GB_SHV1
ID GB_SHV1 Reviewed; 920 AA.
AC Q04464;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 02-JUN-2021, entry version 85.
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}; ORFNames=UL27;
OS Saimiriine herpesvirus 1 (strain MV-5-4-PSL) (SaHV-1) (Marmoset
OS herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10353;
OH NCBI_TaxID=9481; Callithrix.
OH NCBI_TaxID=9520; Saimiri (squirrel monkeys).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8385913; DOI=10.1007/bf01316893;
RA Eberle R., Black D.;
RT "Sequence analysis of herpes simplex virus gB gene homologs of two
RT platyrrhine monkey alpha-herpesviruses.";
RL Arch. Virol. 129:167-182(1993).
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 -!- SIMILARITY: Belongs to the herpesviridae glycoprotein B family.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M95786; AAA43841.1; -; Genomic_DNA.
DR SMR; Q04464; -.
DR PRIDE; Q04464; -.
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..39
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 40..920
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038183"
FT TOPO_DOM 40..783
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 784..804
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 805..920
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 46..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..190
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 269..276
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 728..781
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 740..781
FT /note="Hydrophobic membrane proximal region"
FT REGION 876..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 863..866
FT /note="Golgi targeting"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 409
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 683
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 127..582
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 144..538
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 218..282
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 375..423
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 605..642
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 920 AA; 101662 MW; 62C4D0315D8C2DB7 CRC64;
MAPPAAKSRA SRVAPLTSLV SMLAAAAAAV ALCAAFAEAA RGVTPVYSDD ADESSESIIT
GGAELPGEDA GPPGPEPGLP DRPTKPRKPR PGRRQRANKT REDARAQLRE SVRQIRAENA
TSMFYVCPPP TGATVVQFEE PRPCPDVAAG KNFTEGIAVI FKENIAPYKF TATMYYKEIT
VTQTWQGSRY LQLTGLYNDR APVPFEEITD VINAKGLCRS DVTYVRSQRR VTAYDRDEWG
REVKLVPSKT STPNSRGWYT TDRMYAPNAH AGFYKAGTTV NCIVEEVEAR SAYPYSNFVL
ATGDFVYVSP FYGLGEDAHR EYNAYSADRF KQVDGFFPRD LDSGETAPEP VVRNLLTTPK
FTIGWDWKPK DPSVCSVTKW QEVEEMMRAE YGSTFRFTSS SLSATFTTNV TQYPPQRIEL
SDCVAREAQA AVDAIYARRY NASHVKVGGL QYYLAQGGFL VVYQPLISNS LAEMYLREAE
ARALEPAPLP TTPAPEAAGS RGTLSTTQSV EFARLQFTYD HIQKHVNEML GRIAAAWCQL
QNQELVLWNE ARKLNPNAIA SATVGRRVGA RMLGDVMAVS TCIAVAPHNV IMQNSMRLPA
RPKTCYARPL VSFRYADEGE LIEGQLGEDN EIRLEQNNLE PCTVGHKRYF VFGDGYVYFE
EYAYSHQVSR ADVPVVSTFV DLNLTMLEDH EFLPLEVYTR QEIKDSGLLD YAEVQRRNQM
HALRFSDIDH IINDTTNAAL MDGLFRFFDG LGAAGQAIGK AVLGVTEAVI SVVSGVSSFL
SNPFGALAVG LLVLAGLTAA FFALRYIMRL RANPMRALYP ITTHGIKAEA KASLASGEPR
SGPGGIEDFD EAKLEEARTM IKYMTLVSAM ERTAHKAKKR GTSARISRHL TDMVLRKRNT
ARPPSSEYQP ILEDEDDAAV
