V021_FOWPN
ID V021_FOWPN Reviewed; 320 AA.
AC Q9J5I0;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 23-FEB-2022, entry version 81.
DE RecName: Full=G-protein coupled receptor homolog FPV021;
GN OrderedLocusNames=FPV021;
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; AAF44365.1; -; Genomic_DNA.
DR RefSeq; NP_038984.1; NC_002188.1.
DR SMR; Q9J5I0; -.
DR GeneID; 1486740; -.
DR KEGG; vg:1486740; -.
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; IPR000248; ATII_rcpt.
DR InterPro; IPR000826; Formyl_rcpt-rel.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24225; PTHR24225; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00241; ANGIOTENSINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
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..320
FT /note="G-protein coupled receptor homolog FPV021"
FT /id="PRO_0000070248"
FT TOPO_DOM 1..18
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..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..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..260
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
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 320 AA; 37809 MW; 5F082B9A1C616958 CRC64;
MDTDYGTVHT QQSVKGNTLI LLIYFISFIV GFPGNCTVIW FTGYRWKKSV TTIWFLNLAI
ADTLFVIFIP FEITYILMGH YWPFGLFVCR IGSLMFNTGM YASIFFLTFI SIDRYCLAFR
RDICNKYRYR INIMVMIIIS WIISILLSTP YMYFKNTNEK YRNNRDCLED YHSDNNTYLL
RRVVFCISLV MRYLVPSVVM LFCYCLLLFK HSLFLSKGQT YTIVIMITSF MVLWTPYNIL
YFIDVIGSHY YNADTIIDAA PISISLIFLS SSINPMIYML VGRYVSFENY SMRESLKLIL
SEERDNQTNH ENEIKMENIN