ID   GPC6A_RAT               Reviewed;         928 AA.
AC   Q70VB1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=G-protein coupled receptor family C group 6 member A;
DE   Flags: Precursor;
GN   Name=Gprc6a;
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], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP   LOCATION, AND GLYCOSYLATION.
RC   STRAIN=Wistar; TISSUE=Circumvallate papilla;
RX   PubMed=17478059; DOI=10.1016/j.gene.2007.03.008;
RA   Wellendorph P., Burhenne N., Christiansen B., Walter B., Schmale H.,
RA   Brauner-Osborne H.;
RT   "The rat GPRC6A: cloning and characterization.";
RL   Gene 396:257-267(2007).
CC   -!- FUNCTION: Receptor activated by multiple ligands, including osteocalcin
CC       (BGLAP), basic amino acids, and various cations (By similarity).
CC       Activated by amino acids with a preference for basic amino acids such
CC       as L-Lys, L-Arg and L-ornithine but also by small and polar amino acids
CC       (PubMed:17478059). The L-alpha amino acids respond is augmented by
CC       divalent cations Ca(2+) and Mg(2+) (By similarity). Seems to act
CC       through a G(q)/G(11) and G(i)-coupled pathway (By similarity).
CC       Regulates testosterone production by acting as a ligand for
CC       uncarboxylated osteocalcin hormone: osteocalcin-binding at the surface
CC       of Leydig cells initiates a signaling response that promotes the
CC       expression of enzymes required for testosterone synthesis in a CREB-
CC       dependent manner (By similarity). Mediates the non-genomic effects of
CC       androgens in multiple tissue (By similarity). May coordinate
CC       nutritional and hormonal anabolic signals through the sensing of
CC       extracellular amino acids, osteocalcin, divalent ions and its
CC       responsiveness to anabolic steroids (By similarity).
CC       {ECO:0000250|UniProtKB:Q8K4Z6, ECO:0000269|PubMed:17478059}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q8K4Z6}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17478059};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:17478059}.
CC   -!- TISSUE SPECIFICITY: High expression in soft palate. Weak expression in
CC       kidney, liver, lung and brain. No expression detected in heart, testis,
CC       skeletal muscle amd spleen. {ECO:0000269|PubMed:17478059}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17478059}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ535460; CAD59483.1; -; mRNA.
DR   RefSeq; NP_001258035.1; NM_001271106.1.
DR   AlphaFoldDB; Q70VB1; -.
DR   SMR; Q70VB1; -.
DR   MINT; Q70VB1; -.
DR   STRING; 10116.ENSRNOP00000000451; -.
DR   GlyCosmos; Q70VB1; 2 sites, No reported glycans.
DR   GlyGen; Q70VB1; 2 sites.
DR   PhosphoSitePlus; Q70VB1; -.
DR   PaxDb; 10116-ENSRNOP00000000451; -.
DR   Ensembl; ENSRNOT00000000451.6; ENSRNOP00000000451.3; ENSRNOG00000000401.8.
DR   Ensembl; ENSRNOT00055025717; ENSRNOP00055020984; ENSRNOG00055015033.
DR   Ensembl; ENSRNOT00060012928; ENSRNOP00060009806; ENSRNOG00060007836.
DR   Ensembl; ENSRNOT00065004560; ENSRNOP00065003261; ENSRNOG00065003223.
DR   GeneID; 294394; -.
DR   KEGG; rno:294394; -.
DR   UCSC; RGD:735077; rat.
DR   AGR; RGD:735077; -.
DR   CTD; 222545; -.
DR   RGD; 735077; Gprc6a.
DR   eggNOG; KOG1056; Eukaryota.
DR   GeneTree; ENSGT00940000158416; -.
DR   HOGENOM; CLU_005389_1_0_1; -.
DR   InParanoid; Q70VB1; -.
DR   OMA; ICFICAF; -.
DR   OrthoDB; 4224743at2759; -.
DR   PhylomeDB; Q70VB1; -.
