O04714 · GCR1_ARATH
- ProteinG-protein coupled receptor 1
- GeneGCR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids326 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Together with GPA1, may regulate the cell cycle via a signaling cascade that uses phosphatidylinositol-specific phospholipase C (PI-PLC) as an effector and inositol 1,4,5-trisphosphate(IP3) as a second messenger. Promotes PI-PLC activity and IP3 accumulation. Involved in the blue light (BL) signaling. Together with GPA1 and ADT3, required for BL-mediated synthesis of phenylpyruvate and subsequently of phenylalanine (Phe), in etiolated seedlings. Probably involved in cytokinin signal transduction. Plays a positive role in gibberellin- (GA) and brassinosteroid- (BR) regulated seed germination, probably independently of a heterotrimeric G-protein. Mediates seed dormancy abolition, and promotes seed germination and flowering.
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameG-protein coupled receptor 1
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionO04714
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: Localized to the outer edge of the leaf epidermal cells in a punctuate pattern.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 2-23 | Extracellular | ||||
Sequence: SAVLTAGGGLTAGDRSIITAIN | ||||||
Transmembrane | 24-44 | Helical; Name=1 | ||||
Sequence: TGASSLSFVGSAFIVLCYCLF | ||||||
Topological domain | 45-51 | Cytoplasmic | ||||
Sequence: KELRKFS | ||||||
Transmembrane | 52-72 | Helical; Name=2 | ||||
Sequence: FKLVFYLALSDMLCSFFLIVG | ||||||
Topological domain | 73-84 | Extracellular | ||||
Sequence: DPSKGFICYAQG | ||||||
Transmembrane | 85-105 | Helical; Name=3 | ||||
Sequence: YTTHFFCVASFLWTTTIAFTL | ||||||
Topological domain | 106-120 | Cytoplasmic | ||||
Sequence: HRTVVKHKTDVEDLE | ||||||
Transmembrane | 121-141 | Helical; Name=4 | ||||
Sequence: AMFHLYVWGTSLVVTVIRSFG | ||||||
Topological domain | 142-160 | Extracellular | ||||
Sequence: NNHSHLGPWCWTQTGLKGK | ||||||
Transmembrane | 161-181 | Helical; Name=5 | ||||
Sequence: AVHFLTFYAPLWGAILYNGFT | ||||||
Topological domain | 182-213 | Cytoplasmic | ||||
Sequence: YFQVIRMLRNARRMAVGMSDRVDQFDNRAELK | ||||||
Transmembrane | 214-234 | Helical; Name=6 | ||||
Sequence: VLNRWGYYPLILIGSWAFGTI | ||||||
Topological domain | 235-246 | Extracellular | ||||
Sequence: NRIHDFIEPGHK | ||||||
Transmembrane | 247-267 | Helical; Name=7 | ||||
Sequence: IFWLSVLDVGTAALMGLFNSI | ||||||
Topological domain | 268-326 | Cytoplasmic | ||||
Sequence: AYGFNSSVRRAIHERLELFLPERLYRWLPSNFRPKNHLILHQQQQQRSEMVSLKTEDQQ |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Improved drought tolerance accompanied by lower rates of water loss. Impaired sensitivity to gibberellin (GA) and brassinosteroid (BR) in seed germination. Hypersensitivity to ABA and glucose (Glc) during and after seed germination. Altered response to blue light (BL).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 13 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000412191 | 2-326 | G-protein coupled receptor 1 | |||
Sequence: SAVLTAGGGLTAGDRSIITAINTGASSLSFVGSAFIVLCYCLFKELRKFSFKLVFYLALSDMLCSFFLIVGDPSKGFICYAQGYTTHFFCVASFLWTTTIAFTLHRTVVKHKTDVEDLEAMFHLYVWGTSLVVTVIRSFGNNHSHLGPWCWTQTGLKGKAVHFLTFYAPLWGAILYNGFTYFQVIRMLRNARRMAVGMSDRVDQFDNRAELKVLNRWGYYPLILIGSWAFGTINRIHDFIEPGHKIFWLSVLDVGTAALMGLFNSIAYGFNSSVRRAIHERLELFLPERLYRWLPSNFRPKNHLILHQQQQQRSEMVSLKTEDQQ | ||||||
Disulfide bond | 80↔151 | |||||
Sequence: CYAQGYTTHFFCVASFLWTTTIAFTLHRTVVKHKTDVEDLEAMFHLYVWGTSLVVTVIRSFGNNHSHLGPWC | ||||||
Glycosylation | 143 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Mostly present in the meristematic regions. Expressed at low levels in seedlings, vascular tissues of cotyledons, hypocotyl, and roots, stems, leaves, flowering buds and siliques. In dark-grown seedlings, localized in the cotyledons and the hook.
Induction
Modulated during the cell cycle with a peak during the early G1 phase.
Developmental stage
In seedlings, mostly expressed in small roots, and to a lower extent in hypocotyls. In young plants, equaly expressed in leaves, roots, and shoot tip. In old plants, present in roots, flower buds and young siliques, but not in leaves.
Gene expression databases
Interaction
Subunit
Interacts with GPA1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O04714 | GPA1 P18064 | 6 | EBI-443899, EBI-443890 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length326
- Mass (Da)37,248
- Last updated1997-07-01 v1
- ChecksumC00F1109720A4453
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 63 | in Ref. 5; AAM20722/AAN15633 | ||||
Sequence: M → V | ||||||
Sequence conflict | 96 | in Ref. 1; CAA72145 | ||||
Sequence: L → F |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y11278 EMBL· GenBank· DDBJ | CAA72145.1 EMBL· GenBank· DDBJ | mRNA | ||
U95142 EMBL· GenBank· DDBJ | AAC49961.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U95143 EMBL· GenBank· DDBJ | AAC49962.1 EMBL· GenBank· DDBJ | mRNA | ||
AC007932 EMBL· GenBank· DDBJ | AAD49769.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE32270.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | ANM59445.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY099871 EMBL· GenBank· DDBJ | AAM20722.1 EMBL· GenBank· DDBJ | mRNA | ||
BT000314 EMBL· GenBank· DDBJ | AAN15633.1 EMBL· GenBank· DDBJ | mRNA | ||
AK228479 EMBL· GenBank· DDBJ | BAF00405.1 EMBL· GenBank· DDBJ | mRNA |