GPC6A_DANRE
ID GPC6A_DANRE Reviewed; 867 AA.
AC Q5U9X3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-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 AltName: Full=Odorant receptor ZO6;
DE Flags: Precursor;
GN Name=gprc6a;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF LYS-386.
RX PubMed=15537883; DOI=10.1523/jneurosci.3117-04.2004;
RA Luu P., Acher F., Bertrand H.-O., Fan J., Ngai J.;
RT "Molecular determinants of ligand selectivity in a vertebrate odorant
RT receptor.";
RL J. Neurosci. 24:10128-10137(2004).
CC -!- FUNCTION: Olfactory receptor that is activated by amino acids that act
CC as potent odorants in fish. Displays preference for acidic amino acids
CC such as Glu over basic amino acids. {ECO:0000269|PubMed:15537883}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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; AY770492; AAV51935.1; -; mRNA.
DR RefSeq; NP_001008731.1; NM_001008731.1.
DR AlphaFoldDB; Q5U9X3; -.
DR SMR; Q5U9X3; -.
DR STRING; 7955.ENSDARP00000002697; -.
DR PaxDb; Q5U9X3; -.
DR PRIDE; Q5U9X3; -.
DR Ensembl; ENSDART00000008880; ENSDARP00000002697; ENSDARG00000005371.
DR GeneID; 494131; -.
DR KEGG; dre:494131; -.
DR CTD; 222545; -.
DR ZFIN; ZDB-GENE-041217-22; gprc6a.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT00940000158416; -.
DR HOGENOM; CLU_005389_1_0_1; -.
DR InParanoid; Q5U9X3; -.
DR OMA; VFIITDQ; -.
DR OrthoDB; 119538at2759; -.
DR PhylomeDB; Q5U9X3; -.
DR TreeFam; TF331269; -.
DR Reactome; R-DRE-416476; G alpha (q) signalling events.
DR Reactome; R-DRE-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR PRO; PR:Q5U9X3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000005371; Expressed in swim bladder and 3 other tissues.
DR ExpressionAtlas; Q5U9X3; baseline.
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:0016597; F:amino acid binding; IDA:ZFIN.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0016595; F:glutamate binding; IDA:ZFIN.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:ZFIN.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
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; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Olfaction; Receptor; Reference proteome; Sensory transduction; Signal;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..867
FT /note="G-protein coupled receptor family C group 6 member
FT A"
FT /id="PRO_0000043199"
FT TOPO_DOM 20..566
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 624..634
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 635..655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 656..675
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 676..696
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 697..716
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 717..737
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 738..754
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..775
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 776..781
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 782..802
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 803..867
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 386
FT /note="Critical determinant of selectivity of acidic versus
FT basic amino acid ligands"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 386
FT /note="K->M: Induces nonselectivity for Arg and Glu."
FT /evidence="ECO:0000269|PubMed:15537883"
SQ SEQUENCE 867 AA; 97136 MW; 011AFB96DBB944A3 CRC64;
MDLMSFILLW AGLMKVAEAS IAQFSQLGAS APGNIIIGGL FPIHEAVVPV NYTGNNSISA
PEHPDCIRFY TKGLNQALAM INAVEMANKS PMLSSLNITL GYRIYDTCSD VTTALRAVHD
IMRPFSDCES PEDSSQPVQP IMAVIGTTSS EISIAVARDL NLQMIPQISY ASTATILSDK
SRFPAFMRTV PSDEYQTCAM AKLLKSNKWS WVGIIITDGD YGRSALEGFI QHTETEGICI
AFKAILPDSL ADQQKLNTDI ENTLNIIENN PKVRVVISFA KSSQMQLLFK GLQSRNISNN
MVWVASDNWS TAKHILNDGS ITDIGKVLGF TFKSGNFTSF HQYLKNLQFE SEDEMNNSFL
KEFLKLNAGN ASNTVLELMK STNLDKIFSI EMAVTAVANA VAKLCAERQC QDSTALQPWE
LLRQLRSITF ENGGEMYKFD ANGDINLGYD LFLWEGDQSD EHADDIIAEY DPTKGGFHYI
HNDLSEIKKV VSRCSNSCQP GQYKKTAEGQ HTCCYECLTC VENHYSNITD ADECSPCDSE
SMWSLANSTE CHPKVFEYFD WNSGFAIVLL ILAALGVLLL FFMSALFFWQ RHSPVVKAAG
GPLCHLILVS LLGSFISVVF FVGEPSDLTC RARQVIFGFS FTLCVSCILV KSLKILLAFE
MNFELKELLC MLYKPYMIVS VGMGVQIIIC TVWLTLYKPF KDKEVQTESI LLECNEGFYV
MFWLMLGYIA LLALFCFTFA YIGRKLPQKY NEAKFITFSM VICLMAWIIF IPIHVTTSGK
YVPAVEMVVI LISNYGILSC HFLPKSYIIL FKKEHNTKDA FMKNVYEYAR KSAENIKGLT
GTEPQFKQEN SVYTISNLSF VPEEKHE