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
Falcon (Edison Scientific) deep research report for PIN1
PIN-FORMED 1 regulates cell fate at the periphery of the shoot apical meristem.
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PIN1 regulates cell fate at the periphery of the shoot apical meristem, controlling organ initiation and overall shoot system development.
"Loss of function severely affects organ initiation, and pin1 mutants are characterised by an inflorescence meristem that does not initiate any flowers"
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.
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PIN1 acts with PINOID to regulate boundary formation and cotyledon development during embryogenesis, via patterning of auxin distribution.
"Single mutations in the PIN-FORMED1 (PIN1) and PINOID (PID) genes, which mediate auxin-dependent organ formation, moderately disrupt the symmetric patterning of cotyledons"
High-throughput protein localization in Arabidopsis using Agrobacterium-mediated transient expression of GFP-ORF fusions.
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PIN1 has an intracellular trafficking pool in addition to its plasma-membrane transport pool.
"These patterns have been classified into five main categories, including cytoplasmic, nuclear, nucleolar, organellar and endomembrane compartments."
The gene ENHANCER OF PINOID controls cotyledon development in the Arabidopsis embryo.
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PIN1 apical polar localization observed during cotyledon and embryo development. Correct but a broad anatomical parent of apical plasma membrane.
"reversal of polarity of the PIN1 auxin transport facilitator in the apex is only occasional"
Brassinosteroids stimulate plant tropisms through modulation of polar auxin transport in Brassica and Arabidopsis.
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Traceable author statement: the paper states that PIN1 is required for basipetal auxin movement and is crucial for shoot vascular development, gravitropic responses and photomorphogenesis.
"the PIN-FORMED1 (PIN1) protein is required for basipetal auxin movement and crucial for shoot vascular development, gravitropic responses, and photomorphogenesis"
PIN proteins perform a rate-limiting function in cellular auxin efflux.
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Gravitropism IMP for PIN1 citing Petrasek et al. 2006. The cached abstract covers PIN-mediated rate-limiting auxin efflux in heterologous systems and cultured cells only; any gravitropism data would be in the full text, which is not cached.
"the action of PINs in auxin efflux is distinct from PGP, rate-limiting, specific to auxins, and sensitive to auxin transport inhibitors"
The HVE/CAND1 gene is required for the early patterning of leaf venation in Arabidopsis.
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Alonso-Peral et al. used double-mutant analysis including pin1 to place HVE/CAND1 in a venation pathway independent of PIN1; the IMP for PIN1 in xylem/phloem patterning presumably comes from the pin1 single-mutant venation phenotype reported in the full text. PIN1-dependent auxin canalization in vascular patterning is well established.
"Our analyses of double mutant and transgenic plants indicated that auxin transport and perception act independently to pattern leaf veins"
ASYMMETRIC LEAVES1 and auxin activities converge to repress BREVIPEDICELLUS expression and promote leaf development in Arabidopsis.
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Hay et al. showed that regulated auxin gradients control leaf shape independently of KNOX; the cached abstract does not name PIN1 but the full text (not cached) is where the pin1 mutant analysis would be. PIN1-generated convergence points are well known to pattern leaf serrations.
"We also demonstrate that regulated auxin gradients control leaf shape in a KNOX-independent fashion"
Interactions among PIN-FORMED and P-glycoprotein auxin transporters in Arabidopsis.
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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.
"Specific PGP–PIN interactions were seen in yeast two-hybrid and coimmunoprecipitation assays."
Ubiquitin lysine 63 chain forming ligases regulate apical dominance in Arabidopsis.
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UniProt interaction (Q9LY87) in the context of K63 ubiquitin chain ligases regulating apical dominance. Generic protein binding term is uninformative about molecular function.
"RGLG2 and PIN1 can interact in the yeast two-hybrid system"
Antagonistic regulation of PIN phosphorylation by PP2A and PINOID directs auxin flux.
