TAS1R1

UniProt ID: A0A7L3NBT4
Organism: Oreotrochilus melanogaster
Review Status: DRAFT
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Gene Description

TAS1R1 (taste receptor type 1 member 1) is a class C ("family 3") G protein-coupled receptor with a large extracellular venus-flytrap (VFT) ligand-binding domain, a cysteine-rich linker region, and a seven- transmembrane signalling domain. Across most vertebrates TAS1R1 heterodimerizes obligately with TAS1R3 to form the umami taste receptor, which is expressed in type II taste-bud cells and detects L-amino acids (most notably glutamate), signalling through a heterotrimeric G protein/PLCbeta2/IP3/Ca2+/TRPM5 cascade. Birds generally lack the TAS1R2 subunit required for the canonical vertebrate sweet receptor. In hummingbirds (family Trochilidae), the ancestral TAS1R1-TAS1R3 umami receptor was repurposed after divergence from their insectivorous swift relatives to respond primarily to carbohydrates rather than amino acids, giving hummingbirds an alternate, T1R2-independent route to sweet taste perception that is thought to have supported their nectarivorous radiation. This UniProt entry (A0A7L3NBT4) is an unreviewed, fragmentary (572 aa, non-terminal at both ends) TAS1R1 sequence from a preliminary whole-genome-shotgun assembly of the black-breasted hillstar, Oreotrochilus melanogaster, produced by the Bird 10,000 Genomes (B10K) project. No experimental characterization exists for this exact species/accession; the functional picture here is inferred from domain architecture/orthology to TAS1R1 and from the well-documented, genus/family-wide sweet-taste repurposing phenomenon in hummingbirds, which was originally demonstrated in a different hummingbird species, Calypte anna (Anna's hummingbird).

