GP350_EBVA8
ID GP350_EBVA8 Reviewed; 886 AA.
AC P68343; Q07284; Q1HVG6;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 1.
DT 23-FEB-2022, entry version 62.
DE RecName: Full=Envelope glycoprotein GP350;
DE AltName: Full=Membrane antigen;
DE Short=MA;
GN ORFNames=BLLF1;
OS Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=82830;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8393237; DOI=10.1006/viro.1993.1409;
RA Lees J.F., Arrand J.E., Pepper S.V., Stewart J.P., Mackett M., Arrand J.R.;
RT "The Epstein-Barr virus candidate vaccine antigen gp340/220 is highly
RT conserved between virus types A and B.";
RL Virology 195:578-586(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16490228; DOI=10.1016/j.virol.2006.01.015;
RA Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.;
RT "The genome of Epstein-Barr virus type 2 strain AG876.";
RL Virology 350:164-170(2006).
CC -!- FUNCTION: Initiates virion attachment to host B-lymphocyte cell,
CC leading to virus entry. Acts by binding to host CR2 at the surface of
CC B-lymphocytes, facilitating the binding of viral glycoprotein gp42 to
CC HLA class II molecules. Attachment triggers virion-host membrane fusion
CC and invasion of the host cell (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with host CR2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein.
CC Host membrane; Single-pass membrane protein. Note=Most abundant
CC component of the viral envelope. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=GP350;
CC IsoId=P68343-1; Sequence=Displayed;
CC Name=GP220;
CC IsoId=P68343-2; Sequence=VSP_041035;
CC -!- PTM: Extensively glycosylated. {ECO:0000250}.
CC -!- BIOTECHNOLOGY: Primary surface antigen capable of inducing and reacting
CC with virus-neutralizing antibodies. Almost all EBV candidate vaccines
CC are based on gp350 proteins.
CC -!- SIMILARITY: Belongs to the Epstein-Barr GP350 family. {ECO:0000305}.
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DR EMBL; L07923; AAA02787.1; -; Genomic_DNA.
DR EMBL; DQ279927; ABB89242.1; -; Genomic_DNA.
DR RefSeq; YP_001129462.1; NC_009334.1.
DR SMR; P68343; -.
DR IntAct; P68343; 1.
DR PRIDE; P68343; -.
DR GeneID; 5176231; -.
DR KEGG; vg:5176231; -.
DR Proteomes; UP000007639; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR007796; Herpes_BLLF1.
DR Pfam; PF05109; Herpes_BLLF1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Host membrane; Host-virus interaction;
KW Late protein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Virion.
FT CHAIN 1..886
FT /note="Envelope glycoprotein GP350"
FT /id="PRO_0000116184"
FT TOPO_DOM 1..839
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 840..860
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 861..886
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 423..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
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 169
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 714
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 794
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 837
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VAR_SEQ 502..729
FT /note="Missing (in isoform GP220)"
FT /evidence="ECO:0000305"
FT /id="VSP_041035"
SQ SEQUENCE 886 AA; 92389 MW; 4394F6130DECCA8A CRC64;
MEAALLVCQY TIQSLIQLTR DDPGFFNVEI LEFPFYPACN VCTADVNATI NFDVGGKKHK
LNLDFGLLTP HTKAVYQPRG AFGGSENATN LFLLELLGAG ELALTMRSKK LPINITTGEE
QQVSLESVDV YFQDVFGTMW CHHAEMQNPV YLIPETVPYI KWDNCNSTNI TAVVRAQGLD
VTLPLSLPTS AQDSNFSVKT EMLGNEIDIE CIMEDGEISQ VLPGDNKFNI TCSGYESHVP
SGGILTSTSP VATPIPGTGY AYSLRLTPRP VSRFLGNNSI LYVFYSGNGP KASGGDYCIQ
SNIVFSDEIP ASQDMPTNTT DITYVGDNAT YSVPMVTSED ANSPNVTVTA FWAWPNNTET
DFKCKWTLTS GTPSGCENIS GAFASNRTFD ITVSGLGTAP KTLIITRTAT NATTTTHKVI
FSKAPESTTT SPTLNTTGFA APNTTTGLPS STHVPTNLTA PASTGPTVST ADVTSPTPAG
TTSGASPVTP SPSPRDNGTE SKAPDMTSPT SAVTTPTPNA TSPTPAVTTP TPNATSPTLG
KTSPTSAVTT PTPNATSPTP AVTTPTPNAT IPTLGKTSPT SAVTTPTPNA TSPTVGETSP
QANTTNHTLG GTSSTPVVTS PPKNATSAVT TGQHNITSSS TSSMSLRPSS ISETLSPSTS
DNSTSHMPLL TSAHPTGGEN ITQVTPASTS THHVSTSSPA PRPGTTSQAS GPGNSSTSTK
PGEVNVTKGT PPKNATSPQA PSGQKTAVPT VTSTGGKANS TTGGKHTTGH GARTSTEPTT
DYGGDSTTPR TRYNATTYLP PSTSSKLRPR WTFTSPPVTT AQATVPVPPT SQPRFSNLSM
LVLQWASLAV LTLLLLLVMA DCAFRRNLST SHTYTTPPYD DAETYV