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Protein

G protein-coupled receptor GPR1

Gene

GPR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Seems to associate with GPA2 and act as G protein-coupled receptor that senses glucose and controls filamentous growth. It acts upstream of adenylate cyclase and is required for glucose activation of cAMP synthesis in concert with a glucose phosphorylation-dependent mechanism.

GO - Molecular functioni

  • glucose binding Source: SGD
  • G-protein coupled receptor activity Source: SGD

GO - Biological processi

  • detection of glucose Source: SGD
  • detection of sucrose stimulus Source: SGD
  • glucose mediated signaling pathway Source: SGD
  • G-protein coupled receptor signaling pathway Source: SGD
  • hexose mediated signaling Source: SGD
  • invasive growth in response to glucose limitation Source: SGD
  • pseudohyphal growth Source: SGD
  • replicative cell aging Source: SGD
  • sucrose mediated signaling Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

BioCyciYEAST:G3O-29459-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
G protein-coupled receptor GPR1
Gene namesi
Name:GPR1
Ordered Locus Names:YDL035C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL035C.
SGDiS000002193. GPR1.

Subcellular locationi

  • Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5656ExtracellularSequence analysisAdd
BLAST
Transmembranei57 – 7923Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini80 – 9112CytoplasmicSequence analysisAdd
BLAST
Transmembranei92 – 11423Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini115 – 13319ExtracellularSequence analysisAdd
BLAST
Transmembranei134 – 15623Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini157 – 17822CytoplasmicSequence analysisAdd
BLAST
Transmembranei179 – 19820Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini199 – 25052ExtracellularSequence analysisAdd
BLAST
Transmembranei251 – 27323Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini274 – 619346CytoplasmicSequence analysisAdd
BLAST
Transmembranei620 – 64223Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini643 – 822180ExtracellularSequence analysisAdd
BLAST
Transmembranei823 – 84321Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini844 – 961118CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 961961G protein-coupled receptor GPR1PRO_0000195084Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei373 – 3731PhosphoserineCombined sources
Modified residuei903 – 9031PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12361.
PRIDEiQ12361.

PTM databases

iPTMnetiQ12361.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
URE2P232021EBI-7844,EBI-20138
YDC1Q028961EBI-7844,EBI-22203

Protein-protein interaction databases

BioGridi32023. 52 interactions.
DIPiDIP-8949N.
IntActiQ12361. 3 interactions.
MINTiMINT-1354367.

Structurei

3D structure databases

ProteinModelPortaliQ12361.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi501 – 54747Poly-AsnAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiQ12361.
KOiK12762.
OMAiAWCYLPP.
OrthoDBiEOG7VTDZ0.

