic (~pH 5.5) while the cytosol is near neutral (~pH 7.0), favoring diffusion of protonated IAAH into the cell and trapping auxin as IAAβˆ’ in the cytosol. Export of the anionic form (IAAβˆ’) then requires efflux carriers (notably PINs), and PIN polar localization defines where IAAβˆ’ exits, shaping tissue-scale auxin gradients and maxima. (luschnig2024over25years pages 2-3)

1.3 Molecular function (substrate)

Structural and biochemical evidence directly supports indole-3-acetic acid (IAA) as a direct ligand/substrate for PIN1. PIN1 contains an intracellular binding pocket that coordinates IAA through hydrophobic and hydrogen-bond interactions; this provides a molecular definition of PIN1’s substrate recognition. (yang2022structuralinsightsinto pages 1-2, yang2022structuralinsightsinto pages 4-5)

2) Molecular mechanism and quantitative biochemical evidence

2.1 Cryo-EM structures and binding pocket chemistry

Arabidopsis PIN1 was solved in multiple inward-facing conformations (apo, IAA-bound, NPA-bound), revealing a conserved transporter fold and a defined intracellular binding pocket that coordinates IAA. (yang2022structuralinsightsinto pages 1-2)

A key quantitative result is ligand binding affinity measured by ITC at pH 7.0:
- IAA–PIN1 Kd = 83 Β± 10 ΞΌM
- NPA–PIN1 Kd = 0.15 Β± 0.08 ΞΌM
Thus, the inhibitor NPA binds several hundred-fold more tightly than IAA and competes for the same binding pocket. (yang2022structuralinsightsinto pages 4-4, yang2022structuralinsightsinto media 2cf96299)

Mutational analyses identify residues critical for recognition/transport: for example, mutations in pocket-coordinating residues can prevent IAA binding, markedly increase cellular [3H]IAA retention, and decrease net efflux (e.g., effects reported for variants including N112A/I582A and transport-impairing mutants such as R547A/Q580A). (yang2022structuralinsightsinto pages 4-5, yang2022structuralinsightsinto pages 4-4)

2.2 Transport model and energetics (current consensus and open questions)

Across PIN-family structural studies, an elevator-like alternating-access mechanism is supported, with conformational transitions moving the substrate-binding site from the cytosolic side toward the non-cytosolic side. (ung2022structuresandmechanism pages 1-2, ung2022structuresandmechanism pages 4-5)

Energetically, available biochemical systems support transport that is largely independent of classical proton/ion gradients:
- In the PIN1 study, relative [3H]IAA retention did not differ significantly between pH 5.5 and 6.5 in the referenced assay, suggesting no strong pH-gradient dependence under those conditions. (yang2022structuralinsightsinto pages 4-5)
- For a related PIN structure/function dataset, activity was reported as minimally pH dependent and consistent with a uniport-like mechanism. (ung2022structuresandmechanism pages 4-5, ung2022structuresandmechanism pages 1-2)

However, expert synthesis emphasizes that the energy source for PIN1-mediated transport in vivo remains unresolved, and mechanistic coupling could be context-dependent in planta. (yang2022structuralinsightsinto pages 4-5)

3) Subcellular localization and where PIN1 acts

3.1 Plasma membrane polarity as a functional determinant

PIN1 is a plasma-membrane localized auxin exporter whose polar distribution is central to its function. In vascular tissues and the root stele, PIN1 is frequently described as basally localized, aligning with directional auxin transport routes and supporting tissue-scale patterning. (luschnig2024over25years pages 4-5, luschnig2024over25years pages 2-3)

3.2 Expression/tissue context

PIN1 is described as broadly important in embryos, apical meristems, vascular tissues, and developing organs. Loss of function leads to characteristic organ initiation defects (notably naked β€œpin-like” inflorescences), consistent with PIN1’s role in generating auxin maxima that specify sites of organogenesis. (yang2022structuralinsightsinto pages 1-2, reiter2025ovuledefectsin pages 12-15)

4) Biological processes and pathway context (PIN1-centered)

4.1 Organ initiation and phyllotactic patterning

PIN1’s polar transport contributes to local auxin maxima that specify where new organs initiate in shoots/flowers. pin1 mutants exhibit severe organ initiation failures, producing β€œpin-like” stems with reduced or absent flowers/organs, supporting a causal link between PIN1-mediated PAT and organogenesis. (reiter2025ovuledefectsin pages 12-15, reiter2025ovuledefectsin pages 15-19)

A 2024 quantitative modeling + experimental study links robustness of primordium initiation to PIN1 repolarization dynamics: the model explains phenotypes via CUC1-mediated effects on PIN1 repolarization, connecting PIN1 polarization kinetics to the number/position of auxin maxima in developing floral buds. (kong2024tradeoffbetweenspeed pages 9-10)

4.2 Vascular patterning and canalization

Expert synthesis identifies PIN1 as a major contributor to vascular tissue patterning and auxin β€œcanalization”-like processes underlying vein formation, consistent with long-standing conceptual models where directed auxin efflux reinforces provascular strands. (luschnig2024over25years pages 8-9, luschnig2024over25years pages 2-3)

4.3 Reproductive development (gynoecium/ovules)

PIN1-mediated PAT is implicated in gynoecium patterning, carpel/ovule initiation, and megagametogenesis, supported by observed PIN1 localization in developing ovule-related tissues and by phenotypes induced through pharmacological manipulation of PAT. In particular, application of the auxin transport inhibitor NPA can shift auxin gradients and produce morphological alterations in gynoecial tissues (e.g., style/stigma changes and altered carpel valve formation), connecting auxin efflux modulation to reproductive morphology and (indirectly) seed-setting capacity. (reiter2025ovuledefectsin pages 35-38)

5) Regulation of PIN1 activity, polarity, abundance, and trafficking

5.1 Phosphorylation and kinase control (expert consensus)

PIN1 function is regulated by phosphorylation in its long cytosolic loop, with different kinase modules tuning either polarity sorting or transport activity. A key experimentally supported example is that D6PK activates PIN1 in heterologous [3H]IAA efflux assays, indicating that kinase co-expression can increase functional efflux. (yang2022structuralinsightsinto pages 1-2)

High-level expert synthesis (2024) further describes how AGCVIII kinases (e.g., PID/WAG, D6PK, and context-specific modules) modulate PIN polarity decisions and transport activity, while phosphatases act antagonistically to tune polarity states. (luschnig2024over25years pages 5-6, luschnig2024over25years pages 4-5)

5.2 Trafficking, recycling, and turnover

PIN1 polarity is maintained by endocytosis and recycling; ARF-GEF–dependent recycling (notably GNOM) is described as important for maintaining basal targeting of PINs. (luschnig2024over25years pages 4-5)

Ubiquitin-linked vacuolar targeting is also emphasized as a mechanism regulating PIN abundance (e.g., reversible K63-linked polyubiquitination promoting vacuolar turnover), integrating signaling with transporter lifetime at the plasma membrane. (luschnig2024over25years pages 5-6)

5.3 Recent developments (prioritized 2023–2024)

(i) 2023: Phosphoinositide–peptide signaling hub controlling PIN1 patterns in protophloem
A 2023 Nature Communications study connected CLE45 peptide signaling (BAM3 receptor), RLCK-VII/PBL kinases, and phosphoinositide 5-kinases (PIP5K) to regulation of auxin efflux through dynamic control of PIN patterning/abundance in developing protophloem sieve elements. Quantitative imaging analyses were performed at substantial scale (e.g., n = 19–51 roots, 210–540 PPSEs per genotype, with p < 0.0001 for reported comparisons), supporting the conclusion that these signaling/ lipid modules converge on local PIN control. (wang2023aphosphoinositidehub pages 7-8, wang2023aphosphoinositidehub pages 1-2)

(ii) 2024: ENHANCER OF PINOID (ENP) as a PIN1-supporting/recruiting factor
A 2024 preprint provides evidence that ENP contains separable domains for its own polarization versus supporting PIN1 function, with an intrinsically disordered region that interacts with PIN cytosolic regions (via FLIM-FRET evidence) and is required to support PIN1 activity/recruitment at apical plasma-membrane domains; genetic interactions (enp pid) suggest PID-independent inputs into PIN1 functional polarity. (matthes2024separatedomainsof pages 1-6)

(iii) 2024: Field-level synthesis of PIN biology
A 2024 Nature Communications review summarizes β€œ25 years” of progress and frames PIN1 as a master regulator whose activity emerges from coordinated control of expression, phosphorylation, trafficking, clustering, and degradation, integrating environmental and endogenous signals into developmental patterning. (luschnig2024over25years pages 1-2, luschnig2024over25years pages 5-6)

6) Current applications and real-world implementations

6.1 Chemical perturbation of PIN1/PAT (NPA as a tool and prototype)

The auxin transport inhibitor NPA is widely used experimentally to manipulate PAT; authoritative synthesis notes that NPA treatment of wild-type plants can phenocopy pin1 developmental defects, making it a practical tool to functionally interrogate PIN1-mediated transport. (luschnig2024over25years pages 1-2)

At the molecular level, the resolved PIN1 binding pocket and the quantitative affinity gap between IAA and NPA (Kd 83 ΞΌM vs 0.15 ΞΌM) provide a rationale for NPA’s potency and a framework for designing/optimizing transport modulators. (yang2022structuralinsightsinto pages 4-4, yang2022structuralinsightsinto media 2cf96299)

6.2 Reporter- and imaging-based implementation

A 2023 study deployed PIN1-GFP (and multiple CITRINE-tagged pathway components) as quantitative reporters in vivo to track protein polarity/abundance dynamics in specific tissues (protophloem), exemplifying a real-world implementation pipeline for monitoring PIN1 behavior under genetic and peptide perturbations. (wang2023aphosphoinositidehub pages 1-2)

6.3 Structure-enabled engineering and screening paradigms

The PIN1 structure defines a concrete set of residues governing binding and efflux, and the authors explicitly position the structure as a framework for structure-based functional analysis and the design of auxin analogues/inhibitors relevant to agriculture. (yang2022structuralinsightsinto pages 4-5)

7) Expert opinions and analysis (authoritative synthesis)

Two high-authority Nature-family sources provide field-level consensus:
- The 2024 review emphasizes that PIN-mediated development arises from a regulated network of PIN expression, localization, and activity and that PIN1’s polar localization provides a plant-specific mechanism for directional distribution of the major coordinative signal auxin. (luschnig2024over25years pages 1-2, luschnig2024over25years pages 2-3)
- The 2022 structural work advances the field from phenomenological models toward a molecular mechanism by defining the IAA/NPA binding pocket and supporting an alternating-access model, while explicitly noting unresolved questions about energy coupling in vivo. (yang2022structuralinsightsinto pages 1-2, yang2022structuralinsightsinto pages 4-5)

8) Recent statistics and quantitative data highlights

Key quantitative/statistical datapoints from recent studies include:
- Ligand affinities (ITC, pH 7.0): IAA Kd = 83 Β± 10 ΞΌM; NPA Kd = 0.15 Β± 0.08 ΞΌM. (yang2022structuralinsightsinto pages 4-4, yang2022structuralinsightsinto media 2cf96299)
- Protophloem imaging quantification sample sizes: n = 19–51 roots and 210–540 PPSEs per genotype, with p < 0.0001 for reported comparisons of localization/abundance metrics in the CLE45–PIP5K–rheostat–PIN regulatory context. (wang2023aphosphoinositidehub pages 7-8)
- Structural resolutions/scale (cryo-EM): PIN1 structures captured at ~3.1–3.2 Γ… with hundreds of thousands of particles contributing to reconstructions across apo/IAA/NPA states. (yang2022structuralinsightsinto pages 6-7)

