ID GCR1_ARATH Reviewed; 326 AA.
AC O04714; O04214; Q8LPG0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 24-JAN-2024, entry version 146.
DE RecName: Full=G-protein coupled receptor 1;
GN Name=GCR1; OrderedLocusNames=At1g48270; ORFNames=F11A17.17;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9370348; DOI=10.1111/j.1432-1033.1997.t01-1-00415.x;
RA Josefsson L.G., Rask L.;
RT "Cloning of a putative G-protein-coupled receptor from Arabidopsis
RT thaliana.";
RL Eur. J. Biochem. 249:415-420(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9512416; DOI=10.1016/s0960-9822(98)70131-9;
RA Plakidou-Dymock S., Dymock D., Hooley R.;
RT "A higher plant seven-transmembrane receptor that influences sensitivity to
RT cytokinins.";
RL Curr. Biol. 8:315-324(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX DOI=10.1078/0176-1617-00316;
RA Humphrey T.V., Botella J.R.;
RT "Re-evaluation of the cytokinin receptor role of the Arabidopsis gene
RT GCR1.";
RL J. Plant Physiol. 158:645-653(2001).
RN [8]
RP FUNCTION, INDUCTION DURING THE CELL CYCLE, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=11930019; DOI=10.1073/pnas.072087699;
RA Colucci G., Apone F., Alyeshmerni N., Chalmers D., Chrispeels M.J.;
RT "GCR1, the putative Arabidopsis G protein-coupled receptor gene is cell
RT cycle-regulated, and its overexpression abolishes seed dormancy and
RT shortens time to flowering.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4736-4741(2002).
RN [9]
RP FUNCTION.
RX PubMed=12972659; DOI=10.1104/pp.103.026005;
RA Apone F., Alyeshmerni N., Wiens K., Chalmers D., Chrispeels M.J.,
RA Colucci G.;
RT "The G-protein-coupled receptor GCR1 regulates DNA synthesis through
RT activation of phosphatidylinositol-specific phospholipase C.";
RL Plant Physiol. 133:571-579(2003).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH GPA1.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=15155892; DOI=10.1105/tpc.020321;
RA Pandey S., Assmann S.M.;
RT "The Arabidopsis putative G protein-coupled receptor GCR1 interacts with
RT the G protein alpha subunit GPA1 and regulates abscisic acid signaling.";
RL Plant Cell 16:1616-1632(2004).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=15181210; DOI=10.1104/pp.104.038992;
RA Chen J.-G., Pandey S., Huang J., Alonso J.M., Ecker J.R., Assmann S.M.,
RA Jones A.M.;
RT "GCR1 can act independently of heterotrimeric G-protein in response to
RT brassinosteroids and gibberellins in Arabidopsis seed germination.";
RL Plant Physiol. 135:907-915(2004).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16415218; DOI=10.1104/pp.105.071282;
RA Warpeha K.M., Lateef S.S., Lapik Y., Anderson M., Lee B.-S., Kaufman L.S.;
RT "G-protein-coupled receptor 1, G-protein Galpha-subunit 1, and prephenate
RT dehydratase 1 are required for blue light-induced production of
RT phenylalanine in etiolated Arabidopsis.";
RL Plant Physiol. 140:844-855(2006).
RN [13]
RP RETRACTED PAPER.
RC STRAIN=cv. Columbia;
RX PubMed=16581874; DOI=10.1104/pp.106.079038;
RA Pandey S., Chen J.-G., Jones A.M., Assmann S.M.;
RT "G-protein complex mutants are hypersensitive to abscisic acid regulation
RT of germination and postgermination development.";
RL Plant Physiol. 141:243-256(2006).
RN [14]
RP RETRACTION NOTICE OF PUBMED:16581874.
