V206_FOWPN
ID V206_FOWPN Reviewed; 308 AA.
AC Q9J529;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 23-FEB-2022, entry version 79.
DE RecName: Full=G-protein coupled receptor homolog FPV206;
GN OrderedLocusNames=FPV206;
OS Fowlpox virus (strain NVSL) (FPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX NCBI_TaxID=928301;
OH NCBI_TaxID=7742; Vertebrata.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT "The genome of fowlpox virus.";
RL J. Virol. 74:3815-3831(2000).
CC -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF198100; AAF44550.1; -; Genomic_DNA.
DR RefSeq; NP_039169.1; NC_002188.1.
DR SMR; Q9J529; -.
DR GeneID; 1486778; -.
DR KEGG; vg:1486778; -.
DR Proteomes; UP000008597; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Host cell membrane; Host membrane; Membrane; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..308
FT /note="G-protein coupled receptor homolog FPV206"
FT /id="PRO_0000070250"
FT TOPO_DOM 1..20
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 89..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 308 AA; 35375 MW; 5ABFE53EE1FEB28A CRC64;
MNFTGDCLLY AGYEKLSLSL AVVTILIFSS SLILNISALV IGFYTTAPGP MKMYLINLIV
SDILFTVTLP LKIDYYYYFF NWRWGEMACR IMSFLSYINT YVSINFMTWI SVNRYYAVTR
PHKYNSRDNI MRTKIACACT WVIILVPMSS ILFVSTTSSD HETKIRCMEY NKVGDSMYLP
PWVTIVMCFI GFVIPFAMMA ISYSAVCYTV LSGISKSTRS YRTCKLVACI LTEFVICFLP
YHASVISYMI HIITSKTVLC ENVSYYQMLL HATQCLMKLN CCMDPIIYLF VSSYKSKAKS
NSIKLMFK