9) Summary table of key findings (with URLs and dates)

The following table consolidates the most important functional annotation points and recent developments:

Topic Key takeaways Key evidence Key recent sources URL
Definition Arabidopsis thaliana PIN1 (UniProt Q9C6B8; At1g73590) is the canonical long PIN-FORMED auxin exporter matching the UniProt description for an auxin efflux carrier, not the unrelated animal PIN1 prolyl isomerase. It is a plasma-membrane transporter central to polar auxin transport. (yang2022structuralinsightsinto pages 1-2, luschnig2024over25years pages 2-3, luschnig2024over25years pages 1-2) Nature structural work explicitly identifies Arabidopsis PIN1 with UniProt Q9C6B8 and shows PIN1-mediated auxin efflux in heterologous assays; reviews describe PIN1/2 as auxin exporters with 10 transmembrane helices and a long hydrophilic loop. Assays included cryo-EM and [3H]IAA efflux in HEK293F cells. (yang2022structuralinsightsinto pages 1-2, luschnig2024over25years pages 2-3) Luschnig & Friml, 2024 Nov; Yang et al., 2022 Aug https://doi.org/10.1038/s41467-024-54240-y ; https://doi.org/10.1038/s41586-022-05143-9
Primary function PIN1’s primary molecular function is auxin export, specifically transport of indole-3-acetic acid (IAA/IAAβˆ’) from the cytosol toward the apoplast to establish directional cell-to-cell auxin flow. Long PINs such as PIN1 are the major plasma-membrane auxin efflux carriers. (yang2022structuralinsightsinto pages 1-2, luschnig2024over25years pages 2-3, seifu2004ofthesisbiochemical pages 9-13) PIN1 is described as the β€œmain PIN auxin exporter” in Arabidopsis; in transport assays, loss or mutation of key residues increases cellular [3H]IAA retention and reduces net efflux. Chemiosmotic context: apoplast ~pH 5.5, cytosol ~pH 7.0, with IAAH diffusion inward and PIN-dependent IAAβˆ’ export outward. (yang2022structuralinsightsinto pages 4-5, luschnig2024over25years pages 2-3) Luschnig & Friml, 2024 Nov; Yang et al., 2022 Aug https://doi.org/10.1038/s41467-024-54240-y ; https://doi.org/10.1038/s41586-022-05143-9
Transport mechanism Structural studies support an elevator-like alternating-access mechanism for PIN-family auxin transporters, with PIN1 captured in inward-facing apo, IAA-bound, and NPA-bound states. NPA competitively occupies the same intracellular pocket as auxin and locks the transporter in an inward-open state. (yang2022structuralinsightsinto pages 4-5, luschnig2024over25years pages 2-3, ung2022structuresandmechanism pages 1-2) PIN1 cryo-EM structures were solved at ~3.1–3.2 Γ… for apo/IAA/NPA states; IAA binds an intracellular pocket coordinated by residues including V51, N112, N478, I582. For the related PIN8 family structure, transporter domains rotate ~20Β° and move the binding site ~5 Γ…, supporting the elevator model. (yang2022structuralinsightsinto pages 4-5, yang2022structuralinsightsinto pages 6-7, ung2022structuresandmechanism pages 3-4, ung2022structuresandmechanism pages 4-5) Luschnig & Friml, 2024 Nov; Yang et al., 2022 Aug; Ung et al., 2022 Jun https://doi.org/10.1038/s41467-024-54240-y ; https://doi.org/10.1038/s41586-022-05143-9 ; https://doi.org/10.1038/s41586-022-04883-y
Substrate specificity and inhibitor pharmacology PIN1 directly recognizes natural auxin IAA, while N-1-naphthylphthalamic acid (NPA) is a high-affinity competitive inhibitor of the same site. Current structural evidence supports IAA as the principal demonstrated substrate. (yang2022structuralinsightsinto pages 4-4, yang2022structuralinsightsinto pages 4-5, yang2022structuralinsightsinto media 2cf96299) ITC at pH 7.0: PIN1 binds IAA with Kd = 83 Β± 10 Β΅M and NPA with Kd = 0.15 Β± 0.08 Β΅M, showing several-hundred-fold tighter binding of NPA. V51A raised IAA Kd to 1.39 mM (~17-fold weaker than WT); N112A and I582A prevented IAA binding, and Y145A impaired both IAA transport and NPA inhibition. (yang2022structuralinsightsinto pages 4-4, yang2022structuralinsightsinto pages 4-5, yang2022structuralinsightsinto media 2cf96299) Yang et al., 2022 Aug https://doi.org/10.1038/s41586-022-05143-9
Energetics PIN-family transport appears largely independent of classical proton or ion gradients in available biochemical systems, although the in vivo energy source for PIN1 remains unresolved. Expert synthesis therefore favors a uniport-like mechanism but does not fully exclude context-dependent coupling in planta. (yang2022structuralinsightsinto pages 4-5, ung2022structuresandmechanism pages 4-5, ung2022structuresandmechanism pages 1-2) For PIN1, no significant difference in relative [3H]IAA retention was observed between pH 5.5 and 6.5 in the cited assay. For PIN8, activity was reported as minimally pH-dependent, insensitive to proton-motive-force decouplers, and retained in sodium- or potassium-exclusive buffers; authors concluded the data support a uniport mechanism. (yang2022structuralinsightsinto pages 4-5, ung2022structuresandmechanism pages 4-5, ung2022structuresandmechanism pages 1-2) Luschnig & Friml, 2024 Nov; Yang et al., 2022 Aug; Ung et al., 2022 Jun https://doi.org/10.1038/s41467-024-54240-y ; https://doi.org/10.1038/s41586-022-05143-9 ; https://doi.org/10.1038/s41586-022-04883-y
Localization PIN1 is a canonical long PIN predominantly localized asymmetrically at the plasma membrane, especially with basal polarity in vascular tissues and dynamic localization in shoot meristems and developing organs. Its polar localization determines auxin flow direction. (yang2022structuralinsightsinto pages 1-2, luschnig2024over25years pages 2-3, luschnig2024over25years pages 3-4) Reviews highlight basal PIN1 localization in stem vasculature matching known auxin transport routes; PIN1 is widely expressed in embryos, meristems, and vascular tissues. Long PINs localize to the PM and are dynamically regulated by endocytosis and recycling. (yang2022structuralinsightsinto pages 1-2, luschnig2024over25years pages 2-3) Luschnig & Friml, 2024 Nov; Yang et al., 2022 Aug https://doi.org/10.1038/s41467-024-54240-y ; https://doi.org/10.1038/s41586-022-05143-9
Regulation: phosphorylation and trafficking PIN1 polarity, abundance, and activity are tightly regulated by phosphorylation and membrane trafficking. PID/WAG kinases bias apical sorting/polarity, D6PK stimulates transport activity, GNOM-dependent trafficking maintains polar domains, and ubiquitin/vacuolar pathways tune turnover. (luschnig2024over25years pages 5-6, bilanovicovaUnknownyearfacultyofscience pages 21-24, luschnig2024over25years pages 3-4, yang2022structuralinsightsinto pages 1-2) PID/WAG target conserved hydrophilic-loop phosphosites and can shift PIN1 from basal to apical localization; pid mutants phenocopy pin1-like naked inflorescences. D6PK activates PIN1 in HEK293F [3H]IAA efflux assays. Brefeldin A-sensitive GNOM controls recycling; reversible K63-linked polyubiquitination promotes vacuolar targeting. (bilanovicovaUnknownyearfacultyofscience pages 21-24, luschnig2024over25years pages 5-6, yang2022structuralinsightsinto pages 1-2) Luschnig & Friml, 2024 Nov; Wang et al., 2023 Jan; Yang et al., 2022 Aug https://doi.org/10.1038/s41467-024-54240-y ; https://doi.org/10.1038/s41467-023-36200-0 ; https://doi.org/10.1038/s41586-022-05143-9
Recent regulation advances (2023-2024) Recent work links PIN1 control to phosphoinositide signaling, CLE peptide signaling, and ENHANCER OF PINOID (ENP), refining the view that PIN1 behavior is embedded in multiprotein polarity modules rather than controlled by phosphorylation alone. (wang2023aphosphoinositidehub pages 2-3, wang2023aphosphoinositidehub pages 1-2, wang2023aphosphoinositidehub pages 7-8, matthes2024separatedomainsof pages 1-6) In developing protophloem, CLE45-BAM3-PBL signaling antagonizes PIP5K-dependent phosphoinositide control of PAX/BRX rheostat polarity, thereby affecting PIN1 patterning; imaging quantification used n = 19–51 roots and 210–540 PPSEs per genotype, with p < 0.0001 in reported comparisons. ENP bioRxiv 2024 showed its IDR interacts with PINs and is required to recruit/support PIN1 at apical PM domains; enp pid double mutants lacked cotyledons and flowers. (wang2023aphosphoinositidehub pages 2-3, wang2023aphosphoinositidehub pages 7-8, matthes2024separatedomainsof pages 1-6) Wang et al., 2023 Jan 27; Matthes et al., 2024 Mar 11; Luschnig & Friml, 2024 Nov https://doi.org/10.1038/s41467-023-36200-0 ; https://doi.org/10.1101/2024.03.11.584374 ; https://doi.org/10.1038/s41467-024-54240-y
Developmental roles PIN1 is a master regulator of auxin-dependent patterning in embryogenesis, organ initiation, phyllotaxis, vascular formation/canalization, and reproductive development. Its developmental effects are best explained by its role in creating local auxin maxima and directional fluxes. (luschnig2024over25years pages 8-9, luschnig2024over25years pages 4-5, kong2024tradeoffbetweenspeed pages 9-10) pin1 loss-of-function mutants produce naked, pin-like inflorescences or sterile stems lacking normal flowers; pid mutants show a similar phenotype. Reviews and modeling connect PIN1 to organ initiation, lateral organ positioning, embryonic axis formation, vascular patterning, and female gametophyte development. (luschnig2024over25years pages 8-9, luschnig2024over25years pages 4-5, reiter2025ovuledefectsin pages 12-15, luschnig2024over25years pages 3-4) Kong et al., 2024 Jul; Luschnig & Friml, 2024 Nov https://doi.org/10.1038/s41467-024-50172-9 ; https://doi.org/10.1038/s41467-024-54240-y
Reproductive and ovule-associated roles PIN1-mediated auxin transport contributes to gynoecium, carpel, and ovule patterning, linking sporophytic auxin transport to seed-setting capacity. In these contexts, localization and transport inhibition studies support a spatial patterning role rather than a direct enzymatic one. (reiter2025ovuledefectsin pages 35-38) PIN1 localizes in ovule primordia, developing nucellus, and funiculus. NPA treatment altered carpel auxin gradients and caused increased stigma/style elongation, basalized style/ovary boundary, reduced ovary production, fewer carpel valves, and altered ovule initiation along the placenta. (reiter2025ovuledefectsin pages 35-38) Reiter, 2025; synthesized against 2024 review context N/A
Applications and real-world implementation Direct translational deployment of AtPIN1 itself was not demonstrated in the gathered Arabidopsis-specific sources, but the evidence supports PIN1 as a validated mechanistic target for engineering plant architecture through auxin transport control. Real-world implementation in this evidence base is strongest at the level of chemical inhibition (NPA) and developmental modeling/reporter systems. (yang2022structuralinsightsinto pages 4-5, kong2024tradeoffbetweenspeed pages 9-10, wang2023aphosphoinositidehub pages 2-3) Practical implementations in the gathered studies include use of NPA to manipulate auxin transport and morphology, pPIN1::PIN1-GFP reporter lines to monitor polarity, and quantitative image-based protophloem analyses with large sample sizes. Structural resolution of the IAA/NPA pocket provides a framework for future rational modulation of auxin transport. (reiter2025ovuledefectsin pages 35-38, kong2024tradeoffbetweenspeed pages 9-10, wang2023aphosphoinositidehub pages 2-3, yang2022structuralinsightsinto media 2cf96299) Wang et al., 2023 Jan 27; Kong et al., 2024 Jul 18; Luschnig & Friml, 2024 Nov; Yang et al., 2022 Aug https://doi.org/10.1038/s41467-023-36200-0 ; https://doi.org/10.1038/s41467-024-50172-9 ; https://doi.org/10.1038/s41467-024-54240-y ; https://doi.org/10.1038/s41586-022-05143-9

Table: This table summarizes the verified identity, function, mechanism, regulation, localization, developmental roles, and application-relevant findings for Arabidopsis thaliana PIN1 (Q9C6B8). It prioritizes 2023-2024 sources where available and includes quantitative evidence such as binding affinities, assay types, and sample sizes.

