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GPC6A_RAT
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   03-AUG-2022, entry version 112.
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 amino acids with a preference for basic
CC       amino acids such as L-Lys, L-Arg and L-ornithine but also by small and
CC       polar amino acids. The L-alpha amino acids respond is augmented by
CC       divalent cations Ca(2+) and Mg(2+). Activated by extracellular calcium
CC       and osteocalcin. Seems to act through a G(q)/G(11) and G(i)-coupled
CC       pathway. Mediates the non-genomic effects of androgens in multiple
CC       tissue. May coordinate nutritional and hormonal anabolic signals
CC       through the sensing of extracellular amino acids, osteocalcin, divalent
CC       ions and its responsiveness to anabolic steroids (By similarity).
CC       {ECO:0000250, ECO:0000269|PubMed:17478059}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
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   GlyGen; Q70VB1; 2 sites.
DR   PhosphoSitePlus; Q70VB1; -.
DR   PaxDb; Q70VB1; -.
DR   PRIDE; Q70VB1; -.
DR   Ensembl; ENSRNOT00000000451; ENSRNOP00000000451; ENSRNOG00000000401.
DR   GeneID; 294394; -.
DR   KEGG; rno:294394; -.
DR   UCSC; RGD:735077; rat.
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; VFIITDQ; -.
DR   OrthoDB; 119538at2759; -.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0043200; P:response to amino acid; ISO:RGD.
DR   Gene3D; 2.10.50.30; -; 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; PTHR24061; 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; SSF53822; 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
 
 
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