DR   TreeFam; TF331269; -.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   Reactome; R-RNO-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR   PRO; PR:Q70VB1; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR   GO; GO:2000224; P:regulation of testosterone biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0043200; P:response to amino acid; ISO:RGD.
DR   CDD; cd06361; PBP1_GPC6A-like; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 2.10.50.30; GPCR, family 3, nine cysteines domain; 1.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR000337; GPCR_3.
DR   InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR   InterPro; IPR038550; GPCR_3_9-Cys_sf.
DR   InterPro; IPR017978; GPCR_3_C.
DR   InterPro; IPR000068; GPCR_3_Ca_sens_rcpt-rel.
DR   InterPro; IPR017979; GPCR_3_CS.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   PANTHER; PTHR24061; CALCIUM-SENSING RECEPTOR-RELATED; 1.
DR   PANTHER; PTHR24061:SF5; G-PROTEIN COUPLED RECEPTOR FAMILY C GROUP 6 MEMBER A; 1.
DR   Pfam; PF00003; 7tm_3; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF07562; NCD3G; 1.
DR   PRINTS; PR00592; CASENSINGR.
DR   PRINTS; PR00248; GPCRMGR.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..928
FT                   /note="G-protein coupled receptor family C group 6 member
FT                   A"
FT                   /id="PRO_0000043198"
FT   TOPO_DOM        21..594
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        595..615
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        616..630
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        631..651
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        652..669
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        670..690
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        691..706
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        707..727
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        728..750
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        751..771
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        772..784
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        785..805
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        806..812
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        813..833
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        834..928
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        555
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        131
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   928 AA;  104353 MW;  0B13BF36E6A60BC4 CRC64;
     MALSFVFITC FMILLDTSQS CHTPDDFVAI TSPGHIMIGG LFAIHEKMLS SDDHPRQPQI
     QKCVGFEISV FLQTLAMIHS IEMINNSSLL SGVKLGYEIY DTCTEVTAAM AATLRFLSKF
     NCSRETVIFQ CDYSSYVPRV KAIIGAGYSE ISMAVSRMLN LQLMPQVSYE STAEILSDKI
     RFPSFLRTVP SDFYQTKAMA HLIRQSGWNW VGAITTDDDY GRLALNTFAI QAAENNVCIA
     FKEVLPAFLS DNTIEVRINQ TLEKIIAEAQ VNVIVVFLRK FHVFNLFNKA IERKISKIWI
     ASDNWSTAAK IITIPNVKKL GKVVGFTFRR GNMSSFHSFL QTLHMYPSDN NKPLHEFAML
     FSACKHIKDG DLSQCISNYS QATWTYDTTK TIETHLFKRN DFLWHYTEPG LIHSIQLAVL
     ALGHAIRDLC QDRDCQKPNA FQPWELLAVL KNVTFTDGKN SFHFDAHGDL NTGYEVVLWK
     ETNGLMTVTK MAEYDLQHDV FITTNQETKH EFRKLKQILS KCSKECIPGQ MKKATGSQHS
     CCYECVNCPE NHYSNETDMD HCLVCNNETH WAPVRSTMCF EKEVEYLDWD DSLALLLIAL
     SLLGIAFVLA VGIIFTRNLK TPVVKSSGGL VVCYVMLACH ALNFASTGFF IGEPQDFTCK
     TRQTLFGVSF TLCVSCILTK SLKILLAFSF DPTLKTFLKC LYRPVPIVLT CTGIQVVICT
     LWLVLAAPTV EENTSLPRVI ILECEEGSAL AFGTMLGYIA VLAFICFVFA FKGRKLPENY
     NEAKFLTFGM LIYFIAWITF IPVYATTFGK YLPAVEIIVI LISNYGILCC TFFPKCYIIL
     CKQKTNTKSV FLQMVYNYSA HSVDSLALSH VSLDSASHST ATTNPRPGNK TAACQNYKHL
     PVQVLAHTGM EKTMHASKTL HQKRSSSI
//