10) Figures supporting binding pocket and affinity claims

The structural binding pocket (IAA vs NPA) and ITC affinity plots were extracted from the PIN1 structural study figures; these directly support the quantitative claims above. (yang2022structuralinsightsinto media 2cf96299, yang2022structuralinsightsinto media 46dbabc4, yang2022structuralinsightsinto media eb31d734)

Key citations (with publication dates and URLs)

  • Yang Z. et al. Structural insights into auxin recognition and efflux by Arabidopsis PIN1. Nature (Aug 2022). https://doi.org/10.1038/s41586-022-05143-9 (yang2022structuralinsightsinto pages 1-2, yang2022structuralinsightsinto pages 4-4)
  • Wang Q. et al. A phosphoinositide hub connects CLE peptide signaling and polar auxin efflux regulation. Nature Communications (Jan 2023). https://doi.org/10.1038/s41467-023-36200-0 (wang2023aphosphoinositidehub pages 1-2, wang2023aphosphoinositidehub pages 7-8)
  • Kong S. et al. Tradeoff between speed and robustness in primordium initiation mediated by auxin-CUC1 interaction. Nature Communications (Jul 2024). https://doi.org/10.1038/s41467-024-50172-9 (kong2024tradeoffbetweenspeed pages 9-10)
  • Luschnig C., Friml J. Over 25 years of decrypting PIN-mediated plant development. Nature Communications (Nov 2024). https://doi.org/10.1038/s41467-024-54240-y (luschnig2024over25years pages 1-2, luschnig2024over25years pages 5-6)
  • Matthes M.S. et al. Separate domains of the Arabidopsis ENHANCER OF PINOID drive its own polarization and recruit PIN1 to the plasma membrane. bioRxiv (Mar 11, 2024). https://doi.org/10.1101/2024.03.11.584374 (matthes2024separatedomainsof pages 1-6)

References

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  8. (luschnig2024over25years pages 4-5): Christian Luschnig and JiΕ™Γ­ Friml. Over 25 years of decrypting pin-mediated plant development. Nature Communications, Nov 2024. URL: https://doi.org/10.1038/s41467-024-54240-y, doi:10.1038/s41467-024-54240-y. This article has 42 citations and is from a highest quality peer-reviewed journal.

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  10. (reiter2025ovuledefectsin pages 15-19): JW Reiter. Ovule defects in arabidopsis thaliana pin localization pathway mutants lead to reduced seed set. Unknown journal, 2025.

  11. (kong2024tradeoffbetweenspeed pages 9-10): Shuyao Kong, Mingyuan Zhu, David Pan, Brendan Lane, Richard S. Smith, and Adrienne H. K. Roeder. Tradeoff between speed and robustness in primordium initiation mediated by auxin-cuc1 interaction. Nature Communications, Jul 2024. URL: https://doi.org/10.1038/s41467-024-50172-9, doi:10.1038/s41467-024-50172-9. This article has 18 citations and is from a highest quality peer-reviewed journal.

  12. (luschnig2024over25years pages 8-9): Christian Luschnig and JiΕ™Γ­ Friml. Over 25 years of decrypting pin-mediated plant development. Nature Communications, Nov 2024. URL: https://doi.org/10.1038/s41467-024-54240-y, doi:10.1038/s41467-024-54240-y. This article has 42 citations and is from a highest quality peer-reviewed journal.

  13. (reiter2025ovuledefectsin pages 35-38): JW Reiter. Ovule defects in arabidopsis thaliana pin localization pathway mutants lead to reduced seed set. Unknown journal, 2025.

  14. (luschnig2024over25years pages 5-6): Christian Luschnig and JiΕ™Γ­ Friml. Over 25 years of decrypting pin-mediated plant development. Nature Communications, Nov 2024. URL: https://doi.org/10.1038/s41467-024-54240-y, doi:10.1038/s41467-024-54240-y. This article has 42 citations and is from a highest quality peer-reviewed journal.

  15. (wang2023aphosphoinositidehub pages 7-8): Qian Wang, A. Cecilia Aliaga Fandino, Moritz Graeff, Thomas A. DeFalco, Cyril Zipfel, and Christian S. Hardtke. A phosphoinositide hub connects cle peptide signaling and polar auxin efflux regulation. Nature Communications, Jan 2023. URL: https://doi.org/10.1038/s41467-023-36200-0, doi:10.1038/s41467-023-36200-0. This article has 25 citations and is from a highest quality peer-reviewed journal.

  16. (wang2023aphosphoinositidehub pages 1-2): Qian Wang, A. Cecilia Aliaga Fandino, Moritz Graeff, Thomas A. DeFalco, Cyril Zipfel, and Christian S. Hardtke. A phosphoinositide hub connects cle peptide signaling and polar auxin efflux regulation. Nature Communications, Jan 2023. URL: https://doi.org/10.1038/s41467-023-36200-0, doi:10.1038/s41467-023-36200-0. This article has 25 citations and is from a highest quality peer-reviewed journal.

  17. (matthes2024separatedomainsof pages 1-6): Michaela S. Matthes, Nicole Yun, Miriam Luichtl, Ulrich BΓΌschges, Birgit S. Fiesselmann, Benjamin Strickland, Marietta S. Lehnardt, and Ramon A. Torres Ruiz. Separate domains of the arabidopsis enhancer of pinoid drive its own polarization and recruit pin1 to the plasma membrane. bioRxiv, Mar 2024. URL: https://doi.org/10.1101/2024.03.11.584374, doi:10.1101/2024.03.11.584374. This article has 1 citations.

  18. (luschnig2024over25years pages 1-2): Christian Luschnig and JiΕ™Γ­ Friml. Over 25 years of decrypting pin-mediated plant development. Nature Communications, Nov 2024. URL: https://doi.org/10.1038/s41467-024-54240-y, doi:10.1038/s41467-024-54240-y. This article has 42 citations and is from a highest quality peer-reviewed journal.

  19. (yang2022structuralinsightsinto pages 6-7): Zhisen Yang, Jing Xia, Jingjing Hong, Chenxi Zhang, Hong Wei, Wei Ying, Chunqiao Sun, Lianghanxiao Sun, Yanbo Mao, Yongxiang Gao, Shutang Tan, JiΕ™Γ­ Friml, Dianfan Li, Xin Liu, and Linfeng Sun. Structural insights into auxin recognition and efflux by arabidopsis pin1. Nature, 609:611-615, Aug 2022. URL: https://doi.org/10.1038/s41586-022-05143-9, doi:10.1038/s41586-022-05143-9. This article has 148 citations and is from a highest quality peer-reviewed journal.

  20. (seifu2004ofthesisbiochemical pages 9-13): YW Seifu. Of thesis: biochemical and structural insights into pin-mediated auxin. Unknown journal, 2004.

  21. (ung2022structuresandmechanism pages 3-4): Kien Lam Ung, Mikael Winkler, Lukas Schulz, Martina Kolb, Dorina P. Janacek, Emil Dedic, David L. Stokes, Ulrich Z. Hammes, and BjΓΈrn Panyella Pedersen. Structures and mechanism of the plant pin-formed auxin transporter. Nature, 609:605-610, Jun 2022. URL: https://doi.org/10.1038/s41586-022-04883-y, doi:10.1038/s41586-022-04883-y. This article has 164 citations and is from a highest quality peer-reviewed journal.

  22. (luschnig2024over25years pages 3-4): Christian Luschnig and JiΕ™Γ­ Friml. Over 25 years of decrypting pin-mediated plant development. Nature Communications, Nov 2024. URL: https://doi.org/10.1038/s41467-024-54240-y, doi:10.1038/s41467-024-54240-y. This article has 42 citations and is from a highest quality peer-reviewed journal.

  23. (bilanovicovaUnknownyearfacultyofscience pages 21-24): V BilanovičovÑ. Faculty of science. Unknown journal, Unknown year.

  24. (wang2023aphosphoinositidehub pages 2-3): Qian Wang, A. Cecilia Aliaga Fandino, Moritz Graeff, Thomas A. DeFalco, Cyril Zipfel, and Christian S. Hardtke. A phosphoinositide hub connects cle peptide signaling and polar auxin efflux regulation. Nature Communications, Jan 2023. URL: https://doi.org/10.1038/s41467-023-36200-0, doi:10.1038/s41467-023-36200-0. This article has 25 citations and is from a highest quality peer-reviewed journal.

  25. (yang2022structuralinsightsinto media 46dbabc4): Zhisen Yang, Jing Xia, Jingjing Hong, Chenxi Zhang, Hong Wei, Wei Ying, Chunqiao Sun, Lianghanxiao Sun, Yanbo Mao, Yongxiang Gao, Shutang Tan, JiΕ™Γ­ Friml, Dianfan Li, Xin Liu, and Linfeng Sun. Structural insights into auxin recognition and efflux by arabidopsis pin1. Nature, 609:611-615, Aug 2022. URL: https://doi.org/10.1038/s41586-022-05143-9, doi:10.1038/s41586-022-05143-9. This article has 148 citations and is from a highest quality peer-reviewed journal.

  26. (yang2022structuralinsightsinto media eb31d734): Zhisen Yang, Jing Xia, Jingjing Hong, Chenxi Zhang, Hong Wei, Wei Ying, Chunqiao Sun, Lianghanxiao Sun, Yanbo Mao, Yongxiang Gao, Shutang Tan, JiΕ™Γ­ Friml, Dianfan Li, Xin Liu, and Linfeng Sun. Structural insights into auxin recognition and efflux by arabidopsis pin1. Nature, 609:611-615, Aug 2022. URL: https://doi.org/10.1038/s41586-022-05143-9, doi:10.1038/s41586-022-05143-9. This article has 148 citations and is from a highest quality peer-reviewed journal.

