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BILF2_EBVB9
ID   BILF2_EBVB9             Reviewed;         248 AA.
AC   P03218; Q777B4;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Glycoprotein BILF2;
DE   Flags: Precursor;
GN   ORFNames=BILF2;
OS   Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=10377;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6087149; DOI=10.1038/310207a0;
RA   Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA   Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA   Tuffnell P.S., Barrell B.G.;
RT   "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL   Nature 310:207-211(1984).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=2159529; DOI=10.1128/jvi.64.6.2545-2552.1990;
RA   Mackett M., Conway M.J., Arrand J.R., Haddad R.S., Hutt-Fletcher L.M.;
RT   "Characterization and expression of a glycoprotein encoded by the Epstein-
RT   Barr virus BamHI I fragment.";
RL   J. Virol. 64:2545-2552(1990).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Epstein-Barr virus BILF2 protein family.
CC       {ECO:0000305}.
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DR   EMBL; V01555; CAA24803.1; -; Genomic_DNA.
DR   EMBL; M37129; AAA45876.1; -; Genomic_RNA.
DR   EMBL; AJ507799; CAD53456.1; -; Genomic_DNA.
DR   PIR; A03780; QQBE4L.
DR   RefSeq; YP_401706.1; NC_007605.1.
DR   PRIDE; P03218; -.
DR   DNASU; 3783708; -.
DR   GeneID; 3783708; -.
DR   KEGG; vg:3783708; -.
DR   Proteomes; UP000153037; 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   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Late protein;
KW   Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..248
FT                   /note="Glycoprotein BILF2"
FT                   /id="PRO_0000116182"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          19..125
FT                   /note="Ig-like"
FT   REGION          167..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        95
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        116
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        40..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   248 AA;  27076 MW;  C3F33A253B959ADA CRC64;
     MTHLVLLLCC CVGSVCAFFS DLVKFENVTA HAGARVNLTC SVPSNESVSR IELGRGYTPG
     DGQLPLAVAT SNNGTHITNG GYNYSLTLEW VNDSNTSVSL IIPNVTLAHA GYYTCNVTLR
     NCSVASGVHC NYSAGEEDDQ YHANRTLTQR MHLTVIPATT IAPTTLVSHT TSTSHRPHRR
     PVSKRPTHKP VTLGPFPIDP WRPKTTWVHW ALLLITCAVV APVLLIIIIS CLGWLAGWGR
     RRKGWIPL
 
 
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