Existing Annotations Review

GO Term Evidence Action Reason
GO:0004930 G protein-coupled receptor activity
IEA
GO_REF:0000120
ACCEPT
Summary: This fragment carries the canonical class C GPCR domain architecture (VFT/ANF ligand-binding region, 9-Cys linker, and a 7TM "GPCR family 3" domain with three predicted transmembrane helices), consistent with TAS1R1's established identity as a family C GPCR subunit.
Reason: The InterPro domain matches recorded on this record (ANF_lig-bd_rcpt, GPCR_3, GPCR_3_9-Cys_dom/sf, GPCR_3_C) and the UniProt-annotated 7TM "G-protein coupled receptors family 3 profile" domain (residues 438-533) with three transmembrane helices are diagnostic of a class C GPCR, and TAS1R1 orthologs are established GPCRs across vertebrates: "In vertebrates, sweet and savory... tastes are sensed by G protein-coupled receptors (GPCRs) termed T1Rs." GPCR-activity is family-architecture evidence, independent of whether this particular lineage's receptor detects sugars or amino acids, so the call is sound even though this exact accession/species has not been assayed directly.
Supporting Evidence:
PMID:25146290
sweet and savory
PMID:25146290
are sensed by G protein
file:9AVES/TAS1R1/TAS1R1-uniprot.txt
Belongs to the G protein-coupled receptor 3 family. TAS1R
GO:0005886 plasma membrane
IEA
GO_REF:0000120
ACCEPT
Summary: Class C GPCRs, including all characterized TAS1R subunits, are cell-surface receptors; this fragment retains three predicted transmembrane helices consistent with a multi-pass plasma-membrane protein.
Reason: UniProt's own subcellular-location call for this record ("Cell membrane... Multi-pass membrane protein") plus the three TRANSMEM features (440-464, 476-497, 509-532) support plasma-membrane localization. Heterologously expressed hummingbird T1R1-T1R3 traffics to and signals from the cell surface in the founding functional study (HEK293T calcium-reporter assays), consistent with native plasma-membrane residence. This is expected identity-level evidence; it is not itself evidence of the fragment's ligand specificity.
Supporting Evidence:
file:9AVES/TAS1R1/TAS1R1-uniprot.txt
SUBCELLULAR LOCATION: Cell membrane
file:9AVES/TAS1R1/TAS1R1-uniprot.txt
Multi-pass membrane protein
GO:0007186 G protein-coupled receptor signaling pathway
IEA
GO_REF:0000002
ACCEPT
Summary: Consistent with TAS1R1's class C GPCR domain architecture and with TAS1R1-TAS1R3's established role initiating G-protein-mediated taste signal transduction.
Reason: Direct consequence of the GPCR molecular function; T1R1-T1R3 signaling in taste cells canonically proceeds through a G-protein/PLCbeta2/IP3/ Ca2+/TRPM5 cascade regardless of whether the ligand is an amino acid (ancestral/umami) or a carbohydrate (derived, hummingbird-specific). The process-level GPCR signaling call does not depend on resolving that ligand-specificity question.
Supporting Evidence:
PMID:25146290
are sensed by G protein
GO:0016020 membrane
IEA
GO_REF:0000002
MARK AS OVER ANNOTATED
Summary: Generic membrane call from the same InterPro domain matches that support the more specific plasma-membrane annotation.
Reason: Correct but less informative than the co-annotated GO:0005886 (plasma membrane), which is separately supported and preferred as the core location; the generic term is redundant given that more specific, independently-supported annotation. Not core. Consistent with the equivalent generic-membrane calls for the TAS2R38/TAS2R16/TAS1R3 genes in this same PR.
GO:0050909 sensory perception of taste
IEA
GO_REF:0000117
KEEP AS NON CORE
Summary: Broad, accurate parent process term: TAS1R1 is a taste receptor subunit regardless of whether its ligand-specificity is ancestral (umami) or hummingbird-derived (sweet/carbohydrate).
Reason: Uncontroversial at this level of generality; both the ancestral umami-sensing role of TAS1R1-TAS1R3 and the hummingbird-specific sweet-sensing repurposing are instances of "sensory perception of taste." Retained as a valid but non-core parent term, since the more specific process calls below already cover this gene's role. Consistent with the equivalent calls for the other taste-receptor genes in this same PR.
GO:0050917 sensory perception of umami taste
IEA
GO_REF:0000118
KEEP AS NON CORE
Summary: TreeGrafter/PANTHER-propagated umami-taste call reflects the ancestral, tree-wide TAS1R1 function (retained in chicken, swift, and most other vertebrates), but is very likely stale for the hummingbird (Trochilidae) lineage this record belongs to, where TAS1R1-TAS1R3 has been experimentally shown (in a congeneric/confamilial species, Calypte anna) to have been repurposed to detect carbohydrates rather than amino acids.
Reason: GO:0050917 is defined as perception of "the savory taste of meats and other foods that are rich in glutamates" - i.e. amino-acid/glutamate detection. That is the correct, ancestral TAS1R1-TAS1R3 function, and it is retained in non-hummingbird birds: "cells expressing chicken or swift T1R1-T1R3 failed to detect carbohydrates at any concentration tested and instead recognized alanine and serine." But hummingbirds transformed this same receptor complex after diverging from swifts: "Receptor expression studies revealed that the ancestral umami receptor (the T1R1-T1R3 heterodimer) was repurposed in hummingbirds to function as a carbohydrate receptor," and behavioral assays in multiple hummingbird species confirmed this receptor logic drives sugar-seeking taste behavior. Oreotrochilus melanogaster is a hummingbird (family Trochilidae), so by strong phylogenetic/functional inference its TAS1R1-TAS1R3 more likely mediates carbohydrate (sweet) perception than umami perception, even though this exact species and accession have not been assayed. Some residual amino-acid sensitivity may persist ("low-affinity responses were observed to some amino acids"), so umami sensing is not necessarily fully abolished. TAS1R1 and TAS1R3 are an obligate heterodimer with a single shared ligand spectrum (see PMID:25146290: "Responses were not observed when T1R1 or T1R3 alone was used"), so this call is kept identical to the equivalent GO:0050917 row on the partner subunit TAS1R3 (genes/9AVES/TAS1R3): retained as a non-core, likely-partially-retained ancestral function, while sweet-taste detection (GO:0050916/GO:0033041, see below and in TAS1R3) is treated as the core, derived function of this receptor complex in the hummingbird lineage. KEEP_AS_NON_CORE rather than REMOVE or MODIFY because the underlying capacity is plausibly retained at low affinity, not clearly absent or simply mis-termed.
Supporting Evidence:
PMID:25146290
Receptor expression studies revealed that the ancestral umami receptor (the T1R1-T1R3 heterodimer) was repurposed in hummingbirds to function as a carbohydrate receptor.
PMID:25146290
cells expressing chicken or swift T1R1-T1R3 failed to detect carbohydrates at any concentration tested and instead recognized alanine and serine.
PMID:25146290
Low-affinity responses were observed to some amino acids
file:9AVES/TAS1R1/TAS1R1-deep-research-falcon.md
No retrieved publication independently validates this accession, gene model, or fragment boundaries.
GO:0050916 sensory perception of sweet taste
ISS NEW
Summary: NEW: proposed addition reflecting the hummingbird-specific TAS1R1-TAS1R3 sweet-taste repurposing (see review of GO:0050917 above); mirrors the annotation already present on the partner subunit TAS1R3 in this genome.
Reason: Not present in GOA for this record (TreeGrafter placed TAS1R3, but not TAS1R1, in the sweet-taste-annotated PANTHER node), but strongly supported by the same evidence base as the GO:0050917 KEEP_AS_NON_CORE review above: hummingbird T1R1-T1R3 is an obligate heterodimer whose sugar responses require both subunits, and behavioral data confirm this drives sugar-taste preference in hummingbirds. Encoded as ISS (inferred from sequence/structural similarity), with no GO_REF, since this is a curator-proposed cross-species inference (from Calypte anna data) rather than a genuine TreeGrafter/GOA-sourced row for this record. Proposed with moderate rather than high confidence because it rests on that cross-species/cross-genus inference rather than a direct assay of Oreotrochilus melanogaster or this fragment.
Supporting Evidence:
PMID:25146290
Responses were not observed when T1R1 or T1R3 alone was used, suggesting that hummingbird T1R1-T1R3 functions as an obligate heterodimer.
PMID:25146290
We propose that changing taste receptor function enabled hummingbirds to perceive and use nectar, facilitating the massive radiation of hummingbird species.

