GP151_HUMAN
ID GP151_HUMAN Reviewed; 419 AA.
AC Q8TDV0; Q86SN8; Q8NGV2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=G-protein coupled receptor 151;
DE AltName: Full=G-protein coupled receptor PGR7;
DE AltName: Full=GPCR-2037;
DE AltName: Full=Galanin receptor 4 {ECO:0000312|HGNC:HGNC:23624};
DE AltName: Full=Galanin-receptor-like protein {ECO:0000303|PubMed:15111018};
DE Short=GalRL;
GN Name=GPR151; Synonyms=GALR4, GALRL {ECO:0000303|PubMed:15111018}, PGR7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15111018; DOI=10.1016/j.neuropharm.2004.02.004;
RA Ignatov A., Hermans-Borgmeyer I., Schaller H.C.;
RT "Cloning and characterization of a novel G-protein-coupled receptor with
RT homology to galanin receptors.";
RL Neuropharmacology 46:1114-1120(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12044878; DOI=10.1016/s0014-5793(02)02775-8;
RA Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.;
RT "Identification of G protein-coupled receptor genes from the human genome
RT sequence.";
RL FEBS Lett. 520:97-101(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-274.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31119277; DOI=10.1093/jb/mvz042;
RA Mashiko M., Kurosawa A., Tani Y., Tsuji T., Takeda S.;
RT "GPR31 and GPR151 are activated under acidic conditions.";
RL J. Biochem. 0:0-0(2019).
CC -!- FUNCTION: Proton-sensing G-protein coupled receptor.
CC {ECO:0000269|PubMed:31119277}.
CC -!- INTERACTION:
CC Q8TDV0; P05090: APOD; NbExp=3; IntAct=EBI-11955647, EBI-715495;
CC Q8TDV0; Q13520: AQP6; NbExp=3; IntAct=EBI-11955647, EBI-13059134;
CC Q8TDV0; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-11955647, EBI-714543;
CC Q8TDV0; Q92843: BCL2L2; NbExp=3; IntAct=EBI-11955647, EBI-707714;
CC Q8TDV0; Q08708: CD300C; NbExp=3; IntAct=EBI-11955647, EBI-3915344;
CC Q8TDV0; O14735: CDIPT; NbExp=3; IntAct=EBI-11955647, EBI-358858;
CC Q8TDV0; Q9HA82: CERS4; NbExp=3; IntAct=EBI-11955647, EBI-2622997;
CC Q8TDV0; Q99675: CGRRF1; NbExp=3; IntAct=EBI-11955647, EBI-2130213;
CC Q8TDV0; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-11955647, EBI-6942903;
CC Q8TDV0; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-11955647, EBI-2680384;
CC Q8TDV0; P52803: EFNA5; NbExp=3; IntAct=EBI-11955647, EBI-1753674;
CC Q8TDV0; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-11955647, EBI-781551;
CC Q8TDV0; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-11955647, EBI-18304435;
CC Q8TDV0; P48165: GJA8; NbExp=3; IntAct=EBI-11955647, EBI-17458373;
CC Q8TDV0; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-11955647, EBI-11955647;
CC Q8TDV0; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-11955647, EBI-13345167;
CC Q8TDV0; Q8TED1: GPX8; NbExp=3; IntAct=EBI-11955647, EBI-11721746;
CC Q8TDV0; P24593: IGFBP5; NbExp=3; IntAct=EBI-11955647, EBI-720480;
CC Q8TDV0; Q14145: KEAP1; NbExp=3; IntAct=EBI-11955647, EBI-751001;
CC Q8TDV0; O43561-2: LAT; NbExp=3; IntAct=EBI-11955647, EBI-8070286;
CC Q8TDV0; Q9NQG1: MANBAL; NbExp=3; IntAct=EBI-11955647, EBI-3867271;
CC Q8TDV0; Q8IXM6: NRM; NbExp=3; IntAct=EBI-11955647, EBI-10262547;
CC Q8TDV0; O15173: PGRMC2; NbExp=3; IntAct=EBI-11955647, EBI-1050125;
CC Q8TDV0; Q04941: PLP2; NbExp=3; IntAct=EBI-11955647, EBI-608347;
CC Q8TDV0; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-11955647, EBI-3917235;
CC Q8TDV0; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-11955647, EBI-17247926;
CC Q8TDV0; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-11955647, EBI-18037857;
CC Q8TDV0; Q14973: SLC10A1; NbExp=3; IntAct=EBI-11955647, EBI-3923031;
CC Q8TDV0; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-11955647, EBI-18159983;
CC Q8TDV0; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-11955647, EBI-17595455;
CC Q8TDV0; Q05940: SLC18A2; NbExp=3; IntAct=EBI-11955647, EBI-18036244;
CC Q8TDV0; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-11955647, EBI-10290130;
CC Q8TDV0; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-11955647, EBI-17280858;
CC Q8TDV0; Q9UNK0: STX8; NbExp=3; IntAct=EBI-11955647, EBI-727240;
CC Q8TDV0; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-11955647, EBI-6268651;
CC Q8TDV0; P55061: TMBIM6; NbExp=3; IntAct=EBI-11955647, EBI-1045825;
CC Q8TDV0; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-11955647, EBI-11724423;
CC Q8TDV0; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-11955647, EBI-11528917;
CC Q8TDV0; A5PKU2: TUSC5; NbExp=4; IntAct=EBI-11955647, EBI-11988865;
CC Q8TDV0; Q86WB7-2: UNC93A; NbExp=3; IntAct=EBI-11955647, EBI-13356252;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:31119277};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: High expression in the spinal cord.