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IntAct interaction of PIN1 with PINOID (PID, O64682), the AGC kinase that phosphorylates the PIN1 hydrophilic loop to control apical-basal polarity. The cached abstract reports colocalization and antagonistic PP2A/PID control of PIN loop phosphorylation; the binding assay itself is presumably in the full text.
"PP2A and PINOID both partially colocalize with PINs and act antagonistically on the phosphorylation state of their central hydrophilic loop"
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.
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IntAct interaction of PIN1 with PID (O64682) in the context of the conserved phosphorylation site that controls PIN polarity.
"The PIN polarity and the resulting auxin flow directionality are mediated by the antagonistic actions of PINOID kinase and protein phosphatase 2A."
Phosphorylation of conserved PIN motifs directs Arabidopsis PIN1 polarity and auxin transport.
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Reflects PIN1 apical polar localization. Correct but a broad cellular anatomical parent of apical plasma membrane.
"Conversely, phosphomimic PIN1:GFP (Ser to Glu) showed apical localization in the shoot apex but did not rescue pin1 inflorescence defects."
Differential auxin-transporting activities of PIN-FORMED proteins in Arabidopsis root hair cells.
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Experimental localization of PIN1 to the plasma membrane in root hair cells, consistent with its function as a PM auxin efflux carrier.
"those PINs were localized in the plasma membrane, where they likely export auxin to the apoplast"
Arabidopsis plasmodesmal proteome.
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PIN1 was assigned to the plasmodesmal proteome (identification presumably in supplementary tables, not in the cached main text). The plasmodesmal plasma membrane is continuous with the cell-surface PM, so co-purification of a PM transporter is plausible.
"Arabidopsis plasmodesmal proteome."
A PP6-type phosphatase holoenzyme directly regulates PIN phosphorylation and auxin efflux in Arabidopsis.
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UniProt interactions with FYPP1 and FYPP3, subunits of a PP6-type phosphatase holoenzyme that dephosphorylates PIN1 and regulates auxin efflux. Generic protein binding term is uninformative.
"FyPP1 and FyPP3 interact with a subset of PIN proteins and regulate PIN protein phosphorylation and targeting in vivo"
AGC kinases and MAB4/MEL proteins maintain PIN polarity by limiting lateral diffusion in plant cells.
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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.
"PINs, MAB4/MELs, and AGC kinases interact in the same complex at the plasma membrane."
Structural insights into auxin recognition and efflux by Arabidopsis PIN1.
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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.
"The transmembrane domain of PIN1 has ten transmembrane segments (TM1 to TM10), with both N and C termini located extracellularly"
SUE4, a novel PIN1-interacting membrane protein, regulates acropetal auxin transport in response to sulfur deficiency.
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TAIR interaction with SUE4 (AT3G55880), a PIN1-interacting membrane protein that regulates acropetal auxin transport under sulfur deficiency. Generic protein binding term is uninformative.
"SUE4, a novel plasma membrane-localized protein, interacts with the polar auxin transporter PIN1"
Endogenous auxin maintains embryonic cell identity and promotes somatic embryo development in Arabidopsis.
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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.
"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"
Mapping of the Classical Mutation rosette Highlights a Role for Calcium in Wound-Induced Rooting.
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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.
"ro mutants were severely inhibited in formation of wound-induced roots (WiRs) and had reduced auxin transport rates."
Regulation of polar auxin transport by AtPIN1 in Arabidopsis vascular tissue.
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PIN1 is the founding auxin efflux carrier and a central mediator of auxin transport. This ARBA electronic annotation is well supported.
"Mutations affecting the PIN-FORMED (PIN1) gene diminish polar auxin transport in Arabidopsis thaliana inflorescence axes."
https://oup.silverchair-cdn.com/article-minimal/6833154
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The ER-body imaging is of the BIG fragment, not PIN1.
"Confocal images of the C-terminal region of the BIG protein fused to the mScarlet-i (A)"
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Arabidopsis pin1-containing mutant combinations impair wound-induced rooting.
"pin1;2 mutants exhibiting a 32% reduction in rooting rates"
Target-specific inspection of plasmodesmata proteomics supplementary tables