GPC6A_CARAU
ID GPC6A_CARAU Reviewed; 877 AA.
AC Q9PW88;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=G-protein coupled receptor family C group 6 member A;
DE AltName: Full=Odorant receptor 5.24;
DE Flags: Precursor;
GN Name=gprc6a;
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10433261; DOI=10.1016/s0896-6273(00)80802-8;
RA Speca D.J., Lin D.M., Sorensen P.W., Isacoff E.Y., Ngai J., Dittman A.H.;
RT "Functional identification of a goldfish odorant receptor.";
RL Neuron 23:487-498(1999).
RN [2]
RP MUTAGENESIS OF LYS-74; GLN-78; SER-111; SER-111; SER-151; SER-152; THR-175;
RP ARG-190; ASP-195; TYR-223; LYS-283; SER-284; SER-285; ASP-309 AND ASP-388.
RX PubMed=12912984; DOI=10.1074/jbc.m307120200;
RA Kuang D., Yao Y., Wang M., Pattabiraman N., Kotra L.P., Hampson D.R.;
RT "Molecular similarities in the ligand binding pockets of an odorant
RT receptor and the metabotropic glutamate receptors.";
RL J. Biol. Chem. 278:42551-42559(2003).
RN [3]
RP MUTAGENESIS OF GLU-47; SER-152; THR-175; TYR-223; ASP-309; ASP-388 AND
RP MET-389.
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. Most highly activated by basic amino acids
CC such as L-lysine and L-arginine. {ECO:0000269|PubMed:10433261}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in olfactory epithelium. Also expressed
CC in gills, tongue, lips and palatal organ. Not expressed in brain,
CC kidney, liver, muscle, intestine, ovary and skin. In olfactory
CC epithelium, it is widely expressed over the apical and medial portions
CC of the olfactory sensory neurons, regions that contain olfactory
CC neurons. Expressed in external epithelia, which contains taste buds and
CC solitary chemosensory cells. On gill rakers, it is widely expressed in
CC the surface epithelium, but excluded from taste buds.
CC {ECO:0000269|PubMed:10433261}.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; AF158963; AAD46570.2; -; mRNA.
DR AlphaFoldDB; Q9PW88; -.
DR SMR; Q9PW88; -.
DR TCDB; 9.A.14.7.7; the g-protein-coupled receptor (gpcr) family.
DR Proteomes; UP000515129; Genome assembly.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
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; 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; Olfaction; Receptor; Reference proteome; Sensory transduction;
KW Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..877
FT /note="G-protein coupled receptor family C group 6 member
FT A"
FT /id="PRO_0000043200"
FT TOPO_DOM 25..567
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 589..603
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 625..635
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..676
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 677..697
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 698..720
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 721..741
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 742..755
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..776
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 777..782
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 783..803
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 804..877
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 388
FT /ligand="L-lysine"
FT /ligand_id="ChEBI:CHEBI:32551"
FT SITE 389
FT /note="Important for basic amino acid selectivity"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
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 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 47
FT /note="E->L,K: Induces a mild reduction in ligand-
FT affinity."
FT /evidence="ECO:0000269|PubMed:15537883"
FT MUTAGEN 74
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:12912984"
FT MUTAGEN 78
FT /note="Q->A: Induces reduction in ligand-affinity."
FT /evidence="ECO:0000269|PubMed:12912984"
FT MUTAGEN 111
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:12912984"
FT MUTAGEN 150
FT /note="S->A: No effect."
FT MUTAGEN 151
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:12912984"
FT MUTAGEN 152
FT /note="S->A: Induces reduction in ligand-affinity."
FT /evidence="ECO:0000269|PubMed:12912984,
FT ECO:0000269|PubMed:15537883"
FT MUTAGEN 175
FT /note="T->A,S: Almost abolishes L-Lys- and L-Arg-affinity."
FT /evidence="ECO:0000269|PubMed:12912984,
FT ECO:0000269|PubMed:15537883"
FT MUTAGEN 190
FT /note="R->A: Induces reduction in ligand-affinity."
