GP350_EBVB9
ID GP350_EBVB9 Reviewed; 907 AA.
AC P03200; P03201; Q66536; Q66537; Q777F0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 23-FEB-2022, entry version 106.
DE RecName: Full=Envelope glycoprotein GP350;
DE AltName: Full=Membrane antigen;
DE Short=MA;
GN ORFNames=BLLF1;
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] (ISOFORMS GP220 AND GP350).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS GP220 AND GP350), AND
RP INTERACTION WITH HOST CR2.
RX PubMed=2987520; DOI=10.1128/jvi.54.3.665-674.1985;
RA Beisel C., Tanner J., Matsuo T., Thorley-Lawson D., Kezdy F., Kieff E.;
RT "Two major outer envelope glycoproteins of Epstein-Barr virus are encoded
RT by the same gene.";
RL J. Virol. 54:665-674(1985).
RN [3]
RP GLYCOSYLATION.
RX PubMed=6319581; DOI=10.1099/0022-1317-65-2-397;
RA Morgan A.J., Smith A.R., Barker R.N., Epstein M.A.;
RT "A structural investigation of the Epstein-Barr (EB) virus membrane antigen
RT glycoprotein, gp340.";
RL J. Gen. Virol. 65:397-404(1984).
RN [4]
RP REVIEW.
RX PubMed=1323899; DOI=10.1016/0264-410x(92)90434-l;
RA Morgan A.J.;
RT "Epstein-Barr virus vaccines.";
RL Vaccine 10:563-571(1992).
RN [5]
RP IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX PubMed=15534216; DOI=10.1073/pnas.0407320101;
RA Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E.,
RA Illanes D., Sarracino D., Kieff E.;
RT "Proteins of purified Epstein-Barr virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004).
RN [6]
RP INTERACTION WITH HOST CR2, AND MUTAGENESIS OF GLU-21; ASP-22; TYR-151;
RP GLU-155; ILE-160; TRP-162; GLU-201; ASP-208; GLU-210; ASP-215 AND ASP-296.
RX PubMed=18786993; DOI=10.1128/jvi.01673-08;
RA Young K.A., Herbert A.P., Barlow P.N., Holers V.M., Hannan J.P.;
RT "Molecular basis of the interaction between complement receptor type 2
RT (CR2/CD21) and Epstein-Barr virus glycoprotein gp350.";
RL J. Virol. 82:11217-11227(2008).
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.
CC -!- SUBUNIT: Interacts with host CR2. {ECO:0000269|PubMed:18786993,
CC ECO:0000269|PubMed:2987520}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:15534216};
CC Single-pass membrane protein {ECO:0000269|PubMed:15534216}. Host
CC membrane {ECO:0000269|PubMed:15534216}; Single-pass membrane protein
CC {ECO:0000269|PubMed:15534216}. Note=Most abundant component of the
CC viral envelope.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=GP350;
CC IsoId=P03200-1; Sequence=Displayed;
CC Name=GP220;
CC IsoId=P03200-2; Sequence=VSP_002070;
CC -!- PTM: Extensively glycosylated. {ECO:0000269|PubMed:6319581}.
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; V01555; CAA24854.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53417.1; -; Genomic_DNA.
DR EMBL; M10593; AAA45881.1; -; Genomic_DNA.
DR EMBL; M10593; AAA45880.1; -; Genomic_DNA.
DR PIR; A43042; QQBE21.
DR PIR; B43042; QQBE22.
DR RefSeq; YP_401667.1; NC_007605.1.
DR SMR; P03200; -.
DR IntAct; P03200; 2.
DR MINT; P03200; -.
DR DrugBank; DB00632; Docosanol.
DR PRIDE; P03200; -.
DR ABCD; P03200; 1 sequenced antibody.
DR DNASU; 3783713; -.
DR GeneID; 3783713; -.
DR KEGG; vg:3783713; -.
DR SIGNOR; P03200; -.
DR Proteomes; UP000153037; 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..907
FT /note="Envelope glycoprotein GP350"
FT /id="PRO_0000116183"
FT TOPO_DOM 1..860
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 861..881
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 882..907
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 423..830
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 547
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 610
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 627
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 683
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 755
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 815
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 858
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VAR_SEQ 502..750
FT /note="Missing (in isoform GP220)"
FT /evidence="ECO:0000305"
FT /id="VSP_002070"
FT MUTAGEN 21
FT /note="E->A: 40% loss of interaction with host CR2."
FT /evidence="ECO:0000269|PubMed:18786993"
FT MUTAGEN 22
FT /note="D->A: Complete loss of interaction with host CR2."
FT /evidence="ECO:0000269|PubMed:18786993"
FT MUTAGEN 151
FT /note="Y->A: Complete loss of interaction with host CR2."
FT /evidence="ECO:0000269|PubMed:18786993"
FT MUTAGEN 155
FT /note="E->A: 60% loss of interaction with host CR2."
FT /evidence="ECO:0000269|PubMed:18786993"
FT MUTAGEN 160
FT /note="I->A: Complete loss of interaction with host CR2."
FT /evidence="ECO:0000269|PubMed:18786993"
FT MUTAGEN 162
FT /note="W->A: Complete loss of interaction with host CR2."
FT /evidence="ECO:0000269|PubMed:18786993"
FT MUTAGEN 201
FT /note="E->A: 30% loss of interaction with host CR2."
FT /evidence="ECO:0000269|PubMed:18786993"
FT MUTAGEN 208
FT /note="D->A: 60% loss of interaction with host CR2."
FT /evidence="ECO:0000269|PubMed:18786993"
FT MUTAGEN 210
FT /note="E->A: 60% loss of interaction with host CR2."
FT /evidence="ECO:0000269|PubMed:18786993"
FT MUTAGEN 215
FT /note="D->A: 30% loss of interaction with host CR2."
FT /evidence="ECO:0000269|PubMed:18786993"
FT MUTAGEN 296
FT /note="D->A: Complete loss of interaction with host CR2."
FT /evidence="ECO:0000269|PubMed:18786993"
FT CONFLICT 721
FT /note="A -> E (in Ref. 2; AAA45881)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 907 AA; 94432 MW; 0750141CBCAC52C9 CRC64;
MEAALLVCQY TIQSLIHLTG EDPGFFNVEI PEFPFYPTCN VCTADVNVTI NFDVGGKKHQ
LDLDFGQLTP HTKAVYQPRG AFGGSENATN LFLLELLGAG ELALTMRSKK LPINVTTGEE
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 DPNTTTGLPS STHVPTNLTA PASTGPTVST ADVTSPTPAG
TTSGASPVTP SPSPWDNGTE SKAPDMTSST SPVTTPTPNA TSPTPAVTTP TPNATSPTPA
VTTPTPNATS PTLGKTSPTS AVTTPTPNAT SPTLGKTSPT SAVTTPTPNA TSPTLGKTSP
TSAVTTPTPN ATGPTVGETS PQANATNHTL GGTSPTPVVT SQPKNATSAV TTGQHNITSS
STSSMSLRPS SNPETLSPST SDNSTSHMPL LTSAHPTGGE NITQVTPASI STHHVSTSSP
APRPGTTSQA SGPGNSSTST KPGEVNVTKG TPPQNATSPQ APSGQKTAVP TVTSTGGKAN
STTGGKHTTG HGARTSTEPT TDYGGDSTTP RPRYNATTYL PPSTSSKLRP RWTFTSPPVT
TAQATVPVPP TSQPRFSNLS MLVLQWASLA VLTLLLLLVM ADCAFRRNLS TSHTYTTPPY
DDAETYV
