ID   OX2V_HHV6U              Reviewed;         290 AA.
AC   Q89738; Q76UF8;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   02-JUN-2021, entry version 82.
DE   RecName: Full=Putative OX-2 membrane glycoprotein homolog;
DE   AltName: Full=Protein U85;
DE   Flags: Precursor;
GN   Name=U85; Synonyms=EDLF1;
OS   Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS   lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=10370;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7941342; DOI=10.1006/viro.1994.1589;
RA   Nicholas J.;
RT   "Nucleotide sequence analysis of a 21-kbp region of the genome of human
RT   herpesvirus-6 containing homologues of human cytomegalovirus major
RT   immediate-early and replication genes.";
RL   Virology 204:738-750(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA   Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA   Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT   "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT   genome evolution.";
RL   Virology 209:29-51(1995).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; U13194; AAA68476.1; -; Genomic_DNA.
DR   EMBL; X83413; CAA58334.1; -; Genomic_DNA.
DR   RefSeq; NP_042978.1; NC_001664.2.
DR   PRIDE; Q89738; -.
DR   DNASU; 1487965; -.
DR   GeneID; 1487965; -.
DR   KEGG; vg:1487965; -.
DR   Proteomes; UP000009295; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..290
FT                   /note="Putative OX-2 membrane glycoprotein homolog"
FT                   /id="PRO_0000342560"
FT   TOPO_DOM        18..267
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        289..290
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          23..135
FT                   /note="Ig-like V-type"
FT   DOMAIN          146..236
FT                   /note="Ig-like C2-type"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        41..125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   290 AA;  32900 MW;  3E93C7EAB2CB2C1D CRC64;
     MSSLMLRLLP LLYIISAHFV LHPETSPSLI YEIGSIVTFH CRLETTTNIR SVSWYNKNRL
     ISNHEVQNMD NLSFTDDGYV LIHELNKINN LAVDSKLYFH IKHNRTTSLL KIKAKSAYDA
     TCLTCTFTVD NEKTSATSCL KLFMKPIVVL YFRYLDNFLD VTCTVTSYPK PNVVIKFLGE
     VYKRDIPIVR QNENGSSTVS VNFTFKRRTK LEFVGKTVSC LASSWFTNQK ASALVTSGEH
     TVQNHDEYSK EGVKSSNSDE TVFTWTVPLI LILISVIVLL ISVCIVAFKS