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   24-JAN-2024, entry version 176.
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   PDB; 7Y3G; EM; 2.77 A; R=1-334.
DR   PDBsum; 7Y3G; -.
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   GlyCosmos; P47775; 2 sites, No reported glycans.
DR   GlyGen; P47775; 2 sites.
DR   iPTMnet; P47775; -.
DR   PhosphoSitePlus; P47775; -.
DR   BioMuta; GPR12; -.
DR   DMDM; 1346168; -.
DR   MassIVE; P47775; -.
DR   PaxDb; 9606-ENSP00000384932; -.
DR   PeptideAtlas; P47775; -.
DR   Antibodypedia; 7292; 320 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   AGR; HGNC:4466; -.
DR   CTD; 2835; -.
DR   DisGeNET; 2835; -.
DR   GeneCards; GPR12; -.
DR   HGNC; HGNC:4466; GPR12.
DR   HPA; ENSG00000132975; Tissue enhanced (brain, retina, 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; ENSGT01060000248564; -.
DR   HOGENOM; CLU_065071_0_0_1; -.
DR   InParanoid; P47775; -.
DR   OMA; ELIVNPW; -.
DR   OrthoDB; 5397365at2759; -.
DR   PhylomeDB; P47775; -.
DR   TreeFam; TF330052; -.
DR   PathwayCommons; P47775; -.
DR   SignaLink; P47775; -.
DR   BioGRID-ORCS; 2835; 14 hits in 1143 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 cell types or tissues.
DR   ExpressionAtlas; P47775; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR   CDD; cd15961; 7tmA_GPR12; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000599; GPR12.
DR   InterPro; IPR000723; GPR_3/6/12_orphan.
DR   PANTHER; PTHR22750; G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR22750:SF8; G-PROTEIN COUPLED RECEPTOR 12; 1.
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   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; P47775; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; G-protein coupled receptor; Glycoprotein;
KW   Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW   Reference proteome; 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
//