GPR6_MOUSE
ID GPR6_MOUSE Reviewed; 363 AA.
AC Q6YNI2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=G-protein coupled receptor 6;
DE AltName: Full=Sphingosine 1-phosphate receptor GPR6;
GN Name=Gpr6; Synonyms=Gm233;
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], AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=14592418; DOI=10.1016/j.bbrc.2003.10.006;
RA Ignatov A., Lintzel J., Kreienkamp H.J., Schaller H.C.;
RT "Sphingosine-1-phosphate is a high-affinity ligand for the G protein-
RT coupled receptor GPR6 from mouse and induces intracellular Ca2+ release by
RT activating the sphingosine-kinase pathway.";
RL Biochem. Biophys. Res. Commun. 311:329-336(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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).
RN [4]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17934457; DOI=10.1038/nn1987;
RA Lobo M.K., Cui Y., Ostlund S.B., Balleine B.W., Yang X.W.;
RT "Genetic control of instrumental conditioning by striatopallidal neuron-
RT specific S1P receptor Gpr6.";
RL Nat. Neurosci. 10:1395-1397(2007).
CC -!- FUNCTION: Orphan receptor with constitutive G(s) signaling activity
CC that activate cyclic AMP. Promotes neurite outgrowth and blocks myelin
CC inhibition in neurons (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:14592418}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17284443};
CC Multi-pass membrane protein {ECO:0000305|PubMed:17284443}. Note=Highly
CC expressed and localized along the cytoplasmic membrane as well as in a
CC perinuclear compartment.
CC -!- TISSUE SPECIFICITY: Mainly expressed in the brain. Selectively
CC expressed in striatopallidal neurons in the striatum.
CC {ECO:0000269|PubMed:17284443, ECO:0000269|PubMed:17934457}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice show reduced striatal cyclic AMP
CC production and selective alterations in instrumental conditioning.
CC {ECO:0000269|PubMed:17934457}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: Was originally (PubMed:14592418) thought to be a receptor for
CC sphingosine 1-phosphate. It has been demonstrated that it is not the
CC case in human. {ECO:0000305|PubMed:14592418}.
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DR EMBL; AY064488; AAL40876.1; -; mRNA.
DR EMBL; AK139367; BAE23977.1; -; mRNA.
DR CCDS; CCDS23802.1; -.
DR RefSeq; NP_951013.1; NM_199058.1.
DR RefSeq; XP_006512596.1; XM_006512533.2.
DR AlphaFoldDB; Q6YNI2; -.
DR SMR; Q6YNI2; -.
DR STRING; 10090.ENSMUSP00000057323; -.
DR GuidetoPHARMACOLOGY; 85; -.
DR GlyGen; Q6YNI2; 3 sites.
DR PhosphoSitePlus; Q6YNI2; -.
DR PaxDb; Q6YNI2; -.
DR PRIDE; Q6YNI2; -.
DR Antibodypedia; 19237; 117 antibodies from 27 providers.
DR DNASU; 140741; -.
DR Ensembl; ENSMUST00000061796; ENSMUSP00000057323; ENSMUSG00000046922.
DR GeneID; 140741; -.
DR KEGG; mmu:140741; -.
DR UCSC; uc007exj.1; mouse.
DR CTD; 2830; -.
DR MGI; MGI:2155249; Gpr6.
DR VEuPathDB; HostDB:ENSMUSG00000046922; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01000000214392; -.
DR HOGENOM; CLU_065071_0_0_1; -.
DR InParanoid; Q6YNI2; -.
DR OMA; YCVVGDP; -.
DR OrthoDB; 903801at2759; -.
DR PhylomeDB; Q6YNI2; -.
DR TreeFam; TF330052; -.
DR BioGRID-ORCS; 140741; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q6YNI2; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6YNI2; protein.
DR Bgee; ENSMUSG00000046922; Expressed in dorsal striatum and 51 other tissues.
DR Genevisible; Q6YNI2; 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:0038036; F:sphingosine-1-phosphate receptor activity; IDA:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; 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; IPR001151; GPR6.
DR InterPro; IPR000723; GPR_3/6/12_orphan.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00649; GPR6ORPHANR.
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..363
FT /note="G-protein coupled receptor 6"
FT /id="PRO_0000069515"
FT TOPO_DOM 1..75
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..95
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..131
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..143
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..165
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..206
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..250
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..305
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..332
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT LIPID 346
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 363 AA; 38085 MW; 6870FF769BAAF093 CRC64;
MNASAAALNE SQVVAVAAEG AAAAATAAGA PDTGEWGPPA ASAALGGGGG PNGSLELSSQ
LPAGPSGLLL SAVNPWDVLL CVSGTVIAGE NALVVALIAS TPALRTPMFV LVGSLATADL
LAGCGLILHF VFQYVVPSET VSLLMVGFLV ASFAASVSSL LAITVDRYLS LYNALTYYSR
RTLLGVHLLL AATWTVSLGL GLLPVLGWNC LADRTSCSVV RPLTRSHVAL LSTSFFVVFG
IMLHLYVRIC QVVWRHAHQI ALQQHCLAPP HLAATRKGVG TLAVVLGTFG ASWLPFAIYC
VVGSQEDPAI YTYATLLPAT YNSMINPIIY AFRNQEIQRA LWLLFCGCFQ SKVPFRSRSP
SEV