RX PubMed=31685692; DOI=10.1104/pp.19.01182;
RA Pandey S., Chen J.-G., Jones A.M., Assmann S.M.;
RL Plant Physiol. 181:1393-1393(2019).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=17322342; DOI=10.1104/pp.106.089904;
RA Warpeha K.M., Upadhyay S., Yeh J., Adamiak J., Hawkins S.I., Lapik Y.R.,
RA Anderson M.B., Kaufman L.S.;
RT "The GCR1, GPA1, PRN1, NF-Y signal chain mediates both blue light and
RT abscisic acid responses in Arabidopsis.";
RL Plant Physiol. 143:1590-1600(2007).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Together with GPA1, may regulate the cell cycle via a
CC signaling cascade that uses phosphatidylinositol-specific phospholipase
CC C (PI-PLC) as an effector and inositol 1,4,5-trisphosphate(IP(3)) as a
CC second messenger. Promotes PI-PLC activity and IP(3) accumulation.
CC Involved in the blue light (BL) signaling. Together with GPA1 and ADT3,
CC required for BL-mediated synthesis of phenylpyruvate and subsequently
CC of phenylalanine (Phe), in etiolated seedlings. Probably involved in
CC cytokinin signal transduction. Plays a positive role in
CC gibberellin- (GA) and brassinosteroid- (BR) regulated seed germination,
CC probably independently of a heterotrimeric G-protein. Mediates seed
CC dormancy abolition, and promotes seed germination and flowering.
CC {ECO:0000269|PubMed:11930019, ECO:0000269|PubMed:12972659,
CC ECO:0000269|PubMed:15155892, ECO:0000269|PubMed:15181210,
CC ECO:0000269|PubMed:16415218, ECO:0000269|PubMed:17322342,
CC ECO:0000269|PubMed:9512416}.
CC -!- SUBUNIT: Interacts with GPA1. {ECO:0000269|PubMed:15155892}.
CC -!- INTERACTION:
CC O04714; P18064: GPA1; NbExp=6; IntAct=EBI-443899, EBI-443890;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15181210,
CC ECO:0000269|Ref.7}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15181210, ECO:0000269|Ref.7}. Note=Localized to the
CC outer edge of the leaf epidermal cells in a punctuate pattern.
CC -!- TISSUE SPECIFICITY: Mostly present in the meristematic regions.
CC Expressed at low levels in seedlings, vascular tissues of cotyledons,
CC hypocotyl, and roots, stems, leaves, flowering buds and siliques. In
CC dark-grown seedlings, localized in the cotyledons and the hook.
CC {ECO:0000269|PubMed:11930019, ECO:0000269|PubMed:15181210,
CC ECO:0000269|PubMed:9512416}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, mostly expressed in small roots, and
CC to a lower extent in hypocotyls. In young plants, equaly expressed in
CC leaves, roots, and shoot tip. In old plants, present in roots, flower
CC buds and young siliques, but not in leaves.
CC {ECO:0000269|PubMed:11930019}.
CC -!- INDUCTION: Modulated during the cell cycle with a peak during the early
CC G(1) phase. {ECO:0000269|PubMed:11930019}.
CC -!- DISRUPTION PHENOTYPE: Improved drought tolerance accompanied by lower
CC rates of water loss. Impaired sensitivity to gibberellin (GA) and
CC brassinosteroid (BR) in seed germination. Hypersensitivity to ABA and
CC glucose (Glc) during and after seed germination. Altered response to
CC blue light (BL). {ECO:0000269|PubMed:15155892,
CC ECO:0000269|PubMed:15181210, ECO:0000269|PubMed:16415218,
CC ECO:0000269|PubMed:17322342}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
CC -!- CAUTION: An article reported a role as negative regulator of ABA during
CC seed germination; however, this paper was later retracted.
CC {ECO:0000305|PubMed:16581874, ECO:0000305|PubMed:31685692}.
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DR EMBL; Y11278; CAA72145.1; -; mRNA.
DR EMBL; U95142; AAC49961.1; -; Genomic_DNA.
DR EMBL; U95143; AAC49962.1; -; mRNA.
DR EMBL; AC007932; AAD49769.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32270.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59445.1; -; Genomic_DNA.
DR EMBL; AY099871; AAM20722.1; -; mRNA.
DR EMBL; BT000314; AAN15633.1; -; mRNA.
DR EMBL; AK228479; BAF00405.1; -; mRNA.
DR PIR; F96522; F96522.