Family and domain databases

InterProiIPR023041. Glucose_rcpt_Git3_N.
IPR022596. GPR1_C.
[Graphical view]
PfamiPF11710. Git3. 1 hit.
PF11970. GPR_Gpa2_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12361-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MITEGFPPNL NALKGSSLLE KRVDSLRQLN TTTVNQLLGL PGMTSTFTAP
60 70 80 90 100
QLLQLRIIAI TASAVSLIAG CLGMFFLSKM DKRRKVFRHD LIAFLIICDF
110 120 130 140 150
LKAFILMIYP MIILINNSVY ATPAFFNTLG WFTAFAIEGA DMAIMIFAIH
160 170 180 190 200
FAILIFKPNW KWRNKRSGNM EGGLYKKRSY IWPITALVPA ILASLAFINY
210 220 230 240 250
NKLNDDSDTT IILDNNNYNF PDSPRQGGYK PWSAWCYLPP KPYWYKIVLS
260 270 280 290 300
WGPRYFIIIF IFAVYLSIYI FITSESKRIK AQIGDFNHNV LEEEKEKKKL
310 320 330 340 350
FGLGHWGKAK WYFRSYFKLP LLHLLRNLKN FFTISFIDPN EETDDSGSSN
360 370 380 390 400
GTFNFGESSN EIPTLFRKTN TGSDENVSAS GGVRLLDYNS AKPLDMSKYA
410 420 430 440 450
MSEQPDLERN NPFDCENDIT LNPSELVSKQ KEHKVTFSVE NEGLDTRKSS
460 470 480 490 500
MLGHQTFSCQ NSLESPLAMY DNKNDNSDIT SNIKEKGGII NNNSNNDDDD
510 520 530 540 550
NNNNNDNDND NNNSNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNSNNIKN
560 570 580 590 600
NVDNNNTNPA DNIPTLSNEA FTPSQQFSQE RVNNNADRCE NSSFTNVQQH
610 620 630 640 650
FQAQTYKQMK KRRAQIQKNL RAIFIYPLSY IGIWLFPIIA DALQYNHEIK
660 670 680 690 700
HGPTMWVTYI DTCVRPLSCL VDVIVYLFKE KPWNYSWAKT ESKYLIEKYI
710 720 730 740 750
LKGELGEKEI LKFCHSNWGK RGWYYRGKWK KRKCWKYSTN PLKRILWFVE
760 770 780 790 800
RFFKQLFELK LHFSFYDNCD DFEYWENYYS AKDSNDNKRT ESDETKTNSS
810 820 830 840 850
DRSLPSNSLE LQAMLNNITA EEVEVPLFWR IIHHIPMLGG IDLDELNRLL
860 870 880 890 900
KIRYNNDHFS LPGLKFALNQ NKSHDKHQDV STNSMVKSSF FSSNIVTNDD
910 920 930 940 950
ENSIEEDKNL RYSDASASEN YLVKPTIPGT TPDPIIEAQN DNDSSDSSGI
960
DLIAFLRNGP L
Length:961
Mass (Da):110,709
Last modified:November 1, 1996 - v1
Checksum:i9889D857872A4209
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74083 Genomic DNA. Translation: CAA98593.1.
Z71781 Genomic DNA. Translation: CAA96454.1.
BK006938 Genomic DNA. Translation: DAA11819.1.
PIRiJC5808.
S67568.
RefSeqiNP_010249.1. NM_001180094.1.

Genome annotation databases

EnsemblFungiiYDL035C; YDL035C; YDL035C.
GeneIDi851527.
KEGGisce:YDL035C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74083 Genomic DNA. Translation: CAA98593.1.
Z71781 Genomic DNA. Translation: CAA96454.1.
BK006938 Genomic DNA. Translation: DAA11819.1.
PIRiJC5808.
S67568.
RefSeqiNP_010249.1. NM_001180094.1.

3D structure databases

ProteinModelPortaliQ12361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32023. 52 interactions.
DIPiDIP-8949N.
IntActiQ12361. 3 interactions.
MINTiMINT-1354367.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiQ12361.

Proteomic databases

MaxQBiQ12361.
PRIDEiQ12361.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL035C; YDL035C; YDL035C.
GeneIDi851527.
KEGGisce:YDL035C.

Organism-specific databases

EuPathDBiFungiDB:YDL035C.
SGDiS000002193. GPR1.

Phylogenomic databases

InParanoidiQ12361.
KOiK12762.
OMAiAWCYLPP.
OrthoDBiEOG7VTDZ0.

Enzyme and pathway databases

BioCyciYEAST:G3O-29459-MONOMER.

Miscellaneous databases

PROiQ12361.

Family and domain databases

InterProiIPR023041. Glucose_rcpt_Git3_N.
IPR022596. GPR1_C.
[Graphical view]
PfamiPF11710. Git3. 1 hit.
PF11970. GPR_Gpa2_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "GPR1 encodes a putative G protein-coupled receptor that associates with the Gpa2p Galpha subunit and functions in a Ras-independent pathway."
    Xue Y., Batlle M., Hirsch J.P.
    EMBO J. 17:1996-2007(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
  2. "The sequence of a 36.7 kb segment on the left arm of chromosome IV from Saccharomyces cerevisiae reveals 20 non-overlapping open reading frames (ORFs) including SIT4, FAD1, NAM1, RNA11, SIR2, NAT1, PRP9, ACT2 and MPS1 and 11 new ORFs."
    Saren A.-M., Laamanen P., Lejarcegui J.B., Paulin L.
    Yeast 13:65-71(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGPR1_YEAST
AccessioniPrimary (citable) accession number: Q12361
Secondary accession number(s): D6VRV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.