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Protein

G-protein coupled receptor 1

Gene

GCR1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Acts as a negative regulator of GPA1-mediated abscisic acid (ABA) responses in guard cells, and together with GPA1 and GB1 during seed germination and early seedling development. 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.8 Publications

GO - Molecular functioni

  • G-protein coupled receptor activity Source: TAIR

GO - Biological processi

  • abscisic acid-activated signaling pathway Source: UniProtKB
  • activation of phospholipase C activity Source: UniProtKB
  • blue light signaling pathway Source: UniProtKB
  • brassinosteroid mediated signaling pathway Source: UniProtKB
  • cell surface receptor signaling pathway Source: InterPro
  • cytokinin-activated signaling pathway Source: UniProtKB-KW
  • flower development Source: TAIR
  • gibberellic acid mediated signaling pathway Source: UniProtKB-KW
  • lipid metabolic process Source: UniProtKB-KW
  • L-phenylalanine biosynthetic process Source: TAIR
  • maintenance of seed dormancy Source: TAIR
  • mitotic cell cycle Source: TAIR
  • negative regulation of abscisic acid-activated signaling pathway Source: UniProtKB
  • positive regulation of gibberellic acid mediated signaling pathway Source: UniProtKB
  • regulation of inositol trisphosphate biosynthetic process Source: UniProtKB
  • response to cytokinin Source: TAIR
  • response to low fluence blue light stimulus by blue low-fluence system Source: TAIR
  • seed germination Source: UniProtKB
  • tyrosine biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Abscisic acid signaling pathway, Brassinosteroid signaling pathway, Cell cycle, Cytokinin signaling pathway, Gibberellin signaling pathway, Lipid metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
G-protein coupled receptor 1
Gene namesi
Name:GCR1
Ordered Locus Names:At1g48270
ORF Names:F11A17.17
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G48270.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 2322ExtracellularSequence analysisAdd
BLAST
Transmembranei24 – 4421Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini45 – 517CytoplasmicSequence analysis
Transmembranei52 – 7221Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini73 – 8412ExtracellularSequence analysisAdd
BLAST
Transmembranei85 – 10521Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini106 – 12015CytoplasmicSequence analysisAdd
BLAST
Transmembranei121 – 14121Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini142 – 16019ExtracellularSequence analysisAdd
BLAST
Transmembranei161 – 18121Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini182 – 21332CytoplasmicSequence analysisAdd
BLAST
Transmembranei214 – 23421Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini235 – 24612ExtracellularSequence analysisAdd
BLAST
Transmembranei247 – 26721Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini268 – 32659CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • Golgi apparatus Source: TAIR
  • plasma membrane Source: UniProtKB
  • spanning component of plasma membrane Source: UniProtKB
  • vacuolar membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Hypersensitivity to abscisic acid (ABA) and to the lipid metabolite, sphingosine-1-phosphate (S1P), a transducer of the ABA signal. 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).5 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 326325G-protein coupled receptor 1PRO_0000412191Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Disulfide bondi80 ↔ 151By similarity
Glycosylationi143 – 1431N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO04714.

Expressioni

Tissue specificityi

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.3 Publications

Developmental stagei

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.1 Publication

Inductioni

Modulated during the cell cycle with a peak during the early G1 phase. Induced upon imbibition.2 Publications

Gene expression databases

GenevisibleiO04714. AT.

Interactioni

Subunit structurei

Interacts with GPA1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GPA1P180646EBI-443899,EBI-443890

Protein-protein interaction databases

BioGridi26472. 13 interactions.
IntActiO04714. 2 interactions.
STRINGi3702.AT1G48270.1.

Structurei

3D structure databases

ProteinModelPortaliO04714.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi309 – 3135Poly-Gln

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IGCQ. Eukaryota.
ENOG4110A1U. LUCA.
HOGENOMiHOG000030213.
InParanoidiO04714.
OMAiWAFGTIN.
PhylomeDBiO04714.

Family and domain databases

InterProiIPR022343. GCR1-cAMP_receptor.
IPR017981. GPCR_2-like.
IPR022340. GPCR_GCR1_put.
[Graphical view]
PRINTSiPR02001. GCR1CAMPR.
PR02000. GCR1PLANT.
PROSITEiPS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O04714-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAVLTAGGG LTAGDRSIIT AINTGASSLS FVGSAFIVLC YCLFKELRKF
60 70 80 90 100
SFKLVFYLAL SDMLCSFFLI VGDPSKGFIC YAQGYTTHFF CVASFLWTTT
110 120 130 140 150
IAFTLHRTVV KHKTDVEDLE AMFHLYVWGT SLVVTVIRSF GNNHSHLGPW
160 170 180 190 200
CWTQTGLKGK AVHFLTFYAP LWGAILYNGF TYFQVIRMLR NARRMAVGMS
210 220 230 240 250
DRVDQFDNRA ELKVLNRWGY YPLILIGSWA FGTINRIHDF IEPGHKIFWL
260 270 280 290 300
SVLDVGTAAL MGLFNSIAYG FNSSVRRAIH ERLELFLPER LYRWLPSNFR
310 320
PKNHLILHQQ QQQRSEMVSL KTEDQQ
Length:326
Mass (Da):37,248
Last modified:July 1, 1997 - v1
Checksum:iC00F1109720A4453
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631M → V in AAM20722 (PubMed:14593172).Curated
Sequence conflicti63 – 631M → V in AAN15633 (PubMed:14593172).Curated
Sequence conflicti96 – 961L → F in CAA72145 (PubMed:9370348).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11278 mRNA. Translation: CAA72145.1.
U95142 Genomic DNA. Translation: AAC49961.1.
U95143 mRNA. Translation: AAC49962.1.
AC007932 Genomic DNA. Translation: AAD49769.1.
CP002684 Genomic DNA. Translation: AEE32270.1.
AY099871 mRNA. Translation: AAM20722.1.
BT000314 mRNA. Translation: AAN15633.1.
AK228479 mRNA. Translation: BAF00405.1.
PIRiF96522.
RefSeqiNP_175261.1. NM_103724.2.
UniGeneiAt.21469.

