OX2V_HHV8P
ID OX2V_HHV8P Reviewed; 271 AA.
AC P0C788; P0C789; P88963; Q98149;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=OX-2 membrane glycoprotein homolog;
DE AltName: Full=Viral OX2;
DE Short=vOX2;
DE Flags: Precursor;
GN Name=K14;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bohenzky R.A., Russo J.J., Moore P.S., Chang Y.;
RT "KSHV contains a homolog to OX-2.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11504542; DOI=10.1006/viro.2001.1016;
RA Nador R.G., Milligan L.L., Flore O., Wang X., Arvanitakis L., Knowles D.M.,
RA Cesarman E.;
RT "Expression of Kaposi's sarcoma-associated herpesvirus G protein-coupled
RT receptor monocistronic and bicistronic transcripts in primary effusion
RT lymphomas.";
RL Virology 287:62-70(2001).
RN [4]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Davison A.J.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP CHARACTERIZATION.
RX PubMed=11967286; DOI=10.1128/jvi.76.10.4688-4698.2002;
RA Chung Y.-H., Means R.E., Choi J.-K., Lee B.-S., Jung J.U.;
RT "Kaposi's sarcoma-associated herpesvirus OX2 glycoprotein activates
RT myeloid-lineage cells to induce inflammatory cytokine production.";
RL J. Virol. 76:4688-4698(2002).
CC -!- FUNCTION: Dramatically stimulates primary monocytes, macrophages, and
CC dendritic cells to produce the inflammatory cytokines interleukin 1-
CC beta, IL-6, monocyte chemoattractant protein 1, and TNF-alpha. The
CC induction of inflammatory cytokine production potentially promotes the
CC cytokine-mediated angiogenic proliferation of KSHV-infected cells.
CC -!- SUBUNIT: Interacts with human CD200R1.
CC -!- SUBCELLULAR LOCATION: Host cell membrane; Single-pass type I membrane
CC protein.
CC -!- PTM: N-glycosylated.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB39927.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAC57159.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK53415.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK53417.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U75698; AAC57159.1; ALT_INIT; Genomic_DNA.
DR EMBL; U52065; AAB39927.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF148805; AAD46502.2; -; Genomic_DNA.
DR EMBL; AF367765; AAK53415.1; ALT_INIT; mRNA.
DR EMBL; AF367766; AAK53417.1; ALT_INIT; mRNA.
DR RefSeq; YP_001129432.1; NC_009333.1.
DR SMR; P0C788; -.
DR BioGRID; 1776968; 21.
DR GeneID; 4961465; -.
DR KEGG; vg:4961465; -.
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:0043031; P:negative regulation of macrophage activation; IEA:InterPro.
DR GO; GO:0050776; P:regulation of immune response; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR033321; CD200.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR46841:SF3; PTHR46841:SF3; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Host cell membrane; Host membrane;
KW Host-virus interaction; Immunoglobulin domain; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..271
FT /note="OX-2 membrane glycoprotein homolog"
FT /id="PRO_0000015127"
FT TOPO_DOM 25..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..129
FT /note="Ig-like V-type"
FT DOMAIN 130..220
FT /note="Ig-like C2-type"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 39..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 148..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 271 AA; 28783 MW; E9BB5921121F0034 CRC64;
MSSLFISLPW VAFIWLALLG AVGGARVQGP MRGSAALTCA ITPRADIVSV TWQKRQLPGP
VNVATYSHSY GVVVQTQYRH KANITCPGLW NSTLVIHNLA VDDEGCYLCI FNSFGGRQVS
CTACLEVTSP PTGHVQVNST EDADTVTCLA TGRPPPNVTW AAPWNNASST QEQFTDSDGL
TVAWRTVRLP RGDNTTPSEG ICLITWGNES ISIPASIQGP LAHDLPAAQG TLAGVAITLV
GLFGIFALHH CRRKQGGASP TSDDMDPLST Q