Artifacts

Citations

  1. yang2022structuralinsightsinto pages 1-2
  2. yang2022structuralinsightsinto pages 4-5
  3. kong2024tradeoffbetweenspeed pages 9-10
  4. reiter2025ovuledefectsin pages 35-38
  5. matthes2024separatedomainsof pages 1-6
  6. wang2023aphosphoinositidehub pages 1-2
  7. wang2023aphosphoinositidehub pages 7-8
  8. yang2022structuralinsightsinto pages 6-7
  9. yang2022structuralinsightsinto pages 4-4
  10. ung2022structuresandmechanism pages 1-2
  11. ung2022structuresandmechanism pages 4-5
  12. reiter2025ovuledefectsin pages 12-15
  13. reiter2025ovuledefectsin pages 15-19
  14. seifu2004ofthesisbiochemical pages 9-13
  15. ung2022structuresandmechanism pages 3-4
  16. wang2023aphosphoinositidehub pages 2-3
  17. 3H
  18. https://doi.org/10.1038/s41467-024-54240-y
  19. https://doi.org/10.1038/s41586-022-05143-9
  20. https://doi.org/10.1038/s41586-022-04883-y
  21. https://doi.org/10.1038/s41467-023-36200-0
  22. https://doi.org/10.1101/2024.03.11.584374
  23. https://doi.org/10.1038/s41467-024-50172-9
  24. https://doi.org/10.1038/s41586-022-05143-9,
  25. https://doi.org/10.1038/s41467-024-54240-y,
  26. https://doi.org/10.1038/s41586-022-04883-y,
  27. https://doi.org/10.1038/s41467-024-50172-9,
  28. https://doi.org/10.1038/s41467-023-36200-0,
  29. https://doi.org/10.1101/2024.03.11.584374,

πŸ“š Additional Documentation

Notes

(PIN1-notes.md)

PIN1 (PIN-FORMED 1, AtPIN1) β€” Arabidopsis thaliana β€” curation notes

UniProt: Q9C6B8 (PINI_ARATH); locus AT1G73590; TCDB 2.A.69.1.1 (auxin efflux carrier / AEC family).

Core identity and molecular function

PIN1 is a plasma-membrane, polytopic (10-TM) secondary transporter that mediates
cellular auxin efflux. Its polar (asymmetric) localization at the plasma membrane
sets the direction of intercellular (polar) auxin transport, generating the local auxin
gradients/maxima that drive organogenesis, vascular patterning, embryo axis formation
and phyllotaxis.

  • Founding identification as auxin efflux carrier component, basal localization in vascular
    cells, polar auxin transport: PMID:9856939. Disruption phenotype: naked, pin-shaped inflorescences.
  • Direct demonstration of active auxin efflux and structural mechanism: PIN1 expressed in
    HEK293F cells mediates active IAA efflux (enhanced by D6PK), inhibited by NPA
    PMID:35917925.
  • Substrate recognition: binds IAA (and IBA, IPA, 4-Cl-IAA) at an intracellular pocket;
    residues V51, N112, N478, I582 coordinate IAA PMID:35917925.
  • Fold: 10-TM NhaA fold, TM1–TM5 / TM6–TM10 inverted repeats; inward-facing conformation
    PMID:35917925.
  • Homodimer: cryo-EM shows a dimeric PIN1 (TM1, TM2, TM7 dimer interface)
    PMID:35917925. This supports the GOA
    IDA annotations GO:0042802 identical protein binding and GO:0042803 protein
    homodimerization activity.

So the appropriate, informative MF terms are:
- GO:0010329 auxin efflux transmembrane transporter activity (IDA + IMP) β€” ACCEPT, core.
- GO:0042803 protein homodimerization activity / GO:0042802 identical protein binding β€” ACCEPT (homodimer is structurally established), non-core.

Localization

  • Plasma membrane is the functional site (multiple IDA/EXP): PMID:9856939, PMID:20439545,
    PMID:33705718.
  • Polar PM domains: apical vs basal localization is phosphorylation-dependent
    PMID:20407025.
    Basal PM localization in vascular cells PMID:9856939. Apical/basal domains:
    GO:0016324 apical plasma membrane, GO:0009925 basal plasma membrane, GO:0045177 apical
    part of cell β€” all reflect the polar PM domain (cell periphery GO:0071944).
  • GO:0005737 cytoplasm (HDA, PMID:15610358): PIN1 cycles between PM and endosomal
    compartments via GNOM-dependent recycling (UniProt FUNCTION). Cytoplasmic/endosomal
    signal is real (trafficking intermediates) but not the functional compartment; keep as
    non-core.
  • GO:0009506 plasmodesma (HDA, PMID:21533090, proteomics): high-throughput proteome; PIN1
    is a PM protein and plasmodesmal PM is continuous with PM; weak/peripheral, keep non-core.
  • GO:0009505 plant-type cell wall (IDA, PMID:18539115): PIN1 is an integral membrane
    protein; cell-wall assignment is not biologically meaningful for an auxin efflux carrier
    and likely reflects PM/apoplast-adjacent signal; mark as over-annotated.
  • GO:0010168 ER body (IDA, PMID:36398993): PMID:36398993 is a tomato BIG/rosette paper
    about calcium and wound-induced rooting; it concerns ER localization of BIG, not PIN1
    ER-body localization. ER bodies are ER-derived structures found in Brassicaceae; there is
    no strong support that PIN1 is an ER-body resident. The long PINs (incl. PIN1) are PM
    proteins; only short PINs (PIN5/PIN8) are ER PMID:35917925. Treat ER body as a dubious annotation -> REMOVE/over-annotated. Marked UNDECIDED-leaning-REMOVE; chose MARK_AS_OVER_ANNOTATED conservatively is not appropriate since it appears to be a mis-assignment; chose REMOVE with rationale.

Regulation / interactors (the "protein binding" GO:0005515 IPI rows)

All GO:0005515 rows are uninformative bare "protein binding"; replace with specific
interactor context in reason, action MARK_AS_OVER_ANNOTATED (interaction is real but term
uninformative; per project guidance avoid bare protein binding as core).

  • PMID:17237354 WITH UniProtKB:Q9LJX0 = ABCB19/PGP19 β€” PIN–P-glycoprotein co-action in auxin transport.
  • PMID:17889649 / PMID:20080776 WITH O64682 = PID (PINOID kinase) β€” phosphorylates PIN1 HL, controls polarity.
  • PMID:33705718 WITH Q0WL52 = NPY5/MEL1 (MAB4/MEL family) β€” recruited to PM by PIN1, maintains polarity.
  • PMID:22715043 WITH Q9LHE7 (FYPP1) and Q9SX52 (FYPP3) β€” PP6 phosphatase, dephosphorylates PIN.
  • PMID:36226797 WITH AT3G55880 = SUE4 β€” PIN1-interacting membrane protein, acropetal transport under S deficiency.
  • PMID:17586653 WITH Q9LY87 β€” K63 ubiquitin ligase context (apical dominance).

UniProt SUBUNIT: "Homodimer. Interacts with TOPP4 ... Interacts with FYPP1 and FYPP3 ...
Component of a complex made of PINs, MAB4/MELs and AGC kinases at the plasma membrane.
Binds directly to NPY5/MEL1."

Biological processes (mostly IMP / acts_upstream_of_or_within)

Core BP:
- GO:0009926 auxin polar transport (IMP, PMID:16601150) β€” CORE.
- GO:0060918 auxin transport (IEA/IMP) β€” CORE (parent of polar transport).
- GO:0010315 auxin export across the plasma membrane (IDA, PMID:35917925) β€” CORE, most precise BP for the efflux event.
- GO:0055085 transmembrane transport (IEA) β€” accept as broad-but-correct parent.

Downstream developmental processes (pleiotropic; PIN1 acts upstream-of-or-within via auxin
gradients) β€” keep as non-core:
- GO:0009908 flower development; GO:0010229 inflorescence development (PMID:20407025; pin1 = pin-shaped naked inflorescence).
- GO:0048825 cotyledon development (IGI PMID:15371311); GO:0048826 cotyledon morphogenesis; GO:0009793 embryo development (PMID:20407025).
- GO:0010358 leaf shaping (PMID:16971475); GO:0010051 xylem and phloem pattern formation (PMID:16943276).
- GO:0009630 gravitropism (PMID:16601150); GO:0009640 photomorphogenesis (TAS PMID:16141452).
- GO:0048364 root development; GO:0048367 shoot system development (PMID:9856939/PMID:11060241).
- GO:0010262 somatic embryogenesis (IMP PMID:36345646); GO:0048830 adventitious root development (IMP PMID:36398993 β€” tomato ro/big paper; PIN1 accumulation Ca-sensitive). The adventitious-root annotation rests on an indirect tomato study; keep as non-core but flagged.

Deep research synthesis (Falcon / Edison Scientific, 2026-06-06)

The Falcon deep-research report (file:ARATH/PIN1/PIN1-deep-research-falcon.md) corroborates
the existing review and adds no contradicting evidence. Key points used to strengthen the
review:

  • Disambiguation: the target is the Arabidopsis PIN-FORMED1 auxin transporter (Q9C6B8,
    At1g73590), not the animal PIN1 prolyl isomerase; the 2022 cryo-EM study explicitly
    references Q9C6B8 ["demonstrates PIN1-mediated auxin (IAA) efflux and inhibitor (NPA)
    binding, matching the UniProt record provided"].
  • Core MF: PIN1 "exports auxin from the cytosol toward the apoplast" via "a defined
    intracellular binding pocket that coordinates IAA" (apo/IAA-bound/NPA-bound inward-facing
    states); IAA Kd = 83 Β± 10 Β΅M vs NPA Kd = 0.15 Β± 0.08 Β΅M (ITC, pH 7.0), NPA a competitive
    inhibitor of the same site. Supports GO:0010329 (auxin efflux transmembrane transporter
    activity) and GO:0010315 (auxin export across the PM).
  • Polar transport: polar PM distribution "determines the direction of auxin flow between
    neighboring cells"; PIN1 "frequently described as basally localized" in vascular tissue
    and root stele. Supports GO:0009926 (auxin polar transport) and GO:0009925 (basal PM).
  • Transport mechanism: elevator-like alternating-access; energetics consistent with a
    uniport-like mechanism, though the in vivo energy source remains unresolved (no GO change
    warranted).
  • Developmental output: "pin1 mutants exhibit severe organ initiation failures, producing
    'pin-like' stems with reduced or absent flowers/organs" β€” supports the non-core
    inflorescence/flower-development annotations.
  • Regulation context (2023–2024): D6PK activates PIN1 transport; PID/WAG bias apical sorting;
    GNOM-dependent recycling and K63-ubiquitin/vacuolar turnover; phosphoinositide/CLE-peptide
    hubs and ENHANCER OF PINOID modulate PIN1 patterning. These reinforce (but do not change)
    the MARK_AS_OVER_ANNOTATED decisions on the bare protein-binding (GO:0005515) interactor rows.

No UNDECIDED actions were present and none were created; no new GO term with a verifiable ID
emerged from the report (the regulatory/interactor findings remain best captured by specific
interactor context rather than bare protein binding, consistent with existing decisions).
Status remains DRAFT.

Summary of decisions

  • ACCEPT (core MF/BP/CC): auxin efflux transmembrane transporter activity (x2), auxin export across PM, auxin polar transport, auxin transport (x2), plasma membrane (multiple), transmembrane transport.
  • ACCEPT non-core / homodimer: identical protein binding, protein homodimerization activity.
  • KEEP_AS_NON_CORE: polar PM subdomains (apical/basal PM, apical part of cell, cell periphery), cytoplasm, plasmodesma, and all developmental BPs.
  • MARK_AS_OVER_ANNOTATED: bare protein binding rows; plant-type cell wall.
  • REMOVE: ER body (mis-assignment / wrong paper context).

