GPR6_RAT
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 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=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}.
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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 GlyGen; P51651; 3 sites.
DR iPTMnet; P51651; -.
DR PhosphoSitePlus; P51651; -.
DR PaxDb; P51651; -.
DR Ensembl; ENSRNOT00000073276; ENSRNOP00000067254; ENSRNOG00000049580.
DR GeneID; 83683; -.
DR KEGG; rno:83683; -.
DR CTD; 2830; -.
DR RGD; 70939; Gpr6.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01000000214392; -.
DR HOGENOM; CLU_065071_0_0_1; -.
DR InParanoid; P51651; -.
DR OMA; YCVVGDP; -.
DR OrthoDB; 903801at2759; -.
DR PhylomeDB; P51651; -.
DR PRO; PR:P51651; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000049580; Expressed in duodenum and 4 other tissues.
DR Genevisible; P51651; 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: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 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_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
