ID   VG74_SHV21              Reviewed;         321 AA.
AC   Q01035;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   23-FEB-2022, entry version 92.
DE   RecName: Full=G-protein coupled receptor homolog ECRF3;
GN   Name=74; Synonyms=ECRF3;
OS   Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=10383;
OH   NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA   Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA   Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA   Honess R.W.;
RT   "Primary structure of the herpesvirus saimiri genome.";
RL   J. Virol. 66:5047-5058(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1314457; DOI=10.1016/0042-6822(92)90759-i;
RA   Nicholas J., Cameron K.R., Coleman H., Newman C., Honess R.W.;
RT   "Analysis of nucleotide sequence of the rightmost 43 kbp of herpesvirus
RT   saimiri (HVS) L-DNA: general conservation of genetic organization between
RT   HVS and Epstein-Barr virus.";
RL   Virology 188:296-310(1992).
RN   [3]
RP   SIMILARITY TO G-PROTEIN COUPLED RECEPTORS.
RX   PubMed=1309943; DOI=10.1038/355362a0;
RA   Nicholas J., Cameron K.R., Honess R.W.;
RT   "Herpesvirus saimiri encodes homologues of G protein-coupled receptors and
RT   cyclins.";
RL   Nature 355:362-365(1992).
CC   -!- FUNCTION: May be highly relevant to the process of cellular
CC       transformation and rapid T-cell proliferation effected by HVS during
CC       latent infections of T-cells in susceptible hosts.
CC   -!- SUBCELLULAR LOCATION: Host cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; S76368; AAB21117.1; -; Genomic_DNA.
DR   EMBL; X64346; CAA45697.1; -; Genomic_DNA.
DR   EMBL; M86409; AAA46150.1; -; Genomic_DNA.
DR   RefSeq; NP_040276.1; NC_001350.1.
DR   SMR; Q01035; -.
DR   GeneID; 1682467; -.
DR   KEGG; vg:1682467; -.
DR   Proteomes; UP000000587; 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   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   G-protein coupled receptor; Glycoprotein; Host cell membrane;
KW   Host membrane; Membrane; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..321
FT                   /note="G-protein coupled receptor homolog ECRF3"
FT                   /id="PRO_0000070253"
FT   TOPO_DOM        1..34
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..51
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52..76
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..93
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..124
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..141
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..166
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..196
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..215
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        216..234
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..251
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..286
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..303
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..321
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        18
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   321 AA;  37132 MW;  9C4F4C760B962003 CRC64;
     MEVKLDFSSE DFSNYSYNYS GDIYYGDVAP CVVNFLISES ALAFIYVLMF LCNAIGNSLV
     LRTFLKYRAQ AQSFDYLMMG FCLNSLFLAG YLLMRLLRMF EIFMNTELCK LEAFFLNLSI
     YWSPFILVFI SVLRCLLIFC ATRLWVKKTL IGQVFLCCSF VLACFGALPH VMVTSYYEPS
     SCIEEDGVLT EQLRTKLNTF HTWYSFAGPL FITVICYSMS CYKLFKTKLS KRAEVVTIIT
     MTTLLFIVFC IPYYIMESID TLLRVGVIEE TCAKRSAIVY GIQCTYMLLV LYYCMLPLMF
     AMFGSLFRQR MAAWCKTICH C