Genome annotation databases

EnsemblPlantsiAT1G48270.1; AT1G48270.1; AT1G48270.
GeneIDi841247.
GrameneiAT1G48270.1; AT1G48270.1; AT1G48270.
KEGGiath:AT1G48270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11278 mRNA. Translation: CAA72145.1.
U95142 Genomic DNA. Translation: AAC49961.1.
U95143 mRNA. Translation: AAC49962.1.
AC007932 Genomic DNA. Translation: AAD49769.1.
CP002684 Genomic DNA. Translation: AEE32270.1.
AY099871 mRNA. Translation: AAM20722.1.
BT000314 mRNA. Translation: AAN15633.1.
AK228479 mRNA. Translation: BAF00405.1.
PIRiF96522.
RefSeqiNP_175261.1. NM_103724.2.
UniGeneiAt.21469.

3D structure databases

ProteinModelPortaliO04714.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi26472. 13 interactions.
IntActiO04714. 2 interactions.
STRINGi3702.AT1G48270.1.

Protein family/group databases

GPCRDBiSearch...

Proteomic databases

PaxDbiO04714.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G48270.1; AT1G48270.1; AT1G48270.
GeneIDi841247.
GrameneiAT1G48270.1; AT1G48270.1; AT1G48270.
KEGGiath:AT1G48270.

Organism-specific databases

TAIRiAT1G48270.

Phylogenomic databases

eggNOGiENOG410IGCQ. Eukaryota.
ENOG4110A1U. LUCA.
HOGENOMiHOG000030213.
InParanoidiO04714.
OMAiWAFGTIN.
PhylomeDBiO04714.

Miscellaneous databases

PROiO04714.

Gene expression databases

GenevisibleiO04714. AT.

Family and domain databases

InterProiIPR022343. GCR1-cAMP_receptor.
IPR017981. GPCR_2-like.
IPR022340. GPCR_GCR1_put.
[Graphical view]
PRINTSiPR02001. GCR1CAMPR.
PR02000. GCR1PLANT.
PROSITEiPS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a putative G-protein-coupled receptor from Arabidopsis thaliana."
    Josefsson L.G., Rask L.
    Eur. J. Biochem. 249:415-420(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "A higher plant seven-transmembrane receptor that influences sensitivity to cytokinins."
    Plakidou-Dymock S., Dymock D., Hooley R.
    Curr. Biol. 8:315-324(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "Re-evaluation of the cytokinin receptor role of the Arabidopsis gene GCR1."
    Humphrey T.V., Botella J.R.
    J. Plant Physiol. 158:645-653(2001)
    Cited for: SUBCELLULAR LOCATION.
    Strain: cv. Landsberg erecta.
  8. "GCR1, the putative Arabidopsis G protein-coupled receptor gene is cell cycle-regulated, and its overexpression abolishes seed dormancy and shortens time to flowering."
    Colucci G., Apone F., Alyeshmerni N., Chalmers D., Chrispeels M.J.
    Proc. Natl. Acad. Sci. U.S.A. 99:4736-4741(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION DURING THE CELL CYCLE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: cv. Columbia.
  9. "The G-protein-coupled receptor GCR1 regulates DNA synthesis through activation of phosphatidylinositol-specific phospholipase C."
    Apone F., Alyeshmerni N., Wiens K., Chalmers D., Chrispeels M.J., Colucci G.
    Plant Physiol. 133:571-579(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "The Arabidopsis putative G protein-coupled receptor GCR1 interacts with the G protein alpha subunit GPA1 and regulates abscisic acid signaling."
    Pandey S., Assmann S.M.
    Plant Cell 16:1616-1632(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH GPA1.
    Strain: cv. Columbia and cv. Wassilewskija.
  11. "GCR1 can act independently of heterotrimeric G-protein in response to brassinosteroids and gibberellins in Arabidopsis seed germination."
    Chen J.-G., Pandey S., Huang J., Alonso J.M., Ecker J.R., Assmann S.M., Jones A.M.
    Plant Physiol. 135:907-915(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  12. "G-protein-coupled receptor 1, G-protein Galpha-subunit 1, and prephenate dehydratase 1 are required for blue light-induced production of phenylalanine in etiolated Arabidopsis."
    Warpeha K.M., Lateef S.S., Lapik Y., Anderson M., Lee B.-S., Kaufman L.S.
    Plant Physiol. 140:844-855(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  13. "G-protein complex mutants are hypersensitive to abscisic acid regulation of germination and postgermination development."
    Pandey S., Chen J.-G., Jones A.M., Assmann S.M.
    Plant Physiol. 141:243-256(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY IMBIBITION.
    Strain: cv. Columbia.
  14. "The GCR1, GPA1, PRN1, NF-Y signal chain mediates both blue light and abscisic acid responses in Arabidopsis."
    Warpeha K.M., Upadhyay S., Yeh J., Adamiak J., Hawkins S.I., Lapik Y.R., Anderson M.B., Kaufman L.S.
    Plant Physiol. 143:1590-1600(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: cv. Columbia and cv. Wassilewskija.
  15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGCR1_ARATH
AccessioniPrimary (citable) accession number: O04714
Secondary accession number(s): O04214, Q8LPG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 1, 1997
Last modified: February 17, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.