PR #1417 review fix: bare-title supporting_text (2026-06-06)

Reviewer (ai4c-agent) flagged ~12 supporting_text entries that were merely the
publication TITLE rather than evidentiary excerpts. Each cited PMID was opened and
checked against the specific GO term claim.

Replaced title with a real verbatim quote (publication substantiates the claim):
- PMID:17237354 (GO:0005515, ABCB19/PGP19 interaction) β€” Y2H + coIP statement.
- PMID:20439545 (GO:0005886 plasma membrane) β€” "those PINs were localized in the plasma membrane...".
- PMID:36226797 (GO:0005515, SUE4 interaction) β€” "SUE4...interacts with the polar auxin transporter PIN1".
- PMID:22715043 (GO:0005515, FYPP1/3 interaction) β€” "FyPP1 and FyPP3 interact with a subset of PIN proteins...".
- PMID:17586653 (GO:0005515, RGLG2 interaction) β€” "RGLG2 and PIN1 can interact in the yeast two-hybrid system".
- PMID:15371311 (GO:0048825 cotyledon development) β€” pin1/pid disrupt cotyledon symmetry.
- PMID:16107478 (GO:0045177 apical part of cell) β€” PIN1 polarity in the apex.
- PMID:11060241 (GO:0048367 shoot system development) β€” pin1 organ-initiation/naked inflorescence.
- PMID:16601150 (GO:0009926 auxin polar transport, + same in core_functions[1]) β€” PINs mediate efflux in heterologous cells.
- PMID:36345646 (GO:0010262 somatic embryogenesis) β€” PIN-FORMED1 efflux drives PAT required for proembryo transition (full text).

Set to UNDECIDED (cited paper does NOT substantiate the claim / no usable PIN1-specific text):
- PMID:17889649 (GO:0005515, PID) β€” abstract reports PP2A/PINOID colocalization, not a PIN1-PID binding assay.
- PMID:20080776 (GO:0005515, PID) β€” states in vitro results do NOT support the site as a PID target; no PIN1-PID binding assay.
- PMID:15610358 (GO:0005737 cytoplasm) β€” generic GFP-fusion methods paper; no PIN1-specific localization.
- PMID:21533090 (GO:0009506 plasmodesma) β€” plasmodesmal proteome text does not mention PIN1 at all.
- PMID:18337510 (GO:0005886 plasma membrane) β€” ATI/actin/vesicle study; no PIN1 PM localization data in available text.
- PMID:19825598 (GO:0005886 plasma membrane) β€” about SCAR complex (BRK1/SCAR1) PM localization; PIN1 not mentioned.
- PMID:18539115 (GO:0005886 plasma membrane) β€” WOX2/WOX8 paper; PIN1 only as a reporter for auxin response, no PM localization.
- PMID:16971475 (GO:0010358 leaf shaping) β€” AS1/KNOX paper; PIN1 not mentioned.
- PMID:16943276 (GO:0010051 xylem/phloem patterning) β€” HVE/CAND1 paper explicitly states pathway involves "...but not...PIN1...".
- PMID:16141452 (GO:0009640 photomorphogenesis) β€” BR/PAT/tropism via PIN2 protein; no PIN1-specific photomorphogenesis evidence.
- PMID:16601150 (GO:0009630 gravitropism) β€” rate-limiting efflux paper; does not mention gravitropism.

Note: PIN1 plasma-membrane localization itself remains well supported by other rows
(PMID:33705718, PMID:35917925, PMID:20439545); the UNDECIDED PM rows reflect that those
particular citations don't substantiate localization, hence the validator's
"inconsistent review actions for GO:0005886" warning (expected/acceptable).
Status kept DRAFT; validation: βœ“ Valid.

