GB_HHV8P
ID GB_HHV8P Reviewed; 845 AA.
AC F5HB81;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 29-SEP-2021, entry version 39.
DE RecName: Full=Envelope glycoprotein B {ECO:0000255|HAMAP-Rule:MF_04032};
DE Short=gB {ECO:0000255|HAMAP-Rule:MF_04032};
DE Flags: Precursor;
GN Name=gB {ECO:0000255|HAMAP-Rule:MF_04032}; Synonyms=ORF8;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
RN [3]
RP FUNCTION IN FUSION.
RX PubMed=11932406; DOI=10.1128/jvi.76.9.4390-4400.2002;
RA Pertel P.E.;
RT "Human herpesvirus 8 glycoprotein B (gB), gH, and gL can mediate cell
RT fusion.";
RL J. Virol. 76:4390-4400(2002).
RN [4]
RP FUNCTION.
RX PubMed=12584338; DOI=10.1128/jvi.77.5.3131-3147.2003;
RA Wang F.Z., Akula S.M., Sharma-Walia N., Zeng L., Chandran B.;
RT "Human herpesvirus 8 envelope glycoprotein B mediates cell adhesion via its
RT RGD sequence.";
RL J. Virol. 77:3131-3147(2003).
RN [5]
RP FUNCTION, AND INTERACTION WITH HOST ITGAV AND ITGB3.
RX PubMed=18045938; DOI=10.1128/jvi.01673-07;
RA Garrigues H.J., Rubinchikova Y.E., Dipersio C.M., Rose T.M.;
RT "Integrin alphaVbeta3 Binds to the RGD motif of glycoprotein B of Kaposi's
RT sarcoma-associated herpesvirus and functions as an RGD-dependent entry
RT receptor.";
RL J. Virol. 82:1570-1580(2008).
CC -!- FUNCTION: Envelope glycoprotein that forms spikes at the surface of the
CC virion envelope. Participates in viral entry through an RGD motif that
CC binds ITGAV-ITGB3. Membrane fusion is mediated by the fusion machinery
CC composed at least of gB and the heterodimer gH/gL. May be involved in
CC the fusion between the virion envelope and the outer nuclear membrane
CC during virion egress. {ECO:0000269|PubMed:11932406,
CC ECO:0000269|PubMed:12584338, ECO:0000269|PubMed:18045938}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Binds to heparan sulfate
CC proteoglycans. Interacts with gH/gL heterodimer (By similarity).
CC Interacts with host ITGAV-ITGB3; this interaction mediates viral entry.
CC {ECO:0000250, ECO:0000255|HAMAP-Rule:MF_04032,
CC ECO:0000269|PubMed:18045938}.
CC -!- INTERACTION:
CC F5HB81; P05106: ITGB3; Xeno; NbExp=2; IntAct=EBI-9027696, EBI-702847;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032};
CC Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}.
CC Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi
CC apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type
CC I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Note=During
CC virion morphogenesis, this protein probably accumulates in the
CC endosomes and trans-Golgi where secondary envelopment occurs. It is
CC probably transported to the cell surface from where it is endocytosed
CC and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-
CC Rule:MF_04032}.
CC -!- PTM: A proteolytic cleavage by host furin generates two subunits that
CC remain linked by disulfide bonds. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein B family.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
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DR EMBL; AF148805; ABD28851.1; -; Genomic_DNA.
DR RefSeq; YP_001129354.1; NC_009333.1.
DR SMR; F5HB81; -.
DR BioGRID; 1777004; 2.
DR IntAct; F5HB81; 1.
DR PRIDE; F5HB81; -.
DR DNASU; 4961501; -.
DR GeneID; 4961501; -.
DR KEGG; vg:4961501; -.
DR Proteomes; UP000000942; Genome.
DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IDA:CACAO.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.29.100; -; 2.
DR HAMAP; MF_04032; HSV_GB; 1.
DR InterPro; IPR035377; Glycoprot_B_PH1.
DR InterPro; IPR035381; Glycoprot_B_PH2.
DR InterPro; IPR038631; Glycoprot_B_PH2_sf.
DR InterPro; IPR000234; Herpes_Glycoprot_B.
DR Pfam; PF17416; Glycoprot_B_PH1; 1.
DR Pfam; PF17417; Glycoprot_B_PH2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Host cell membrane; Host endosome;
KW Host Golgi apparatus; Host membrane; Host-virus interaction; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 27..845
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000423905"
FT TOPO_DOM 27..732
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 733..753
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 754..845
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 29..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..130
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 208..216
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 411..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..730
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 802..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 830..833
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 68..528
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 85..484
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 157..222
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 315..362
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 550..587
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 845 AA; 93985 MW; C44A5F2FF29B1E41 CRC64;
MTPRSRLATL GTVILLVCFC AGAAHSRGDT FQTSSSPTPP GSSSKAPTKP GEEASGPKSV
DFYQFRVCSA SITGELFRFN LEQTCPDTKD KYHQEGILLV YKKNIVPHIF KVRRYRKIAT
SVTVYRGLTE SAITNKYELP RPVPLYEISH MDSTYQCFSS MKVNVNGVEN TFTDRDDVNT
TVFLQPVEGL TDNIQRYFSQ PVIYAEPGWF PGIYRVRTTV NCEIVDMIAR SAEPYNYFVT
SLGDTVEVSP FCYNESSCST TPSNKNGLSV QVVLNHTVVT YSDRGTSPTP QNRIFVETGA
YTLSWASESK TTAVCPLALW KTFPRSIQTT HEDSFHFVAN EITATFTAPL TPVANFTDTY
SCLTSDINTT LNASKAKLAS THVPNGTVQY FHTTGGLYLV WQPMSAINLT HAQGDSGNPT
SSPPPSASPM TTSASRRKRR SASTAAAGGG GSTDNLSYTQ LQFAYDKLRD GINQVLEELS
RAWCREQVRD NLMWYELSKI NPTSVMTAIY GRPVSAKFVG DAISVTECIN VDQSSVNIHK
SLRTNSKDVC YARPLVTFKF LNSSNLFTGQ LGARNEIILT NNQVETCKDT CEHYFITRNE
TLVYKDYAYL RTINTTDIST LNTFIALNLS FIQNIDFKAI ELYSSAEKRL ASSVFDLETM
FREYNYYTHR LAGLREDLDN TIDMNKERFV RDLSEIVADL GGIGKTVVNV ASSVVTLCGS
LVTGFINFIK HPLGGMLMII IVIAIILIIF MLSRRTNTIA QAPVKMIYPD VDRRAPPSGG
APTREEIKNI LLGMHQLQQE ERQKADDLKK STPSVFQRTA NGLRQRLRGY KPLTQSLDIS
PETGE