DR RefSeq; NP_001321802.1; NM_001333320.1.
DR RefSeq; NP_175261.1; NM_103724.2.
DR AlphaFoldDB; O04714; -.
DR SMR; O04714; -.
DR BioGRID; 26472; 13.
DR IntAct; O04714; 3.
DR STRING; 3702.O04714; -.
DR TCDB; 9.A.14.5.2; the g-protein-coupled receptor (gpcr) family.
DR GlyCosmos; O04714; 1 site, No reported glycans.
DR iPTMnet; O04714; -.
DR PaxDb; 3702-AT1G48270-1; -.
DR ProteomicsDB; 222023; -.
DR EnsemblPlants; AT1G48270.1; AT1G48270.1; AT1G48270.
DR EnsemblPlants; AT1G48270.2; AT1G48270.2; AT1G48270.
DR GeneID; 841247; -.
DR Gramene; AT1G48270.1; AT1G48270.1; AT1G48270.
DR Gramene; AT1G48270.2; AT1G48270.2; AT1G48270.
DR KEGG; ath:AT1G48270; -.
DR Araport; AT1G48270; -.
DR TAIR; AT1G48270; GCR1.
DR eggNOG; ENOG502QUBH; Eukaryota.
DR HOGENOM; CLU_077260_0_0_1; -.
DR InParanoid; O04714; -.
DR OMA; FYSPDMT; -.
DR OrthoDB; 180737at2759; -.
DR PhylomeDB; O04714; -.
DR PRO; PR:O04714; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04714; baseline and differential.
DR Genevisible; O04714; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0007202; P:activation of phospholipase C activity; IMP:UniProtKB.
DR GO; GO:0009785; P:blue light signaling pathway; IMP:UniProtKB.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IMP:TAIR.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0010231; P:maintenance of seed dormancy; IMP:TAIR.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:TAIR.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009939; P:positive regulation of gibberellic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0032960; P:regulation of inositol trisphosphate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
DR GO; GO:0010244; P:response to low fluence blue light stimulus by blue low-fluence system; IMP:TAIR.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IMP:TAIR.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR022343; GCR1-cAMP_receptor.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR022340; GPCR_GCR1_put.
DR PANTHER; PTHR23112; G PROTEIN-COUPLED RECEPTOR 157-RELATED; 1.
DR PANTHER; PTHR23112:SF0; G-PROTEIN COUPLED RECEPTOR 157; 1.
DR Pfam; PF05462; Dicty_CAR; 1.
DR PRINTS; PR02001; GCR1CAMPR.
DR PRINTS; PR02000; GCR1PLANT.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Acetylation;
KW Brassinosteroid signaling pathway; Cell cycle; Cell membrane;
KW Cytokinin signaling pathway; Disulfide bond; G-protein coupled receptor;
KW Gibberellin signaling pathway; Glycoprotein; Lipid metabolism; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..326
FT /note="G-protein coupled receptor 1"
FT /id="PRO_0000412191"
FT TOPO_DOM 2..23
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..84
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..246
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..151
FT /evidence="ECO:0000250"
FT CONFLICT 63
FT /note="M -> V (in Ref. 5; AAM20722/AAN15633)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="L -> F (in Ref. 1; CAA72145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 37248 MW; C00F1109720A4453 CRC64;
MSAVLTAGGG LTAGDRSIIT AINTGASSLS FVGSAFIVLC YCLFKELRKF SFKLVFYLAL
SDMLCSFFLI VGDPSKGFIC YAQGYTTHFF CVASFLWTTT IAFTLHRTVV KHKTDVEDLE
AMFHLYVWGT SLVVTVIRSF GNNHSHLGPW CWTQTGLKGK AVHFLTFYAP LWGAILYNGF
TYFQVIRMLR NARRMAVGMS DRVDQFDNRA ELKVLNRWGY YPLILIGSWA FGTINRIHDF
IEPGHKIFWL SVLDVGTAAL MGLFNSIAYG FNSSVRRAIH ERLELFLPER LYRWLPSNFR
PKNHLILHQQ QQQRSEMVSL KTEDQQ
//