πŸ“„ View Raw YAML

id: Q9C6B8
gene_symbol: PIN1
product_type: PROTEIN
status: DRAFT
taxon:
  id: NCBITaxon:3702
  label: Arabidopsis thaliana
description: PIN1 (PIN-FORMED 1, AtPIN1) is a plasma-membrane-localized, polytopic
  (ten-transmembrane) secondary transporter of the auxin efflux carrier (PIN/AEC,
  TC 2.A.69.1) family that mediates cellular efflux of the phytohormone auxin
  (indole-3-acetic acid and related indolic auxins). The transmembrane domain adopts
  a NhaA fold composed of two inverted five-helix repeats, with an intracellular
  substrate-binding pocket that coordinates IAA, and PIN1 assembles as a homodimer.
  Auxin efflux activity is enhanced by AGC-kinase (e.g. D6PK) phosphorylation and
  competitively inhibited by the synthetic inhibitor N-1-naphthylphthalamic acid
  (NPA). The defining feature of PIN1 is its polar (apical or basal) localization
  within the plasma membrane, which is established and maintained by reversible
  phosphorylation of its central hydrophilic loop (by PINOID/PID and related AGC
  kinases, counteracted by PP2A/PP6-type phosphatases) and by GNOM-dependent
  endosomal recycling, together with MAB4/MEL adaptor proteins that limit lateral
  diffusion. Because the orientation of PIN1 in the membrane dictates the direction
  of intercellular (polar) auxin flow, PIN1 generates the local auxin gradients and
  maxima that pattern plant development. It controls vascular tissue formation,
  embryonic apical-basal axis and cotyledon formation, leaf shaping and venation,
  shoot apical meristem organ initiation and phyllotaxis, inflorescence and flower
  formation, gravitropism and photomorphogenic growth. Loss of PIN1 produces naked,
  pin-shaped inflorescences and broad defects in lateral organ number, size, shape
  and position.
existing_annotations:
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: PIN1 is an integral plasma-membrane auxin efflux carrier; the plasma
      membrane is its functional location. This UniProt subcellular-location mapping
      is fully consistent with experimental evidence.
    action: ACCEPT
    reason: The plasma membrane is the bona fide functional compartment of PIN1,
      confirmed by multiple experimental studies; this is a core localization.
    supported_by:
    - reference_id: PMID:33705718
      supporting_text: PINs, MAB4/MELs, and AGC kinases interact in the same complex
        at the plasma membrane.
- term:
    id: GO:0016020
    label: membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: located_in
  review:
    summary: Generic membrane localization from InterPro mapping. PIN1 is a multi-pass
      membrane protein, so the term is correct but far less informative than the
      plasma-membrane annotation.
    action: KEEP_AS_NON_CORE
    reason: Correct but a broad parent of the more specific (and experimentally
      supported) plasma membrane term; retained as non-core background.
    supported_by:
    - reference_id: PMID:35917925
      supporting_text: The transmembrane domain of PIN1 has ten transmembrane segments
        (TM1 to TM10), with both N and C termini located extracellularly
- term:
    id: GO:0055085
    label: transmembrane transport
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: PIN1 mediates transmembrane transport of auxin across the plasma
      membrane. The term is correct but is a broad parent of the more specific
      auxin export and polar auxin transport terms.
    action: KEEP_AS_NON_CORE
    reason: Accurate but generic; the more precise auxin-transport terms capture the
      core function. Retained as a correct broad parent.
    supported_by:
    - reference_id: PMID:35917925
      supporting_text: These results show that PIN1 mediates active auxin efflux when
        expressed in HEK293F cells, and is further activated by D6PK.
- term:
    id: GO:0060918
    label: auxin transport
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  qualifier: involved_in
  review:
    summary: PIN1 is the founding auxin efflux carrier and a central mediator of
      auxin transport. This ARBA electronic annotation is well supported.
    action: ACCEPT
    reason: Core biological process; PIN1-mediated efflux is rate-limiting for
      cellular auxin transport.
    supported_by:
    - reference_id: PMID:9856939
      supporting_text: Mutations affecting the PIN-FORMED (PIN1) gene diminish polar
        auxin transport in Arabidopsis thaliana inflorescence axes.
    - reference_id: file:ARATH/PIN1/PIN1-deep-research-falcon.md
      supporting_text: demonstrates PIN1-mediated auxin (IAA) efflux and inhibitor
        (NPA) binding, matching the UniProt record provided.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:17237354
  qualifier: enables
  review:
    summary: IntAct interaction with ABCB19/PGP19 (Q9LJX0), a P-glycoprotein auxin
      transporter that co-acts with PIN1 in directional auxin transport. The bare
      protein binding term is uninformative about molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: The interaction with ABCB19 is real and biologically relevant to auxin
      transport, but GO:0005515 is too generic to convey function; per curation
      guidance bare protein binding is not retained as a core molecular function.
    supported_by:
    - reference_id: PMID:17237354
      supporting_text: Specific PGP–PIN interactions were seen in yeast two-hybrid
        and coimmunoprecipitation assays.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:17889649
  qualifier: enables
  review:
    summary: IntAct interaction with PINOID/PID (O64682), the AGC kinase that
      phosphorylates the PIN1 hydrophilic loop to control apical-basal polarity.
      The generic protein binding term is uninformative.
    action: UNDECIDED
    reason: The cited publication (PMID:17889649) is available only as an abstract
      that describes PP2A/PINOID colocalization with and antagonistic phosphorylation
      of PINs; it does not report a direct physical PIN1-PID binding assay, so it does
      not substantiate this GO:0005515 (protein binding) IPI annotation. No verbatim
      supporting passage for a PIN1-PID interaction could be extracted.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:20080776
  qualifier: enables
  review:
    summary: IntAct interaction with PID (O64682) in the context of phosphorylation
      directing PIN polarity. Generic protein binding term is uninformative.
    action: UNDECIDED
    reason: The cited publication (PMID:20080776) characterizes a conserved
      phosphorylation site that controls PIN polarity and explicitly reports that its
      in vitro results do NOT support this site being a PID target; it does not report
      a direct physical PIN1-PID binding assay and therefore does not substantiate this
      GO:0005515 (protein binding) IPI annotation. No verbatim supporting passage for a
      PIN1-PID interaction could be extracted.
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: EXP
  original_reference_id: PMID:20439545
  qualifier: located_in
  review:
    summary: Experimental localization of PIN1 to the plasma membrane in root hair
      cells, consistent with its function as a PM auxin efflux carrier.
    action: ACCEPT
    reason: Direct experimental support for the core plasma-membrane localization.
    supported_by:
    - reference_id: PMID:20439545
      supporting_text: those PINs were localized in the plasma membrane, where they
        likely export auxin to the apoplast
- term:
    id: GO:0042802
    label: identical protein binding
  evidence_type: IDA
  original_reference_id: PMID:35917925
  qualifier: enables
  review:
    summary: Cryo-EM shows PIN1 forms a homodimer with a TM1/TM2/TM7 dimer interface.
      Identical protein binding (self-association) is directly demonstrated.
    action: ACCEPT
    reason: Directly supported by the structure; a genuine, informative molecular
      property (self-interaction), retained as a non-core but real activity.
    supported_by:
    - reference_id: PMID:35917925
      supporting_text: we determined a dimeric structure of PIN1
- term:
    id: GO:0042803
    label: protein homodimerization activity
  evidence_type: IDA
  original_reference_id: PMID:35917925
  qualifier: enables
  review:
    summary: PIN1 assembles as a homodimer in the cryo-EM structure, with TM1, TM2
      and TM7 forming the dimer interface.
    action: ACCEPT
    reason: Structurally established homodimerization; an informative molecular
      function (more specific than identical protein binding).
    supported_by:
    - reference_id: PMID:35917925
      supporting_text: TM1, TM2 and TM7 constitute the dimer interface, which
        consists mainly of hydrophobic residues
- term:
    id: GO:0010315
    label: auxin export across the plasma membrane
  evidence_type: IDA
  original_reference_id: PMID:35917925
  qualifier: involved_in
  review:
    summary: PIN1 expressed in HEK293F cells mediates active IAA efflux across the
      plasma membrane (enhanced by D6PK, inhibited by NPA). This is the most precise
      biological-process term for the PIN1 efflux event.
    action: ACCEPT
    reason: Directly demonstrated auxin export across the PM; a core process.
    supported_by:
    - reference_id: PMID:35917925
      supporting_text: These results show that PIN1 mediates active auxin efflux when
        expressed in HEK293F cells, and is further activated by D6PK. This
        PIN1-mediated auxin efflux is inhibited by NPA
    - reference_id: file:ARATH/PIN1/PIN1-deep-research-falcon.md
      supporting_text: that exports auxin from the cytosol toward the apoplast, thereby
        enabling
- term:
    id: GO:0010329
    label: auxin efflux transmembrane transporter activity
  evidence_type: IDA
  original_reference_id: PMID:35917925
  qualifier: enables
  review:
    summary: Heterologous reconstitution plus cryo-EM with bound IAA establish PIN1
      as a direct auxin efflux transmembrane transporter; IAA is coordinated in an
      intracellular pocket by conserved residues (V51, N112, N478, I582) and mutation
      of these residues impairs efflux activity. This is the core molecular function.
    action: ACCEPT
    reason: Strongest, most informative MF annotation; directly supported by
      structure-function evidence.
    supported_by:
    - reference_id: PMID:35917925
      supporting_text: In the structure, IAA is coordinated through both hydrogen
        bonding and hydrophobic interactions
    - reference_id: PMID:35917925
      supporting_text: All interacting residues (V51, N112, N478 and I582) are highly
        conserved in PINs
    - reference_id: file:ARATH/PIN1/PIN1-deep-research-falcon.md
      supporting_text: Arabidopsis PIN1 was solved in multiple inward-facing conformations
        (apo, IAA-bound, NPA-bound), revealing a conserved transporter fold and a
        defined intracellular binding pocket that coordinates IAA.
    - reference_id: file:ARATH/PIN1/PIN1-deep-research-falcon.md
      supporting_text: this provides a molecular definition of PIN1’s substrate recognition.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:33705718
  qualifier: enables
  review:
    summary: IntAct/UniProt interaction with NPY5/MEL1 (Q0WL52), a MAB4/MEL adaptor
      recruited to the plasma membrane by PIN1 to maintain polarity. Generic protein
      binding term is uninformative.
    action: MARK_AS_OVER_ANNOTATED
    reason: The PIN1-NPY5/MEL1 interaction is mechanistically important for polarity
      maintenance, but GO:0005515 conveys no specific function.
    supported_by:
    - reference_id: PMID:33705718
      supporting_text: MAB4/MELs are recruited to the plasma membrane by the PINs
        and in concert with the AGC kinases maintain PIN polarity
- term:
    id: GO:0071944
    label: cell periphery
  evidence_type: IDA
  original_reference_id: PMID:33705718
  qualifier: located_in
  review:
    summary: PIN1 localizes to the cell periphery (plasma membrane and polar PM
      domains). Correct but a broad parent of the specific plasma-membrane term.
    action: KEEP_AS_NON_CORE
    reason: Accurate but generic relative to the plasma-membrane and polar-domain
      annotations; retained as non-core.
    supported_by:
    - reference_id: PMID:33705718
      supporting_text: the polar subcellular plasma membrane (PM) localization of the
        PIN-FORMED (PIN) auxin efflux carriers
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IDA
  original_reference_id: PMID:33705718
  qualifier: located_in
  review:
    summary: Direct experimental confirmation of PIN1 plasma-membrane localization
      within the PIN-MAB4/MEL-AGC kinase complex.
    action: ACCEPT
    reason: Core localization with direct experimental support.
    supported_by:
    - reference_id: PMID:33705718
      supporting_text: we demonstrate that PINs, MAB4/MELs, and AGC kinases interact
        in the same complex at the plasma membrane
- term:
    id: GO:0016324
    label: apical plasma membrane
  evidence_type: IDA
  original_reference_id: PMID:33705718
  qualifier: located_in
  review:
    summary: PIN1 occupies polar (apical or basal) plasma-membrane domains; apical
      localization is observed in specific tissues and is phosphorylation-dependent.
      This polar PM subdomain is central to PIN1 directional function.
    action: KEEP_AS_NON_CORE
    reason: A real and functionally important polar PM subdomain; kept as non-core
      because the polarity (apical versus basal) is tissue- and
      phosphorylation-dependent rather than a fixed property, while plasma membrane
      is the core location.
    supported_by:
    - reference_id: PMID:20407025
      supporting_text: The apical-basal polar localization of the PIN proteins that
        determines the direction of auxin flow is controlled by reversible
        phosphorylation of the PIN hydrophilic loop
- term:
    id: GO:0045177
    label: apical part of cell
  evidence_type: IDA
  original_reference_id: PMID:33705718
  qualifier: located_in
  review:
    summary: Reflects PIN1 apical polar localization. Correct but a broad cellular
      anatomical parent of apical plasma membrane.
    action: KEEP_AS_NON_CORE
    reason: Consistent with polar localization; generic relative to apical plasma
      membrane. Retained as non-core.
    supported_by:
    - reference_id: PMID:20407025
      supporting_text: >-
        Conversely, phosphomimic PIN1:GFP (Ser to Glu) showed apical localization in the shoot
        apex but did not rescue pin1 inflorescence defects.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:36226797
  qualifier: enables
  review:
    summary: TAIR interaction with SUE4 (AT3G55880), a PIN1-interacting membrane
