GPC6A_BOVIN
ID GPC6A_BOVIN Reviewed; 888 AA.
AC E1BPQ3;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=G-protein coupled receptor family C group 6 member A;
DE Flags: Precursor;
GN Name=GPRC6A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
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}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; AAFC03094794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03122240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BPQ3; -.
DR SMR; E1BPQ3; -.
DR PRIDE; E1BPQ3; -.
DR InParanoid; E1BPQ3; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
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; IPR004073; GPCR_3_vmron_rcpt_2.
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; PR00248; GPCRMGR.
DR PRINTS; PR01535; VOMERONASL2R.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..888
FT /note="G-protein coupled receptor family C group 6 member
FT A"
FT /id="PRO_0000403981"
FT TOPO_DOM 16..568
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..641
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 663..676
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 677..697
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 698..718
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 719..739
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 740..754
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..775
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 776..779
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 780..800
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 801..888
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 127
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 888 AA; 99778 MW; 9A4E0582E2385AB6 CRC64;
MALLMTCFVI VFAASQPCQT PDDLVAAASP GHIMIGGLFA IHEKILSSEE PRKPEIQKCA
SFEIPTFLQT LAMIHSIEMI NNSTLLSGVK LGYEIYDTCT DITVAMAAAL RCVSKFNSSR
EIVEFKCDYS NYVPRVKAVI GAGYSEISMA VSRTLSLQLM PQVSYESTAE TLSDKIQFPS
FLRSVSSDFY QTKAMAHLIQ KSGWIIGILT TDDDYGLNTL AVQTAANNVC IAFREALPAF
RSDITIEVRI NQTLERTIAE AKVNVIVVFL SQFHVFNLFS KAIERNINKI WIVSSWSTST
IATIPDVKRI GKVVGFTFRR GNVSSFQSFL QNLCVFPSDN NKPLNEHAML SACAHAKDSD
LSQCVSNCSQ GTLATKDSER NFFLRTDFLW DYTELGLVHS IQLAVLALSY AIQDLQADFQ
PWELLAVLKN VTFMEGWSSF HFYAHGAMNT GYNIVLWREI NGHMSIKMAQ YDLKNDVFIV
TNQETKNEHR NLKKIQSKFF KECSSGQMKK TTKSQHTCCY ECVTCPENHY SNQTDTDHYL
LYNNETHWAP VGSTMCFEKE MEYLDSLAIL LLALSLLGIL FVLAIGIIFT RNLNTPVVKS
SGELMVRYVI LFCHFLNFAG TGFFIREPQS FTCKTRQTLI CMSFTLCISY ILMKSLKILL
AFSSKLQNFL KCFYKPIPII FTCTGIVVVC TLLIFAAPAV GQNVSLPRVI IFECEEGSIL
AFGSMLGYAA ILAFMCFICA FKGRKFPENY NEAKFITFGM LIYFIAWITF IPIYTFGKYM
LVVEIIIILI SNYGICCMFF PKCYVILSKQ ETNTKSVFLK MIYSYSPHSA GSLAMSHSNI
TITNRTSAGG SAVQQKSRDL QLQGFAHICR ENAMCRTKAL PPKRISSI
