ID GPR6_RAT Reviewed; 363 AA. AC P51651; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 134. DE RecName: Full=G-protein coupled receptor 6; DE AltName: Full=Sphingosine 1-phosphate receptor GPR6; GN Name=Gpr6; Synonyms=Cnl3; 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=Brain cortex; RX PubMed=8082799; DOI=10.1016/0014-5793(94)00888-4; RA Song Z.-H., Young W.S. III, Brownstein M.J., Bonner T.I.; RT "Molecular cloning of a novel candidate G protein-coupled receptor from rat RT brain."; RL FEBS Lett. 351:375-379(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=11169503; RX DOI=10.1002/1097-4695(20010215)46:3<167::aid-neu1000>3.0.co;2-j; RA Chenn A., Levin M.E., McConnell S.K.; RT "Temporally and spatially regulated expression of a candidate G-protein- RT coupled receptor during cerebral cortical development."; RL J. Neurobiol. 46:167-177(2001). RN [3] RP FUNCTION, AND DEVELOPMENTAL STAGE. 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: Orphan receptor with constitutive G(s) signaling activity CC that activate 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}. Note=Detected in the intracellular compartments. CC It is currently unclear whether this is a cell surface or intracellular CC receptor (By similarity). {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in the brain, with a prominent CC distribution in striatum. {ECO:0000269|PubMed:8082799}. CC -!- DEVELOPMENTAL STAGE: Abundantly expressed in granule neurons at all CC developmental stages. {ECO:0000269|PubMed:17284443}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U12006; AAA21870.1; -; mRNA. DR EMBL; AF064706; AAC16886.1; -; mRNA. DR PIR; S48697; S48697. DR RefSeq; NP_113994.1; NM_031806.1. DR AlphaFoldDB; P51651; -. DR SMR; P51651; -. DR STRING; 10116.ENSRNOP00000067254; -. DR GlyCosmos; P51651; 3 sites, No reported glycans. DR GlyGen; P51651; 3 sites. DR iPTMnet; P51651; -. DR PhosphoSitePlus; P51651; -. DR PaxDb; 10116-ENSRNOP00000067254; -. DR Ensembl; ENSRNOT00000073276.2; ENSRNOP00000067254.1; ENSRNOG00000049580.2. DR Ensembl; ENSRNOT00055001158; ENSRNOP00055000913; ENSRNOG00055000679. DR Ensembl; ENSRNOT00060011533; ENSRNOP00060008654; ENSRNOG00060007021. DR Ensembl; ENSRNOT00065013790; ENSRNOP00065010239; ENSRNOG00065008683. DR GeneID; 83683; -. DR KEGG; rno:83683; -. DR AGR; RGD:70939; -. DR CTD; 2830; -. DR RGD; 70939; Gpr6. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01060000248564; -. DR HOGENOM; CLU_065071_0_0_1; -. DR InParanoid; P51651; -. DR OMA; YCVVGDP; -. DR OrthoDB; 5397365at2759; -. DR PhylomeDB; P51651; -. DR PRO; PR:P51651; -. DR Proteomes; UP000002494; Chromosome 20. DR Bgee; ENSRNOG00000049580; Expressed in duodenum and 4 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; ISO:RGD. 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:RGD. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:RGD. DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central. DR GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; ISO:RGD. 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; P51651; RN. 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_0000069516" 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 28..51 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; 38115 MW; 4B2E665C0BAB2B78 CRC64; MNASAAALNE SQVVAVAAEG AAAAATAAGT PDTSEWGPPA ASAALGGGGG PNGSLELSSQ LPAGPSGLLL SAVNPWDVLL CVSGTVIAGE NALVVALIAS TPALRTPMFV LVGSLATADL LAGCGLILHF VFQYVVPSET VSLLMVGFLV ASFAASVSSL LAITVDRYLS LYNALTYYSR RTLLGVHLLL AATWTVSLGL GLLPVLGWNC LADRASCSVV RPLTRSHVAL LSTSFFVVFG IMLHLYVRIC QVVWRHAHQI ALQQHCLAPP HLAATRKGVG TLAVVLGTFG ASWLPFAIYC VVGSQEDPAI YTYATLLPAT YNSMINPIIY AFRNQEIQRA LWLLFCGCFQ SKVPFRSRSP SEV //