GPR12_HUMAN
ID GPR12_HUMAN Reviewed; 334 AA.
AC P47775; Q5T8P3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=G-protein coupled receptor 12;
GN Name=GPR12;
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 [GENOMIC DNA].
RX PubMed=8530049; DOI=10.1006/geno.1995.1154;
RA Song Z.-H., Modi W., Bonner T.I.;
RT "Molecular cloning and chromosomal localization of human genes encoding
RT three closely related G protein-coupled receptors.";
RL Genomics 28:347-349(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PRELIMINARY FUNCTION.
RX PubMed=12220620; DOI=10.1016/s0898-6568(02)00041-4;
RA Uhlenbrock K., Gassenhuber J., Kostenis E.;
RT "Sphingosine 1-phosphate is a ligand of the human gpr3, gpr6 and gpr12
RT family of constitutively active G protein-coupled receptors.";
RL Cell. Signal. 14:941-953(2002).
RN [5]
RP LACK OF FUNCTION AS A SPHINGOSINE 1-PHOSPHATE RECEPTOR.
RX PubMed=19286662; DOI=10.1074/jbc.m806516200;
RA Yin H., Chu A., Li W., Wang B., Shelton F., Otero F., Nguyen D.G.,
RA Caldwell J.S., Chen Y.A.;
RT "Lipid G protein-coupled receptor ligand identification using beta-arrestin
RT PathHunter assay.";
RL J. Biol. Chem. 284:12328-12338(2009).
CC -!- FUNCTION: Promotes neurite outgrowth and blocks myelin inhibition in
CC neurons (By similarity). Receptor with constitutive G(s) signaling
CC activity that stimulates cyclic AMP production. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: Was originally (PubMed:12220620) thought to be a receptor for
CC sphingosine 1-phosphate. It has been demonstrated that it is not the
CC case in human (PubMed:19286662). {ECO:0000305|PubMed:12220620,
CC ECO:0000305|PubMed:19286662}.
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DR EMBL; U18548; AAA91630.1; -; Genomic_DNA.
DR EMBL; AL159978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067448; AAH67448.1; -; mRNA.
DR EMBL; BC067452; AAH67452.1; -; mRNA.
DR EMBL; BC112144; AAI12145.1; -; mRNA.
DR EMBL; BC112146; AAI12147.1; -; mRNA.
DR CCDS; CCDS9319.1; -.
DR RefSeq; NP_005279.1; NM_005288.3.
DR AlphaFoldDB; P47775; -.
DR SMR; P47775; -.
DR BioGRID; 109096; 109.
DR IntAct; P47775; 1.
DR STRING; 9606.ENSP00000384932; -.
DR ChEMBL; CHEMBL5006; -.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB14011; Nabiximols.
DR GuidetoPHARMACOLOGY; 86; -.
DR GlyGen; P47775; 2 sites.
DR iPTMnet; P47775; -.
DR PhosphoSitePlus; P47775; -.
DR BioMuta; GPR12; -.
DR DMDM; 1346168; -.
DR MassIVE; P47775; -.
DR PaxDb; P47775; -.
DR PeptideAtlas; P47775; -.
DR PRIDE; P47775; -.
DR Antibodypedia; 7292; 302 antibodies from 31 providers.
DR DNASU; 2835; -.
DR Ensembl; ENST00000381436.2; ENSP00000370844.2; ENSG00000132975.8.
DR Ensembl; ENST00000405846.5; ENSP00000384932.3; ENSG00000132975.8.
DR GeneID; 2835; -.
DR KEGG; hsa:2835; -.
DR MANE-Select; ENST00000405846.5; ENSP00000384932.3; NM_005288.4; NP_005279.1.
DR UCSC; uc010aal.5; human.
DR CTD; 2835; -.
DR DisGeNET; 2835; -.
DR GeneCards; GPR12; -.
DR HGNC; HGNC:4466; GPR12.
DR HPA; ENSG00000132975; Group enriched (brain, retina, salivary gland, skin).
DR MIM; 600752; gene.
DR neXtProt; NX_P47775; -.
DR OpenTargets; ENSG00000132975; -.
DR PharmGKB; PA28856; -.
DR VEuPathDB; HostDB:ENSG00000132975; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01000000214392; -.
DR HOGENOM; CLU_065071_0_0_1; -.
DR InParanoid; P47775; -.
DR OMA; ELIVNPW; -.
DR OrthoDB; 903801at2759; -.
DR PhylomeDB; P47775; -.
DR TreeFam; TF330052; -.
DR PathwayCommons; P47775; -.
DR SignaLink; P47775; -.
DR BioGRID-ORCS; 2835; 13 hits in 1065 CRISPR screens.
DR GeneWiki; GPR12; -.
DR GenomeRNAi; 2835; -.
DR Pharos; P47775; Tbio.
DR PRO; PR:P47775; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P47775; protein.
DR Bgee; ENSG00000132975; Expressed in cortical plate and 76 other tissues.
DR ExpressionAtlas; P47775; baseline and differential.
DR Genevisible; P47775; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0031210; F:phosphatidylcholine binding; IEA:Ensembl.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000599; GPR12.
DR InterPro; IPR000723; GPR_3/6/12_orphan.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00650; GPR12ORPHANR.
DR PRINTS; PR00644; GPRORPHANR.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..334
FT /note="G-protein coupled receptor 12"
FT /id="PRO_0000069527"
FT TOPO_DOM 1..48
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..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..282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT LIPID 317
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 334 AA; 36730 MW; 618334A6582D744B CRC64;
MNEDLKVNLS GLPRDYLDAA AAENISAAVS SRVPAVEPEP ELVVNPWDIV LCTSGTLISC
ENAIVVLIIF HNPSLRAPMF LLIGSLALAD LLAGIGLITN FVFAYLLQSE ATKLVTIGLI
VASFSASVCS LLAITVDRYL SLYYALTYHS ERTVTFTYVM LVMLWGTSIC LGLLPVMGWN
CLRDESTCSV VRPLTKNNAA ILSVSFLFMF ALMLQLYIQI CKIVMRHAHQ IALQHHFLAT
SHYVTTRKGV STLAIILGTF AACWMPFTLY SLIADYTYPS IYTYATLLPA TYNSIINPVI
YAFRNQEIQK ALCLICCGCI PSSLAQRARS PSDV