Core Functions

Obligate subunit of the TAS1R1-TAS1R3 heterodimeric class C GPCR taste receptor. In hummingbirds (family Trochilidae, including this genome's source species Oreotrochilus melanogaster) this ancestral umami (amino-acid) receptor complex has been repurposed to respond primarily to carbohydrates (sucrose, fructose, glucose, sucralose), giving hummingbirds a T1R2-independent route to sweet taste perception. Direct experimental ligand data underlying this model come from a different hummingbird, Calypte anna; no assay exists yet for O. melanogaster or this fragmentary accession, so this should be read as a strong lineage-level inference rather than a species-specific demonstration.

Cellular Locations:
Supporting Evidence:
  • PMID:25146290
    Receptor expression studies revealed that the ancestral umami receptor (the T1R1-T1R3 heterodimer) was repurposed in hummingbirds to function as a carbohydrate receptor.
  • PMID:25146290
    Responses were not observed when T1R1 or T1R3 alone was used, suggesting that hummingbird T1R1-T1R3 functions as an obligate heterodimer.

References

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Suggested Questions for Experts

Q: Has TAS1R1-TAS1R3 ligand specificity been directly assayed in any hillstar (Oreotrochilus) or other high-Andean hummingbird, given that Andean hummingbirds face unusual dietary/thermal constraints (e.g. torpor, high-altitude nectar sugar composition) that could plausibly have further tuned receptor pharmacology relative to lowland species like Calypte anna?

Q: Does the B10K genome assembly for Oreotrochilus melanogaster contain a full-length TAS1R1 transcript/CDS that resolves the two NON_TER fragment boundaries in A0A7L3NBT4, and does full-length TAS1R1 retain the amino-acid substitutions (e.g. the T1R3 venus-flytrap sites) that Baldwin et al. 2014 mapped as necessary for sugar sensitivity in Calypte anna?

Suggested Experiments

Experiment: Clone and heterologously express full-length Oreotrochilus melanogaster TAS1R1 with its native TAS1R3 partner (calcium-reporter or IP1 assay in HEK293T/GΞ±15 cells, as in Baldwin et al. 2014) to directly test carbohydrate versus amino-acid responsiveness for this species, replacing the current cross-species inference.

Experiment: Confirm oral/taste-bud expression of TAS1R1 in O. melanogaster (RT-PCR or in situ hybridization/spatial transcriptomics on lingual/oral tissue), since the current annotation of "plasma membrane" localization and involvement in taste perception rests on domain architecture and cross-species orthology rather than tissue-level evidence in this species.

Deep Research

Falcon

(TAS1R1-deep-research-falcon.md)

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πŸ“š Additional Documentation

Notes

(TAS1R1-notes.md)

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