GPR12_RAT
ID GPR12_RAT Reviewed; 334 AA.
AC P30951; A0JPJ1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=G-protein coupled receptor 12;
DE AltName: Full=R334;
GN Name=Gpr12; Synonyms=Gpcr12;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Pituitary;
RX PubMed=1840531; DOI=10.1016/0014-5793(91)80876-5;
RA Eidne K.A., Zabavnik J., Peters T., Yoshida S., Anderson L., Taylor P.L.;
RT "Cloning, sequencing and tissue distribution of a candidate G protein-
RT coupled receptor from rat pituitary gland.";
RL FEBS Lett. 292:243-248(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Bonner T.I., Brownstein M.J.;
RT "A putative rat G protein coupled receptor cDNA isolated from cerebral
RT cortex.";
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17284443; DOI=10.1074/jbc.m700911200;
RA Tanaka S., Ishii K., Kasai K., Yoon S.O., Saeki Y.;
RT "Neural expression of G protein-coupled receptors GPR3, GPR6, and GPR12 up-
RT regulates cyclic AMP levels and promotes neurite outgrowth.";
RL J. Biol. Chem. 282:10506-10515(2007).
CC -!- FUNCTION: Receptor with constitutive G(s) signaling activity that
CC activates cyclic AMP. Promotes neurite outgrowth and blocks myelin
CC inhibition in neurons. {ECO:0000269|PubMed:17284443}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, pituitary gland and testis.
CC {ECO:0000269|PubMed:17284443, ECO:0000269|PubMed:1840531}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA43713.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X61496; CAA43713.1; ALT_FRAME; mRNA.
DR EMBL; U12184; AAB60518.1; -; mRNA.
DR EMBL; BC127447; AAI27448.1; -; mRNA.
DR PIR; S18444; S18444.
DR RefSeq; NP_001032372.1; NM_001037295.1.
DR RefSeq; NP_110458.1; NM_030831.1.
DR RefSeq; XP_017453953.1; XM_017598464.1.
DR AlphaFoldDB; P30951; -.
DR SMR; P30951; -.
DR STRING; 10116.ENSRNOP00000057844; -.
DR GlyGen; P30951; 2 sites.
DR PhosphoSitePlus; P30951; -.
DR PaxDb; P30951; -.
DR Ensembl; ENSRNOT00000061129; ENSRNOP00000057844; ENSRNOG00000039832.
DR Ensembl; ENSRNOT00000092720; ENSRNOP00000075912; ENSRNOG00000039832.
DR GeneID; 80840; -.
DR KEGG; rno:80840; -.
DR CTD; 2835; -.
DR RGD; 68333; Gpr12.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01000000214392; -.
DR HOGENOM; CLU_065071_0_0_1; -.
DR InParanoid; P30951; -.
DR OMA; ELIVNPW; -.
DR OrthoDB; 903801at2759; -.
DR PhylomeDB; P30951; -.
DR PRO; PR:P30951; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000039832; Expressed in Ammon's horn and 5 other tissues.
DR Genevisible; P30951; RN.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
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_0000069529"
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; 36704 MW; DFA50BEA56141E44 CRC64;
MNEDPKVNLS GLPRDCIEAG TPENISAAVP SQGSVVESEP ELVVNPWDIV LCSSGTLICC
ENAVVVLIIF HSPSLRAPMF LLIGSLALAD LLAGLGLIIN FVFAYLLQSE ATKLVTIGLI
VASFSASVCS LLAITVDRYL SLYYALTYHS ERTVTFTYVM LVMLWGTSTC LGLLPVMGWN
CLRDESTCSV VRPLTKNNAA ILSISFLFMF ALMLQLYIQI CKIVMRHAHQ IALQHHFLAT
SHYVTTRKGI STLALILGTF AACWMPFTLY SLIADYTYPS IYTYATLLPA TYNSIINPVI
YAFRNQEIQK ALCLICCGCI PNTLSQRARS PSDV