FT /evidence="ECO:0000269|PubMed:12912984"
FT MUTAGEN 195
FT /note="D->A: Abolishes L-Lys-affinity."
FT /evidence="ECO:0000269|PubMed:12912984"
FT MUTAGEN 223
FT /note="Y->A: Abolishes L-Lys-affinity and strongly reduces
FT L-Arg-affinity."
FT /evidence="ECO:0000269|PubMed:12912984,
FT ECO:0000269|PubMed:15537883"
FT MUTAGEN 223
FT /note="Y->H,F: Almost abolishes L-Arg-affinity."
FT /evidence="ECO:0000269|PubMed:12912984,
FT ECO:0000269|PubMed:15537883"
FT MUTAGEN 283
FT /note="K->A: Abolishes L-Lys-affinity."
FT /evidence="ECO:0000269|PubMed:12912984"
FT MUTAGEN 284
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:12912984"
FT MUTAGEN 285
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:12912984"
FT MUTAGEN 309
FT /note="D->A: Almost abolishes L-Lys-affinity."
FT /evidence="ECO:0000269|PubMed:12912984,
FT ECO:0000269|PubMed:15537883"
FT MUTAGEN 309
FT /note="D->L: Almost abolishes L-Arg-affinity."
FT /evidence="ECO:0000269|PubMed:12912984,
FT ECO:0000269|PubMed:15537883"
FT MUTAGEN 388
FT /note="D->A: Induces a 26-fold reduction in L-Lys-affinity
FT without affecting affinity for L-Gln."
FT /evidence="ECO:0000269|PubMed:12912984,
FT ECO:0000269|PubMed:15537883"
FT MUTAGEN 389
FT /note="M->K: Induces a 24-fold reduction in L-Lys-affinity
FT but increases affinity for L-Glu."
FT /evidence="ECO:0000269|PubMed:15537883"
SQ SEQUENCE 877 AA; 98120 MW; 5359109FD4A8A887 CRC64;
MAGLDLSLVL MLSVLAGVRE VSLTQVNQQG VIAPGDIIIG GLFPIHEAAE AVNFTGLNSF
SSFQHPVCNR YYTKGLNQAL AMIHAVEMAN QSPMLSSLNL TLGYRIYDTC SDVTTALWAV
QDLTRPYSYC DSQTNSSQPV QPIMAVIGPS SSEISIAVAR ELNLLMIPQI SYASTATILS
DKSRFPAFMR TVPNDEYQTH AMVQLLKDNK WTWVGIIITD GDYGRSAMES FVKHTEREGI
CVAFKVILPD SLADEQKLNI HINETVDIIE KNTKVNVVVS FAKSSQMKLL YEGLRSRNVP
KNKVWVASDN WSTSKNILKD VNLSDIGNIL GFTFKSGNVT AFLQYLKDLK FGSEAKMNNS
FLEEFLKLPE IGNAANAVQE QIKNTHLDMV FSVQMAVSAI AKAVVELCVE RQCKTPSAIQ
PWELLKQLRN VTFEKEGVMY NFDANGDINL GYDVCLWDDD ESEKNDIIAE YYPSNSSFTF
TRKNLSNIEN VLSKCSDSCQ PGEYKKTAEG QHTCCYECLA CAENQYSNHT DADTCSKCDT
ESLWSNANSS KCYPKFYEYF EWNSGFAIAL LTLAALGILL LISMSALFFW QRNSLVVKAA
GGPLCHLILF SLLGSFISVI FFVGEPSNES CRVRQVIFGL SFTLCVSCIL VKSLKILLAF
QMNLELKELL RKLYKPYVIV CMCMGLQVTI CTLWLTLHRP FIEKVVQPKS ILLECNEGSD
LMFGLMLGYI VLLALICFTF AYKGRKLPQK YNEAKFITFG MLIYLMAWVI FIPVHVTTSG
KYVPAVEVVV ILISNYGILS CHFLPKCYII IFKKEYNTKD AFLKNVFEYA RKSSENIRGL
SGTDPHSKTD NSVYVISNPS LVPEEKQVSV PEIDNVL
