VGPCR_HHV8P
ID VGPCR_HHV8P Reviewed; 342 AA.
AC Q98146; O12573; P88966; Q77Q35;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=viral G-protein coupled receptor;
DE Short=vGPCR;
DE AltName: Full=Protein ORF74;
GN Name=ORF74;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8892957; DOI=10.1128/jvi.70.11.8218-8223.1996;
RA Cesarman E., Nador R.G., Bai F., Bohenzky R.A., Russo J.J., Moore P.S.,
RA Chang Y., Knowles D.M.;
RT "Kaposi's sarcoma-associated herpesvirus contains G protein-coupled
RT receptor and cyclin D homologs which are expressed in Kaposi's sarcoma and
RT malignant lymphoma.";
RL J. Virol. 70:8218-8223(1996).
RN [2]
RP SEQUENCE REVISION.
RA Cesarman E., Nador R.G., Bai F., Chang J., Moore P.S., Knowles D.M.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Guo H.G., Browning P., Nicholas J., Hayward G.H., Tschachler E.,
RA Jiang Y.W., Sadowska M., Raffeld M., Colombini S., Gallo R.C., Reitz M.S.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8962146; DOI=10.1073/pnas.93.25.14862;
RA Russo J.J., Bohenzky R.A., Chien M.-C., Chen J., Yan M., Maddalena D.,
RA Parry J.P., Peruzzi D., Edelman I.S., Chang Y., Moore P.S.;
RT "Nucleotide sequence of the Kaposi sarcoma-associated herpesvirus (HHV8).";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14862-14867(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9151804; DOI=10.1128/jvi.71.6.4187-4192.1997;
RA Neipel F., Albrecht J.-C., Fleckenstein B.;
RT "Cell-homologous genes in the Kaposi's sarcoma-associated rhadinovirus
RT human herpesvirus 8: determinants of its pathogenicity?";
RL J. Virol. 71:4187-4192(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
RN [7]
RP FUNCTION.
RX PubMed=12477810; DOI=10.1128/jvi.77.1.57-67.2003;
RA Cannon M., Philpott N.J., Cesarman E.;
RT "The Kaposi's sarcoma-associated herpesvirus G protein-coupled receptor has
RT broad signaling effects in primary effusion lymphoma cells.";
RL J. Virol. 77:57-67(2003).
RN [8]
RP FUNCTION.
RX PubMed=14724579; DOI=10.1038/sj.onc.1207021;
RA Cannon M.L., Cesarman E.;
RT "The KSHV G protein-coupled receptor signals via multiple pathways to
RT induce transcription factor activation in primary effusion lymphoma
RT cells.";
RL Oncogene 23:514-523(2004).
RN [9]
RP INTERACTION WITH PROTEIN K7.
RX PubMed=18802460; DOI=10.1371/journal.ppat.1000157;
RA Feng H., Dong X., Negaard A., Feng P.;
RT "Kaposi's sarcoma-associated herpesvirus K7 induces viral G protein-coupled
RT receptor degradation and reduces its tumorigenicity.";
RL PLoS Pathog. 4:E1000157-E1000157(2008).
RN [10]
RP FUNCTION, AND INTERACTION WITH HOST CADM1.
RX PubMed=29698475; DOI=10.1371/journal.ppat.1006968;
RA Hunte R., Alonso P., Thomas R., Bazile C.A., Ramos J.C., van der Weyden L.,
RA Dominguez-Bendala J., Khan W.N., Shembade N.;
RT "CADM1 is essential for KSHV-encoded vGPCR-and vFLIP-mediated chronic NF-
RT kappaB activation.";
RL PLoS Pathog. 14:E1006968-E1006968(2018).
CC -!- FUNCTION: Receptor that signals constitutively via several signaling
CC pathways including PI3K/AKT as well as mitogen- and stress-
CC activated/MAP kinases. Promotes host cell proliferation and survival,
CC modulates cell migration, stimulates angiogenesis, and recruits
CC inflammatory cells, both in expressing cells and in neighboring cells.
CC Maintains chronic activation of NF-kappa-B via interaction with host
CC CADM1 (PubMed:29698475). {ECO:0000269|PubMed:12477810,
CC ECO:0000269|PubMed:14724579, ECO:0000269|PubMed:29698475}.
CC -!- SUBUNIT: Interacts with protein K7; this interaction promotes vGPCR
CC proteasomal degradation (PubMed:18802460). Interacts with host CADM1;
CC this interaction is essential for chronic NF-kappa-B activation
CC (PubMed:29698475). {ECO:0000269|PubMed:18802460,
CC ECO:0000269|PubMed:29698475}.
CC -!- INTERACTION:
CC Q98146; F5HDA4: K7; NbExp=5; IntAct=EBI-7930093, EBI-9002986;
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; U82242; AAB51506.1; -; Genomic_DNA.
DR EMBL; U75698; AAC57160.1; -; Genomic_DNA.
DR EMBL; U40394; AAD04749.1; -; Genomic_DNA.
DR EMBL; U93872; AAB62618.1; -; Genomic_DNA.
DR EMBL; AF148805; AAD46503.1; -; Genomic_DNA.
DR RefSeq; YP_001129433.1; NC_009333.1.
DR SMR; Q98146; -.
DR BioGRID; 1776968; 21.
DR IntAct; Q98146; 3.
DR MINT; Q98146; -.
DR GeneID; 4961460; -.
DR GeneID; 4961465; -.
DR KEGG; vg:4961460; -.
DR Proteomes; UP000000942; 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; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW G-protein coupled receptor; Glycoprotein; Host cell membrane;
KW Host membrane; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..342
FT /note="viral G-protein coupled receptor"
FT /id="PRO_0000070252"
FT TOPO_DOM 1..51
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CONFLICT 44
FT /note="V -> G (in Ref. 2; AAD04749)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="A -> P (in Ref. 2; AAD04749)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="L -> S (in Ref. 3; AAB51506)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="R -> K (in Ref. 3; AAB51506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 38669 MW; 41E4B33CA2D9F069 CRC64;
MAAEDFLTIF LDDDESWNET LNMSGYDYSG NFSLEVSVCE MTTVVPYTWN VGILSLIFLI
NVLGNGLVTY IFCKHRSRAG AIDILLLGIC LNSLCLSISL LAEVLMFLFP NIISTGLCRL
EIFFYYLYVY LDIFSVVCVS LVRYLLVAYS TRSWPKKQSL GWVLTSAALL IALVLSGDAC
RHRSRVVDPV SKQAMCYENA GNMTADWRLH VRTVSVTAGF LLPLALLILF YALTWCVVRR
TKLQARRKVR GVIVAVVLLF FVFCFPYHVL NLLDTLLRRR WIRDSCYTRG LINVGLAVTS
LLQALYSAVV PLIYSCLGSL FRQRMYGLFQ SLRQSFMSGA TT
