GPR12_MOUSE
ID GPR12_MOUSE Reviewed; 334 AA.
AC P35412;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=G-protein coupled receptor 12;
DE AltName: Full=GPCR01;
GN Name=Gpr12; Synonyms=Gpcr12;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8262253; DOI=10.1016/0014-5793(93)80828-i;
RA Saeki Y., Ueno S., Mizuno R., Nishimura T., Fujimura H., Nagai Y.,
RA Yanagihara T.;
RT "Molecular cloning of a novel putative G protein-coupled receptor (GPCR21)
RT which is expressed predominantly in mouse central nervous system.";
RL FEBS Lett. 336:317-322(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP PRELIMINARY FUNCTION.
RX PubMed=12574419; DOI=10.1523/jneurosci.23-03-00907.2003;
RA Ignatov A., Lintzel J., Hermans-Borgmeyer I., Kreienkamp H.J., Joost P.,
RA Thomsen S., Methner A., Schaller H.C.;
RT "Role of the G-protein-coupled receptor GPR12 as high-affinity receptor for
RT sphingosylphosphorylcholine and its expression and function in brain
RT development.";
RL J. Neurosci. 23:907-914(2003).
CC -!- FUNCTION: Receptor with constitutive G(s) signaling activity that
CC stimulates cyclic AMP production (By similarity). Promotes neurite
CC outgrowth and blocks myelin inhibition in neurons. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the forebrain and a
CC lesser extent in the hindbrain. Lower expression in the liver.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: Was originally thought to be a receptor for sphingosine 1-
CC phosphate. {ECO:0000305|PubMed:12574419}.
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DR EMBL; D21061; BAA04640.1; -; mRNA.
DR EMBL; BC055746; AAH55746.1; -; mRNA.
DR CCDS; CCDS19871.1; -.
DR RefSeq; NP_001010941.1; NM_001010941.2.
DR RefSeq; NP_032177.1; NM_008151.3.
DR RefSeq; XP_006504869.1; XM_006504806.3.
DR RefSeq; XP_011239304.1; XM_011241002.2.
DR AlphaFoldDB; P35412; -.
DR SMR; P35412; -.
DR STRING; 10090.ENSMUSP00000038245; -.
DR GlyGen; P35412; 2 sites.
DR PhosphoSitePlus; P35412; -.
DR PaxDb; P35412; -.
DR PRIDE; P35412; -.
DR ProteomicsDB; 271355; -.
DR Antibodypedia; 7292; 302 antibodies from 31 providers.
DR DNASU; 14738; -.
DR Ensembl; ENSMUST00000036211; ENSMUSP00000038245; ENSMUSG00000041468.
DR Ensembl; ENSMUST00000197431; ENSMUSP00000142889; ENSMUSG00000041468.
DR GeneID; 14738; -.
DR KEGG; mmu:14738; -.
DR UCSC; uc009ani.1; mouse.
DR CTD; 2835; -.
DR MGI; MGI:101909; Gpr12.
DR VEuPathDB; HostDB:ENSMUSG00000041468; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01000000214392; -.
DR HOGENOM; CLU_065071_0_0_1; -.
DR InParanoid; P35412; -.
DR OMA; ELIVNPW; -.
DR OrthoDB; 903801at2759; -.
DR PhylomeDB; P35412; -.
DR TreeFam; TF330052; -.
DR BioGRID-ORCS; 14738; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Gpr12; mouse.
DR PRO; PR:P35412; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P35412; protein.
DR Bgee; ENSMUSG00000041468; Expressed in perirhinal cortex and 59 other tissues.
DR ExpressionAtlas; P35412; baseline and differential.
DR Genevisible; P35412; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
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 2: Evidence at transcript 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_0000069528"
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..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..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; 36589 MW; 3BE0EE4371F55F5B CRC64;
MNEDPKVNLS GLPRDCIDAG APENISAAVP SQGSVAESEP ELVVNPWDIV LCSSGTLICC
ENAVVVLIIF HSPSLRAPMF LLIGSLALAD LLAGLGLIIN FVFAYLLQSE ATKLVTIGLI
VASFSASVCS LLAITVDRYL SLYYALTYHS ERTVTFTYVM LVMLWGTSIC LGLLPVMGWN
CLRDESTCSV VRPLTKNNAA ILSISFLFMF ALMLQLYIQI CKIVMRHAHQ IALQHHFLAT
SHYVTTRKGV STLALILGTF AACWMPFTLY SLIADYTYPS IYTYATLLPA TYNSIINPVI
YAFRNQEIQK ALCLICCGCI PSSLSQRARS PSDV
