GPR1_YEAST
ID GPR1_YEAST Reviewed; 961 AA.
AC Q12361; D6VRV9;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=G protein-coupled receptor GPR1;
GN Name=GPR1; OrderedLocusNames=YDL035C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=9524122; DOI=10.1093/emboj/17.7.1996;
RA Xue Y., Batlle M., Hirsch J.P.;
RT "GPR1 encodes a putative G protein-coupled receptor that associates with
RT the Gpa2p Galpha subunit and functions in a Ras-independent pathway.";
RL EMBO J. 17:1996-2007(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9046088;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<65::aid-yea50>3.0.co;2-t;
RA Saren A.-M., Laamanen P., Lejarcegui J.B., Paulin L.;
RT "The sequence of a 36.7 kb segment on the left arm of chromosome IV from
RT Saccharomyces cerevisiae reveals 20 non-overlapping open reading frames
RT (ORFs) including SIT4, FAD1, NAM1, RNA11, SIR2, NAT1, PRP9, ACT2 and MPS1
RT and 11 new ORFs.";
RL Yeast 13:65-71(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Seems to associate with GPA2 and act as G protein-coupled
CC receptor that senses glucose and controls filamentous growth. It acts
CC upstream of adenylate cyclase and is required for glucose activation of
CC cAMP synthesis in concert with a glucose phosphorylation-dependent
CC mechanism.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9524122};
CC Multi-pass membrane protein {ECO:0000269|PubMed:9524122}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor GPR1/git3 family.
CC {ECO:0000305}.
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DR EMBL; Z74083; CAA98593.1; -; Genomic_DNA.
DR EMBL; Z71781; CAA96454.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11819.1; -; Genomic_DNA.
DR PIR; JC5808; JC5808.
DR PIR; S67568; S67568.
DR RefSeq; NP_010249.1; NM_001180094.1.
DR AlphaFoldDB; Q12361; -.
DR BioGRID; 32023; 692.
DR DIP; DIP-8949N; -.
DR IntAct; Q12361; 3.
DR MINT; Q12361; -.
DR STRING; 4932.YDL035C; -.
DR TCDB; 8.A.92.1.15; the g-protein AlphaBetaGama complex (gpc) family.
DR iPTMnet; Q12361; -.
DR MaxQB; Q12361; -.
DR PaxDb; Q12361; -.
DR PRIDE; Q12361; -.
DR EnsemblFungi; YDL035C_mRNA; YDL035C; YDL035C.
DR GeneID; 851527; -.
DR KEGG; sce:YDL035C; -.
DR SGD; S000002193; GPR1.
DR VEuPathDB; FungiDB:YDL035C; -.
DR eggNOG; ENOG502QU8E; Eukaryota.
DR HOGENOM; CLU_314960_0_0_1; -.
DR InParanoid; Q12361; -.
DR OMA; RGWYYRG; -.
DR BioCyc; YEAST:G3O-29459-MON; -.
DR PRO; PR:Q12361; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12361; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IMP:SGD.
DR GO; GO:0005536; F:glucose binding; IMP:SGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0051594; P:detection of glucose; IMP:SGD.
DR GO; GO:0009731; P:detection of sucrose stimulus; IMP:SGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:SGD.
DR GO; GO:0010255; P:glucose mediated signaling pathway; IMP:SGD.
DR GO; GO:0009757; P:hexose mediated signaling; IMP:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0009745; P:sucrose mediated signaling; IMP:SGD.
DR InterPro; IPR023041; Glucose_rcpt_Git3_N.
DR InterPro; IPR022596; GPR1_C.
DR Pfam; PF11710; Git3; 1.
DR Pfam; PF11970; GPR_Gpa2_C; 1.
PE 1: Evidence at protein level;
KW Cell membrane; G-protein coupled receptor; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..961
FT /note="G protein-coupled receptor GPR1"
FT /id="PRO_0000195084"
FT TOPO_DOM 1..56
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..79
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..114
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..133
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..156
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..198
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..273
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..619
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..642
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..822
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 823..843
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..961
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 468..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
SQ SEQUENCE 961 AA; 110709 MW; 9889D857872A4209 CRC64;
MITEGFPPNL NALKGSSLLE KRVDSLRQLN TTTVNQLLGL PGMTSTFTAP QLLQLRIIAI
TASAVSLIAG CLGMFFLSKM DKRRKVFRHD LIAFLIICDF LKAFILMIYP MIILINNSVY
ATPAFFNTLG WFTAFAIEGA DMAIMIFAIH FAILIFKPNW KWRNKRSGNM EGGLYKKRSY
IWPITALVPA ILASLAFINY NKLNDDSDTT IILDNNNYNF PDSPRQGGYK PWSAWCYLPP
KPYWYKIVLS WGPRYFIIIF IFAVYLSIYI FITSESKRIK AQIGDFNHNV LEEEKEKKKL
FGLGHWGKAK WYFRSYFKLP LLHLLRNLKN FFTISFIDPN EETDDSGSSN GTFNFGESSN
EIPTLFRKTN TGSDENVSAS GGVRLLDYNS AKPLDMSKYA MSEQPDLERN NPFDCENDIT
LNPSELVSKQ KEHKVTFSVE NEGLDTRKSS MLGHQTFSCQ NSLESPLAMY DNKNDNSDIT
SNIKEKGGII NNNSNNDDDD NNNNNDNDND NNNSNNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNSNNIKN NVDNNNTNPA DNIPTLSNEA FTPSQQFSQE RVNNNADRCE NSSFTNVQQH
FQAQTYKQMK KRRAQIQKNL RAIFIYPLSY IGIWLFPIIA DALQYNHEIK HGPTMWVTYI
DTCVRPLSCL VDVIVYLFKE KPWNYSWAKT ESKYLIEKYI LKGELGEKEI LKFCHSNWGK
RGWYYRGKWK KRKCWKYSTN PLKRILWFVE RFFKQLFELK LHFSFYDNCD DFEYWENYYS
AKDSNDNKRT ESDETKTNSS DRSLPSNSLE LQAMLNNITA EEVEVPLFWR IIHHIPMLGG
IDLDELNRLL KIRYNNDHFS LPGLKFALNQ NKSHDKHQDV STNSMVKSSF FSSNIVTNDD
ENSIEEDKNL RYSDASASEN YLVKPTIPGT TPDPIIEAQN DNDSSDSSGI DLIAFLRNGP
L