      protein that regulates acropetal auxin transport under sulfur deficiency.
      Generic protein binding term is uninformative.
    action: MARK_AS_OVER_ANNOTATED
    reason: Biologically relevant interaction but GO:0005515 conveys no specific
      molecular function.
    supported_by:
    - reference_id: PMID:36226797
      supporting_text: SUE4, a novel plasma membrane-localized protein, interacts with
        the polar auxin transporter PIN1
- term:
    id: GO:0010168
    label: ER body
  evidence_type: IDA
  original_reference_id: PMID:36398993
  qualifier: located_in
  review:
    summary: This annotation assigns PIN1 to an ER body. PMID:36398993 is a study of
      the tomato classical mutation rosette mapping to the BIG/UBR4 ortholog and the
      role of calcium in wound-induced rooting; the ER association it reports is for
      BIG, not for PIN1. PIN1 is a long PIN that resides at the plasma membrane,
      whereas only the short PINs (PIN5/PIN8) are ER-localized. There is no sound
      evidence that PIN1 is an ER-body resident protein.
    action: REMOVE
    reason: Appears to be a mis-assignment; the cited paper does not support PIN1
      ER-body localization, and PIN1 is an established plasma-membrane protein.
    supported_by:
    - reference_id: PMID:35917925
      supporting_text: The short PINs are typically found at the endoplasmic
        reticulum, whereas the long PINs are at the plasma membrane and dynamically
        regulated by endocytosis and recycling
    - reference_id: PMID:36398993
      supporting_text: Subcellular localization of BIG suggests that, like its
        mammalian ortholog, it is associated with the endoplasmic reticulum.
- term:
    id: GO:0048830
    label: adventitious root development
  evidence_type: IMP
  original_reference_id: PMID:36398993
  qualifier: acts_upstream_of_or_within
  review:
    summary: PIN1-dependent auxin transport is implicated in wound-induced
      (adventitious) rooting; in the cited study PIN1 accumulation was sensitive to
      calcium levels in ro/big mutants, linking PIN1-mediated transport to
      wound-induced root formation. This is a downstream developmental output of
      auxin transport.
    action: KEEP_AS_NON_CORE
    reason: A pleiotropic downstream developmental process mediated via PIN1 auxin
      transport; evidence is indirect (a tomato BIG study). Retained as non-core.
    supported_by:
    - reference_id: PMID:36398993
      supporting_text: accumulation of the auxin transporter PIN-FORMED1 (PIN1) was
        sensitive to calcium levels in the ro/big mutants
- term:
    id: GO:0060918
    label: auxin transport
  evidence_type: IMP
  original_reference_id: PMID:36398993
  qualifier: involved_in
  review:
    summary: Genetic and physiological evidence that PIN1 contributes to auxin
      transport (reduced transport rates and NPA hypersensitivity in the relevant
      mutants). Consistent with PIN1 core role in auxin transport.
    action: ACCEPT
    reason: Core biological process, corroborated by the founding and structural
      studies.
    supported_by:
    - reference_id: PMID:36398993
      supporting_text: ro mutants were severely inhibited in formation of
        wound-induced roots (WiRs) and had reduced auxin transport rates.
- term:
    id: GO:0010262
    label: somatic embryogenesis
  evidence_type: IMP
  original_reference_id: PMID:36345646
  qualifier: acts_upstream_of_or_within
  review:
    summary: Endogenous auxin (transported by PINs including PIN1) maintains embryonic
      cell identity and promotes somatic embryo development. This is a downstream
      developmental process patterned by PIN1-generated auxin gradients.
    action: KEEP_AS_NON_CORE
    reason: Pleiotropic developmental output acting via auxin transport; non-core.
    supported_by:
    - reference_id: PMID:36345646
      supporting_text: polar auxin transport, with AUXIN/LIKE-AUX influx and
        PIN-FORMED1 efflux carriers as important drivers, is required for the
        transition of embryonic cells to proembryos
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: HDA
  original_reference_id: PMID:15610358
  qualifier: located_in
  review:
    summary: High-throughput GFP-fusion localization. PIN1 cycles between the plasma
      membrane and endosomal compartments via GNOM-dependent recycling, so a
      cytoplasmic/endosomal signal is expected for trafficking intermediates, but
      the plasma membrane is the functional site.
    action: UNDECIDED
    reason: The cited publication (PMID:15610358) is a generic high-throughput
      GFP-fusion localization methods paper; its available abstract does not mention
      PIN1 or report a cytoplasmic localization for PIN1 specifically, so it does not
      substantiate this GO:0005737 (cytoplasm) annotation. No verbatim PIN1-specific
      supporting passage could be extracted.
- term:
    id: GO:0009506
    label: plasmodesma
  evidence_type: HDA
  original_reference_id: PMID:21533090
  qualifier: located_in
  review:
    summary: PIN1 was detected in a plasmodesmal proteome. Plasmodesmal plasma
      membrane is continuous with the cell-surface PM, so detection here is plausible
      for a PM protein but does not indicate a distinct functional plasmodesmal role.
    action: UNDECIDED
    reason: The cited publication (PMID:21533090) is the Arabidopsis plasmodesmal
      proteome paper, but its cached text does not mention PIN1 anywhere, so it does
      not substantiate plasmodesmal detection of PIN1 for this GO:0009506 (plasmodesma)
      annotation. No verbatim PIN1-specific supporting passage could be extracted.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:22715043
  qualifier: enables
  review:
    summary: UniProt interactions with FYPP1 (Q9LHE7) and FYPP3 (Q9SX52), subunits
      of a PP6-type phosphatase holoenzyme that dephosphorylates PIN1 and regulates
      auxin efflux. Generic protein binding term is uninformative.
    action: MARK_AS_OVER_ANNOTATED
    reason: A real regulatory phosphatase interaction, but GO:0005515 conveys no
      specific molecular function.
    supported_by:
    - reference_id: PMID:22715043
      supporting_text: FyPP1 and FyPP3 interact with a subset of PIN proteins and
        regulate PIN protein phosphorylation and targeting in vivo
- term:
    id: GO:0010329
    label: auxin efflux transmembrane transporter activity
  evidence_type: IMP
  original_reference_id: PMID:9856939
  qualifier: enables
  review:
    summary: The founding study identified AtPIN1 as a transmembrane component of the
      auxin efflux carrier; pin1 mutants have diminished polar auxin transport. This
      mutant-phenotype evidence supports the core efflux transporter function.
    action: ACCEPT
    reason: Core molecular function, independently established here and later directly
      demonstrated structurally (PMID:35917925).
    supported_by:
    - reference_id: PMID:9856939
      supporting_text: AtPIN1 may act as a transmembrane component of the auxin
        efflux carrier.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:17586653
  qualifier: enables
  review:
    summary: UniProt interaction (Q9LY87) in the context of K63 ubiquitin chain
      ligases regulating apical dominance. Generic protein binding term is
      uninformative about molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: Interaction is recorded but GO:0005515 conveys no specific function.
    supported_by:
    - reference_id: PMID:17586653
      supporting_text: RGLG2 and PIN1 can interact in the yeast two-hybrid system
- term:
    id: GO:0009793
    label: embryo development ending in seed dormancy
  evidence_type: IMP
  original_reference_id: PMID:20407025
  qualifier: acts_upstream_of_or_within
  review:
    summary: Loss-of-phosphorylation PIN1 internalizes during embryogenesis causing
      strong embryo defects, demonstrating a PIN1 requirement in embryo development
      through proper polar auxin transport.
    action: KEEP_AS_NON_CORE
    reason: Important downstream developmental role mediated by PIN1 polar auxin
      transport; pleiotropic, non-core.
    supported_by:
    - reference_id: PMID:20407025
      supporting_text: induced internalization of PIN1:GFP during embryogenesis,
        leading to strong embryo defects
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IDA
  original_reference_id: PMID:18337510
  qualifier: located_in
  review:
    summary: This annotation cites PMID:18337510 for PIN1 plasma-membrane localization,
      but that paper studies how auxin transport inhibitors affect actin-dependent
      vesicle trafficking; its available text does not present PIN1-specific
      plasma-membrane localization data.
    action: UNDECIDED
    reason: The cited publication (PMID:18337510) does not substantiate PIN1
      plasma-membrane localization; its available abstract/discussion concern
      actin-stabilizing effects of auxin transport inhibitors on vesicle motility and
      do not localize PIN1 to the plasma membrane. No verbatim PIN1-specific supporting
      passage could be extracted. (PIN1 plasma-membrane localization remains well
      supported by other annotations here, e.g. PMID:33705718 and PMID:35917925.)
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IDA
  original_reference_id: PMID:19825598
  qualifier: located_in
  review:
    summary: This annotation cites PMID:19825598 for PIN1 plasma-membrane localization,
      but that paper concerns plasma-membrane localization of the SCAR complex subunits
      BRK1 and SCAR1 and cortical F-actin; its available text does not mention PIN1.
    action: UNDECIDED
    reason: The cited publication (PMID:19825598) does not mention PIN1; it reports
      plasma-membrane localization of SCAR complex subunits (BRK1, SCAR1), not PIN1, so
      it does not substantiate this GO:0005886 (plasma membrane) annotation. No verbatim
      PIN1-specific supporting passage could be extracted. (PIN1 plasma-membrane
      localization remains well supported by other annotations here, e.g. PMID:33705718
      and PMID:35917925.)
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IDA
  original_reference_id: PMID:18539115
  qualifier: located_in
  review:
    summary: This annotation cites PMID:18539115 for PIN1 plasma-membrane localization,
      but that paper is a study of WOX gene expression in apical-basal axis formation;
      its abstract mentions PIN1 only as a reporter gene for auxin response and provides
      no PIN1 plasma-membrane localization data.
    action: UNDECIDED
    reason: The cited publication (PMID:18539115) does not substantiate PIN1
      plasma-membrane localization; its available text concerns WOX2/WOX8 cell-fate
      regulators and references a PIN1 reporter only in the context of auxin response
      maxima. No verbatim passage localizing PIN1 to the plasma membrane could be
      extracted. (PIN1 plasma-membrane localization is well supported by other
      annotations in this review, e.g. PMID:33705718 and PMID:35917925.)
- term:
    id: GO:0009505
    label: plant-type cell wall
  evidence_type: IDA
  original_reference_id: PMID:18539115
  qualifier: located_in
  review:
    summary: PIN1 is an integral ten-pass plasma-membrane protein; assignment to the
      plant-type cell wall is not biologically meaningful for an auxin efflux carrier
      and likely reflects PM or apoplast-adjacent signal.
    action: MARK_AS_OVER_ANNOTATED
    reason: Inconsistent with PIN1 being an integral membrane transporter; the cell
      wall is not a functional compartment for PIN1.
    supported_by:
    - reference_id: PMID:35917925
      supporting_text: The transmembrane domain of PIN1 has ten transmembrane segments
        (TM1 to TM10), with both N and C termini located extracellularly
- term:
    id: GO:0048825
    label: cotyledon development
  evidence_type: IGI
  original_reference_id: PMID:15371311
  qualifier: involved_in
  review:
    summary: PIN1 acts with PINOID to regulate boundary formation and cotyledon
      development during embryogenesis, via patterning of auxin distribution.
    action: KEEP_AS_NON_CORE
    reason: Downstream developmental output of PIN1 auxin transport; pleiotropic,
      non-core.
    supported_by:
    - reference_id: PMID:15371311
      supporting_text: Single mutations in the PIN-FORMED1 (PIN1) and PINOID (PID)
        genes, which mediate auxin-dependent organ formation, moderately disrupt the
        symmetric patterning of cotyledons
- term:
    id: GO:0009908
    label: flower development
  evidence_type: IMP
  original_reference_id: PMID:20407025
  qualifier: acts_upstream_of_or_within
  review:
    summary: PIN1-dependent polar auxin transport is required for flower formation at
      the shoot apex; defective PIN1 phosphorylation causes inflorescence and flower
      defects. pin1 mutants form pin-shaped naked inflorescences lacking flowers.
    action: KEEP_AS_NON_CORE
    reason: Downstream developmental process patterned by PIN1 auxin transport;
      pleiotropic, non-core.
    supported_by:
    - reference_id: PMID:20407025
      supporting_text: Loss-of-phosphorylation PIN1:green fluorescent protein (GFP)
        (Ser to Ala) induced inflorescence defects
- term:
    id: GO:0010229
    label: inflorescence development
  evidence_type: IMP
  original_reference_id: PMID:20407025
  qualifier: acts_upstream_of_or_within
  review:
    summary: PIN1 is required for normal inflorescence development; the defining pin1
      phenotype is a naked, pin-shaped inflorescence resulting from failed organ
      initiation at the shoot apex.
    action: KEEP_AS_NON_CORE
    reason: Downstream developmental output of PIN1 polar auxin transport; non-core.
    supported_by:
    - reference_id: PMID:20407025
      supporting_text: Loss-of-phosphorylation PIN1:green fluorescent protein (GFP)
        (Ser to Ala) induced inflorescence defects
    - reference_id: file:ARATH/PIN1/PIN1-deep-research-falcon.md
      supporting_text: pin1 mutants exhibit severe organ initiation failures, producing
        β€œpin-like” stems with reduced or absent flowers/organs, supporting a causal
        link between PIN1-mediated PAT and organogenesis.
- term:
    id: GO:0048826
    label: cotyledon morphogenesis
  evidence_type: IMP
  original_reference_id: PMID:20407025
  qualifier: acts_upstream_of_or_within
  review:
    summary: PIN1-mediated auxin transport during embryogenesis shapes cotyledon
      formation; phosphorylation-deficient PIN1 produces embryo and cotyledon defects.
    action: KEEP_AS_NON_CORE
    reason: Downstream developmental output of PIN1 auxin transport; non-core.
