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   24-JAN-2024, entry version 133.
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   GlyCosmos; Q6YNI2; 3 sites, No reported glycans.
DR   GlyGen; Q6YNI2; 3 sites.
DR   PhosphoSitePlus; Q6YNI2; -.
DR   PaxDb; 10090-ENSMUSP00000057323; -.
DR   Antibodypedia; 19237; 128 antibodies from 27 providers.
DR   DNASU; 140741; -.
DR   Ensembl; ENSMUST00000061796.8; ENSMUSP00000057323.7; ENSMUSG00000046922.8.
DR   GeneID; 140741; -.
DR   KEGG; mmu:140741; -.
DR   UCSC; uc007exj.1; mouse.
DR   AGR; MGI:2155249; -.
DR   CTD; 2830; -.
DR   MGI; MGI:2155249; Gpr6.
DR   VEuPathDB; HostDB:ENSMUSG00000046922; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01060000248564; -.
DR   HOGENOM; CLU_065071_0_0_1; -.
DR   InParanoid; Q6YNI2; -.
DR   OMA; YCVVGDP; -.
DR   OrthoDB; 5397365at2759; -.
DR   PhylomeDB; Q6YNI2; -.
DR   TreeFam; TF330052; -.
DR   BioGRID-ORCS; 140741; 4 hits in 77 CRISPR screens.
DR   PRO; PR:Q6YNI2; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q6YNI2; Protein.
DR   Bgee; ENSMUSG00000046922; Expressed in dorsal striatum and 52 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; 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   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001151; GPR6.
DR   InterPro; IPR000723; GPR_3/6/12_orphan.
DR   PANTHER; PTHR22750; G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR22750:SF19; G-PROTEIN COUPLED RECEPTOR 6; 1.
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   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; Q6YNI2; MM.
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
//