CC {ECO:0000269|PubMed:15111018}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC05899.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY351676; AAQ62567.1; -; mRNA.
DR EMBL; AB083592; BAB89305.1; -; Genomic_DNA.
DR EMBL; AB065674; BAC05899.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY255557; AAO85069.1; -; mRNA.
DR CCDS; CCDS34266.1; -.
DR RefSeq; NP_919227.2; NM_194251.2.
DR AlphaFoldDB; Q8TDV0; -.
DR SMR; Q8TDV0; -.
DR BioGRID; 126397; 53.
DR IntAct; Q8TDV0; 39.
DR STRING; 9606.ENSP00000308733; -.
DR ChEMBL; CHEMBL3085617; -.
DR GlyGen; Q8TDV0; 2 sites.
DR iPTMnet; Q8TDV0; -.
DR PhosphoSitePlus; Q8TDV0; -.
DR BioMuta; GPR151; -.
DR DMDM; 48428097; -.
DR MassIVE; Q8TDV0; -.
DR PaxDb; Q8TDV0; -.
DR PeptideAtlas; Q8TDV0; -.
DR PRIDE; Q8TDV0; -.
DR Antibodypedia; 15831; 322 antibodies from 29 providers.
DR DNASU; 134391; -.
DR Ensembl; ENST00000311104.3; ENSP00000308733.2; ENSG00000173250.3.
DR GeneID; 134391; -.
DR KEGG; hsa:134391; -.
DR MANE-Select; ENST00000311104.3; ENSP00000308733.2; NM_194251.3; NP_919227.2.
DR UCSC; uc003lod.2; human.
DR CTD; 134391; -.
DR DisGeNET; 134391; -.
DR GeneCards; GPR151; -.
DR HGNC; HGNC:23624; GPR151.
DR HPA; ENSG00000173250; Tissue enriched (brain).
DR MIM; 618487; gene.
DR neXtProt; NX_Q8TDV0; -.
DR PharmGKB; PA134975199; -.
DR VEuPathDB; HostDB:ENSG00000173250; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234518; -.
DR HOGENOM; CLU_053982_0_0_1; -.
DR InParanoid; Q8TDV0; -.
DR OMA; YFWRAYG; -.
DR OrthoDB; 658542at2759; -.
DR PhylomeDB; Q8TDV0; -.
DR TreeFam; TF332591; -.
DR PathwayCommons; Q8TDV0; -.
DR SignaLink; Q8TDV0; -.
DR BioGRID-ORCS; 134391; 15 hits in 1060 CRISPR screens.
DR GeneWiki; GPR151; -.
DR GenomeRNAi; 134391; -.
DR Pharos; Q8TDV0; Tbio.
DR PRO; PR:Q8TDV0; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8TDV0; protein.
DR Bgee; ENSG00000173250; Expressed in prefrontal cortex and 9 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0050778; P:positive regulation of immune response; ISS:UniProtKB.
DR GO; GO:0010447; P:response to acidic pH; IMP:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..419
FT /note="G-protein coupled receptor 151"
FT /id="PRO_0000069632"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..286
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 330..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 40
FT /note="P -> L (in dbSNP:rs17104742)"
FT /id="VAR_049404"
FT VARIANT 144
FT /note="A -> V (in dbSNP:rs7713676)"
FT /id="VAR_049405"
FT VARIANT 261
FT /note="L -> V (in dbSNP:rs7709485)"
FT /id="VAR_049406"
SQ SEQUENCE 419 AA; 46637 MW; 769780E6B1FC6140 CRC64;
MLAAAFADSN SSSMNVSFAH LHFAGGYLPS DSQDWRTIIP ALLVAVCLVG FVGNLCVIGI
LLHNAWKGKP SMIHSLILNL SLADLSLLLF SAPIRATAYS KSVWDLGWFV CKSSDWFIHT
CMAAKSLTIV VVAKVCFMYA SDPAKQVSIH NYTIWSVLVA IWTVASLLPL PEWFFSTIRH
HEGVEMCLVD VPAVAEEFMS MFGKLYPLLA FGLPLFFASF YFWRAYDQCK KRGTKTQNLR
NQIRSKQVTV MLLSIAIISA LLWLPEWVAW LWVWHLKAAG PAPPQGFIAL SQVLMFSISS
ANPLIFLVMS EEFREGLKGV WKWMITKKPP TVSESQETPA GNSEGLPDKV PSPESPASIP
EKEKPSSPSS GKGKTEKAEI PILPDVEQFW HERDTVPSVQ DNDPIPWEHE DQETGEGVK