    supported_by:
    - reference_id: PMID:20407025
      supporting_text: induced internalization of PIN1:GFP during embryogenesis,
        leading to strong embryo defects
- term:
    id: GO:0010358
    label: leaf shaping
  evidence_type: IMP
  original_reference_id: PMID:16971475
  qualifier: acts_upstream_of_or_within
  review:
    summary: This annotation cites PMID:16971475 for a PIN1 role in leaf shaping, but
      that paper concerns AS1/KNOX (BREVIPEDICELLUS) interactions with auxin gradients
      in leaf development and does not mention PIN1 specifically.
    action: UNDECIDED
    reason: The cited publication (PMID:16971475) does not mention PIN1 in its available
      text; it addresses ASYMMETRIC LEAVES1/KNOX and generic auxin gradients in leaf
      development, so it does not substantiate this PIN1 (IMP) GO:0010358 (leaf shaping)
      annotation. No verbatim PIN1-specific supporting passage could be extracted.
- term:
    id: GO:0010051
    label: xylem and phloem pattern formation
  evidence_type: IMP
  original_reference_id: PMID:16943276
  qualifier: acts_upstream_of_or_within
  review:
    summary: This annotation cites PMID:16943276 for a PIN1 role in xylem/phloem
      pattern formation, but that paper is about HVE/CAND1 and explicitly states its
      venation-patterning pathway does NOT involve PIN1, so the citation does not
      support a PIN1 function here. (PIN1-dependent auxin canalization in vascular
      patterning is a real concept but is not substantiated by this particular paper.)
    action: UNDECIDED
    reason: The cited publication (PMID:16943276) does not substantiate a PIN1 role; it
      states the HVE/CAND1 venation-patterning pathway acts in a pathway that involves
      AXR1 'but not LOP1, PIN1, CVP1 or CVP2'. The citation therefore does not support
      this PIN1 (IMP) GO:0010051 annotation, and no supporting PIN1 passage exists in
      the text.
- term:
    id: GO:0009630
    label: gravitropism
  evidence_type: IMP
  original_reference_id: PMID:16601150
  qualifier: acts_upstream_of_or_within
  review:
    summary: This annotation cites PMID:16601150 for a PIN1 role in gravitropism, but
      that paper establishes the rate-limiting auxin-efflux function of PINs in
      heterologous systems and does not address gravitropism or provide PIN1-specific
      gravitropic-phenotype evidence.
    action: UNDECIDED
    reason: The cited publication (PMID:16601150) demonstrates that PINs catalyze
      rate-limiting cellular auxin efflux but does not mention gravitropism; it does not
      substantiate this PIN1 (IMP) GO:0009630 (gravitropism) annotation. No verbatim
      supporting passage linking PIN1 to gravitropism could be extracted.
- term:
    id: GO:0009640
    label: photomorphogenesis
  evidence_type: TAS
  original_reference_id: PMID:16141452
  qualifier: acts_upstream_of_or_within
  review:
    summary: This annotation cites PMID:16141452 for a PIN1 role in photomorphogenesis,
      but that paper examines brassinosteroid modulation of polar auxin transport and
      tropisms acting on the PIN2 protein; it does not provide PIN1-specific evidence
      for photomorphogenesis.
    action: UNDECIDED
    reason: The cited publication (PMID:16141452) describes brassinosteroid effects on
      polar auxin transport and tropisms mediated at the protein level by PIN2 (PIN
      genes are only noted as transcriptionally regulated); it does not substantiate a
      specific PIN1 role in photomorphogenesis (GO:0009640). No verbatim PIN1-specific
      supporting passage could be extracted.
- term:
    id: GO:0009925
    label: basal plasma membrane
  evidence_type: IDA
  original_reference_id: PMID:11959844
  qualifier: located_in
  review:
    summary: PIN1 localizes to the basal plasma-membrane domain of vascular cells, the
      polar domain that directs basipetal (rootward) auxin flow. This basal polar
      domain is a defining feature of PIN1 in vascular tissue.
    action: KEEP_AS_NON_CORE
    reason: A real, functionally important polar PM subdomain; kept as non-core because
      apical-versus-basal polarity is tissue- and phosphorylation-dependent while
      plasma membrane is the core location.
    supported_by:
    - reference_id: PMID:9856939
      supporting_text: the AtPIN1 protein was detected at the basal end of auxin
        transport-competent cells in vascular tissue
    - reference_id: file:ARATH/PIN1/PIN1-deep-research-falcon.md
      supporting_text: In vascular tissues and the root stele, PIN1 is frequently
        described as
- term:
    id: GO:0009926
    label: auxin polar transport
  evidence_type: IMP
  original_reference_id: PMID:16601150
  qualifier: acts_upstream_of_or_within
  review:
    summary: PIN proteins, including PIN1, perform the rate-limiting step of cellular
      auxin efflux that underlies directional polar auxin transport. This is a core
      biological process for PIN1.
    action: ACCEPT
    reason: Core biological process; PIN1 polarity dictates the direction of polar
      auxin transport.
    supported_by:
    - reference_id: PMID:16601150
      supporting_text: PINs mediate auxin efflux from mammalian and yeast cells without
        needing additional plant-specific factors
    - reference_id: PMID:9856939
      supporting_text: Mutations affecting the PIN-FORMED (PIN1) gene diminish polar
        auxin transport in Arabidopsis thaliana inflorescence axes.
    - reference_id: file:ARATH/PIN1/PIN1-deep-research-falcon.md
      supporting_text: which determines the direction of auxin flow between neighboring
        cells.
- term:
    id: GO:0045177
    label: apical part of cell
  evidence_type: IDA
  original_reference_id: PMID:16107478
  qualifier: located_in
  review:
    summary: PIN1 apical polar localization observed during cotyledon and embryo
      development. Correct but a broad anatomical parent of apical plasma membrane.
    action: KEEP_AS_NON_CORE
    reason: Consistent with PIN1 polar localization; generic relative to apical plasma
      membrane. Retained as non-core.
    supported_by:
    - reference_id: PMID:16107478
      supporting_text: reversal of polarity of the PIN1 auxin transport facilitator in
        the apex is only occasional
- term:
    id: GO:0048364
    label: root development
  evidence_type: IMP
  original_reference_id: PMID:9856939
  qualifier: acts_upstream_of_or_within
  review:
    summary: PIN1-mediated polar auxin transport is required for normal root system
      development; pin1 mutants show broad organ-formation defects.
    action: KEEP_AS_NON_CORE
    reason: Downstream developmental output of PIN1 auxin transport; non-core.
    supported_by:
    - reference_id: PMID:9856939
      supporting_text: abnormalities in the number, size, shape, and position of
        lateral organs
      full_text_unavailable: true
- term:
    id: GO:0048367
    label: shoot system development
  evidence_type: IMP
  original_reference_id: PMID:11060241
  qualifier: acts_upstream_of_or_within
  review:
    summary: PIN1 regulates cell fate at the periphery of the shoot apical meristem,
      controlling organ initiation and overall shoot system development.
    action: KEEP_AS_NON_CORE
    reason: Downstream developmental output of PIN1 polar auxin transport; non-core.
    supported_by:
    - reference_id: PMID:11060241
      supporting_text: Loss of function severely affects organ initiation, and pin1
        mutants are characterised by an inflorescence meristem that does not initiate
        any flowers
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location
    vocabulary mapping, accompanied by conservative changes to GO terms applied by
    UniProt
  findings: []
- id: GO_REF:0000117
  title: Electronic Gene Ontology annotations created by ARBA machine learning models
  findings: []
- id: file:ARATH/PIN1/PIN1-deep-research-falcon.md
  title: Falcon (Edison Scientific) deep research report for PIN1
  findings: []
- id: PMID:11060241
  title: PIN-FORMED 1 regulates cell fate at the periphery of the shoot apical meristem.
  findings: []
- id: PMID:11959844
  title: The Arabidopsis PILZ group genes encode tubulin-folding cofactor orthologs
    required for cell division but not cell growth.
  findings: []
- id: PMID:15371311
  title: PIN-FORMED1 and PINOID regulate boundary formation and cotyledon development
    in Arabidopsis embryogenesis.
  findings: []
- id: PMID:15610358
  title: High-throughput protein localization in Arabidopsis using Agrobacterium-mediated
    transient expression of GFP-ORF fusions.
  findings: []
- id: PMID:16107478
  title: The gene ENHANCER OF PINOID controls cotyledon development in the Arabidopsis
    embryo.
  findings: []
- id: PMID:16141452
  title: Brassinosteroids stimulate plant tropisms through modulation of polar auxin
    transport in Brassica and Arabidopsis.
  findings: []
- id: PMID:16601150
  title: PIN proteins perform a rate-limiting function in cellular auxin efflux.
  findings: []
- id: PMID:16943276
  title: The HVE/CAND1 gene is required for the early patterning of leaf venation
    in Arabidopsis.
  findings: []
- id: PMID:16971475
  title: ASYMMETRIC LEAVES1 and auxin activities converge to repress BREVIPEDICELLUS
    expression and promote leaf development in Arabidopsis.
  findings: []
- id: PMID:17237354
  title: Interactions among PIN-FORMED and P-glycoprotein auxin transporters in Arabidopsis.
  findings: []
- id: PMID:17586653
  title: Ubiquitin lysine 63 chain forming ligases regulate apical dominance in Arabidopsis.
  findings: []
- id: PMID:17889649
  title: Antagonistic regulation of PIN phosphorylation by PP2A and PINOID directs
    auxin flux.
  findings: []
- id: PMID:18337510
  title: Auxin transport inhibitors impair vesicle motility and actin cytoskeleton
    dynamics in diverse eukaryotes.
  findings: []
- id: PMID:18539115
  title: Differential expression of WOX genes mediates apical-basal axis formation
    in the Arabidopsis embryo.
  findings: []
- id: PMID:19825598
  title: Plasma membrane-associated SCAR complex subunits promote cortical F-actin
    accumulation and normal growth characteristics in Arabidopsis roots.
  findings: []
- id: PMID:20080776
  title: PIN phosphorylation is sufficient to mediate PIN polarity and direct auxin
    transport.
  findings: []
- id: PMID:20407025
  title: Phosphorylation of conserved PIN motifs directs Arabidopsis PIN1 polarity
    and auxin transport.
  findings: []
- id: PMID:20439545
  title: Differential auxin-transporting activities of PIN-FORMED proteins in Arabidopsis
    root hair cells.
  findings: []
- id: PMID:21533090
  title: Arabidopsis plasmodesmal proteome.
  findings: []
- id: PMID:22715043
  title: A PP6-type phosphatase holoenzyme directly regulates PIN phosphorylation
    and auxin efflux in Arabidopsis.
  findings: []
- id: PMID:33705718
  title: AGC kinases and MAB4/MEL proteins maintain PIN polarity by limiting lateral
    diffusion in plant cells.
  findings: []
- id: PMID:35917925
  title: Structural insights into auxin recognition and efflux by Arabidopsis PIN1.
  findings: []
- id: PMID:36226797
  title: SUE4, a novel PIN1-interacting membrane protein, regulates acropetal auxin
    transport in response to sulfur deficiency.
  findings: []
- id: PMID:36345646
  title: Endogenous auxin maintains embryonic cell identity and promotes somatic embryo
    development in Arabidopsis.
  findings: []
- id: PMID:36398993
  title: Mapping of the Classical Mutation rosette Highlights a Role for Calcium in
    Wound-Induced Rooting.
  findings: []
- id: PMID:9856939
  title: Regulation of polar auxin transport by AtPIN1 in Arabidopsis vascular tissue.
  findings: []
core_functions:
- description: Plasma-membrane auxin efflux transmembrane transporter that binds
    indolic auxins (notably IAA) in an intracellular pocket and exports them out of
    the cell; activity is enhanced by AGC-kinase (D6PK) phosphorylation and inhibited
    by NPA. PIN1 adopts a 10-TM NhaA fold and functions as a homodimer.
  molecular_function:
    id: GO:0010329
    label: auxin efflux transmembrane transporter activity
  directly_involved_in:
  - id: GO:0010315
    label: auxin export across the plasma membrane
  locations:
  - id: GO:0005886
    label: plasma membrane
  supported_by:
  - reference_id: PMID:35917925
    supporting_text: These results show that PIN1 mediates active auxin efflux when
      expressed in HEK293F cells, and is further activated by D6PK. This
      PIN1-mediated auxin efflux is inhibited by NPA
  - reference_id: PMID:35917925
    supporting_text: All interacting residues (V51, N112, N478 and I582) are highly
      conserved in PINs
  - reference_id: file:ARATH/PIN1/PIN1-deep-research-falcon.md
    supporting_text: Arabidopsis PIN1 was solved in multiple inward-facing conformations
      (apo, IAA-bound, NPA-bound), revealing a conserved transporter fold and a
      defined intracellular binding pocket that coordinates IAA.
- description: By localizing asymmetrically (apical or basal) within the plasma
    membrane, PIN1 sets the direction of intercellular (polar) auxin transport,
    performing the rate-limiting cellular efflux step that establishes the auxin
    gradients and maxima patterning plant development.
  molecular_function:
    id: GO:0010329
    label: auxin efflux transmembrane transporter activity
  directly_involved_in:
  - id: GO:0009926
    label: auxin polar transport
  locations:
  - id: GO:0009925
    label: basal plasma membrane
  - id: GO:0016324
    label: apical plasma membrane
  supported_by:
  - reference_id: PMID:16601150
    supporting_text: PINs mediate auxin efflux from mammalian and yeast cells without
      needing additional plant-specific factors
  - reference_id: PMID:9856939
    supporting_text: the AtPIN1 protein was detected at the basal end of auxin
      transport-competent cells in vascular tissue
  - reference_id: file:ARATH/PIN1/PIN1-deep-research-falcon.md
    supporting_text: which determines the direction of auxin flow between neighboring
      cells.
- description: Self-associates into a homodimer at the plasma membrane; the dimer
    (TM1/TM2/TM7 interface) is the assembled form observed in the cryo-EM structure.
  molecular_function:
    id: GO:0042803
    label: protein homodimerization activity
  directly_involved_in:
  - id: GO:0010315
    label: auxin export across the plasma membrane
  locations:
  - id: GO:0005886
    label: plasma membrane
  supported_by:
  - reference_id: PMID:35917925
    supporting_text: TM1, TM2 and TM7 constitute the dimer interface, which consists
      mainly of hydrophobic residues