GB_SUHVF
ID GB_SUHVF Reviewed; 913 AA.
AC P08355;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 02-JUN-2021, entry version 92.
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};
OS Suid herpesvirus 1 (strain Indiana-Funkhauser / Becker) (SuHV-1)
OS (Pseudorabies virus (strain Indiana-Funkhauser / Becker)).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31523;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3039163; DOI=10.1128/jvi.61.9.2691-2701.1987;
RA Robbins A.K., Dorney D.J., Wathen M.W., Whealy M.E., Gold C., Watson R.J.,
RA Holland L.E., Weed S.D., Levine M., Glorioso J.C., Enquist L.W.;
RT "The pseudorabies virus gII gene is closely related to the gB glycoprotein
RT gene of herpes simplex virus.";
RL J. Virol. 61:2691-2701(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 847-913.
RX PubMed=2543777; DOI=10.1099/0022-1317-70-5-1239;
RA Simon A., Mettenleiter T.C., Rziha H.J.;
RT "Pseudorabies virus displays variable numbers of a repeat unit adjacent to
RT the 3' end of the glycoprotein gII gene.";
RL J. Gen. Virol. 70:1239-1246(1989).
RN [3]
RP EXPORT PATHWAY.
RX PubMed=2157862; DOI=10.1128/jvi.64.5.1946-1955.1990;
RA Whealy M.E., Robbins A.K., Enquist L.W.;
RT "The export pathway of the pseudorabies virus gB homolog gII involves
RT oligomer formation in the endoplasmic reticulum and protease processing in
RT the Golgi apparatus.";
RL J. Virol. 64:1946-1955(1990).
CC -!- FUNCTION: Envelope glycoprotein that forms spikes at the surface of
CC virion envelope. Essential for the initial attachment to heparan
CC sulfate moieties of the host cell surface proteoglycans. Involved in
CC fusion of viral and cellular membranes leading to virus entry into the
CC host cell. Following initial binding to its host receptors, membrane
CC fusion is mediated by the fusion machinery composed at least of gB and
CC the heterodimer gH/gL. May be involved in the fusion between the virion
CC envelope and the outer nuclear membrane during virion egress.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Binds to heparan sulfate
CC proteoglycans. Interacts with gH/gL heterodimer. {ECO:0000255|HAMAP-
CC Rule:MF_04032}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein B family.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
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DR EMBL; M17321; AAA47465.1; -; Genomic_DNA.
DR EMBL; D00464; BAA00359.1; -; Genomic_DNA.
DR PIR; A29159; VGBEPS.
DR RefSeq; YP_068330.1; NC_006151.1.
DR SMR; P08355; -.
DR IntAct; P08355; 1.
DR GeneID; 2952558; -.
DR KEGG; vg:2952558; -.
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; IEA:UniProtKB-UniRule.
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; -; 1.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Host cell membrane; Host endosome;
KW Host Golgi apparatus; Host membrane; Host-virus interaction; Membrane;
KW Signal; Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Virion; Virus entry into host cell.
FT SIGNAL 1..59
FT /evidence="ECO:0000255"
FT CHAIN 60..913
FT /note="Envelope glycoprotein B"
FT /id="PRO_0000038180"
FT TOPO_DOM 60..797
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 798..818
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 819..913
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..189
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 268..275
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 496..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..795
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 752..795
FT /note="Hydrophobic membrane proximal region"
FT MOTIF 902..905
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 126..600
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 143..556
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 217..281
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 374..423
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 622..658
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 913 AA; 100234 MW; 5D560D235E856437 CRC64;
MPAGGGLWRG PRGHRPGHHG GAGLGRLWPA PHHAAAARGA VALALLLLAL AAAPPCGAAA
VTRAASASPT PGTGATPNDV SAEASLEEIE AFSPGPSEAP DGEYGDLDAR TAVRAAATER
DRFYVCPPPS GSTVVRLEPE QACPEYSQGR NFTEGIAVLF KENIAPHKFK AHIYYKNVIV
TTVWSGSTYA AITNRFTDRV PVPVQEITDV IDRRGKCVSK AEYVRNNHKV TAFDRDENPV
EVDLRPSRLN ALGTRGWHTT NDTYTKIGAA GFYHTGTSVN CIVEEVEARS VYPYDSFALS
TGDIVYMSPF YGLREGAHGE HIGYAPGRFQ QVEHYYPIDL DSRLRASESV TRNFLRTPHF
TVAWDWAPKT RRVCSLAKWR EAEEMTRDET RDGSFRFTSR ALGASFVSDV TQLDLQRVHL
GDCVLREASE AIDAIYRRRY NSTHVLAGDR PEVYLARGGF VVAFRPLISN ELAQLYAREL
ERLGLAGVVG PAAPAAARRA RRSPGPAGTP EPPAVNGTGH LRITTGSAEF ARLQFTYDHI
QAHVNDMLGR IAAAWCELQN KDRTLWSEMS RLNPSAVATA ALGQRVSARM LGDVMAISRC
VEVRGGVYVQ NSMRVPGERG TCYSRPLVTF EHNGTGVIEG QLGDDNELLI SRDLIEPCTG
NHRRYFKLGS GYVYYEDYNY VRMVEVPETI STRVTLNLTL LEDREFLPLE VYTREELADT
GLLDYSEIQR RNQLHALKFY DIDRVVKVDH NVVLLRGIAN FFQGLGDVGA AVGKVVLGAT
GAVISAVGGM VSFLSNPFGA LAIGLLVLAG LVAAFLAYRH ISRLRRNPMK ALYPVTTKTL
KEDGVDEGDV DEAKLDQARD MIRYMSIVSA LEQQEHKARK KNSGPALLAS RVGAMATRRR
HYQRLESEDP DAL
