GB_HSVA1
ID GB_HSVA1 Reviewed; 933 AA.
AC Q04463;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 Herpesvirus ateles type 1 (strain Lennette).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=35243;
OH NCBI_TaxID=9506; Ateles.
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 -!- CAUTION: It is uncertain whether Met-1 or Met-30 is the initiator.
CC {ECO:0000305}.
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DR EMBL; M95785; AAA43839.1; -; Genomic_DNA.
DR PIR; B48349; B48349.
DR SMR; Q04463; -.
DR PRIDE; Q04463; -.
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..36
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 37..933
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038181"
FT TOPO_DOM 37..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..933
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 36..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..199
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 278..285
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 742..795
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 754..795
FT /note="Hydrophobic membrane proximal region"
FT MOTIF 881..884
FT /note="Golgi targeting"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MOTIF 920..923
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT COMPBIAS 56..70
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 450
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 CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 136..596
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 153..552
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 227..291
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 384..432
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 619..656
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 933 AA; 101492 MW; 13A6CF88BB5A18DF CRC64;
MPRPRPRALR GSSPGWALVA AVAVGAALLM ATLAVAAPPG PRGPAARSPG LEDASVEPVE
DGDYDEYDDE GHTPTDVPGS GPESPGPDRP PRGPGGGSGR RRGSPGNGTR SAARRQLRES
LRRIQAEYAA SAFYVCPPPT GATVVQFEEP RPCPDVAAGK NFTEGIAVVF KENIAPYKFT
ATKYYKEITV SQTWQGSRYL QLTGLYNDRA PVPFSEITDL INGKGRCRSD VTYTRSQRRV
TAYDGDEWGR EVALVPAKTS TPNSRGWYTT DRVYAPNAHA GFYKTGTTVN CIVEEMEARS
AFPYDSFVLA TGEFVYASPF SGFSEDARRE RNRYAPDRFR QVDGFYPRDL DSGQRAATPV
VRNLLTTPTF TVGWDWKPKR PNVCSVTKWQ VVEEMVRAEY GSAFRFTSAA LSATFTSNLT
QYPPELIEHS DCVAREAAES IEAIYARRYN ASHVRVGGVQ YYLAAGGFLL AFQPLLSNSL
AEMYRREALL GRSGDLAAAL APPPVAAPAS GAGPRGTIST TQTVEFARLQ FTYDHIQKHV
NEMLGRIAAA WCQLQNQELV LWNEARKLNP GAIASATVGT RVGARMLGDV MAVSTCIPVS
PDNVIMQNSM RIPGDPKTCY ARPLVSFRYT DEGELVEGQL GEDNEIRLEQ NNVEPCTVGH
KRYFVFGGGY VYFEEYAYSH QVSRADVPVV STFVDLNLTM LEDHEFLPLE VYTRREIKDS
GLLDYAEVQR RNQLHALRFS DIDRIMNDSA NAALMAGLAR FFDGMGDAGK AIGRAVLGVT
EGLISVVSGV SSFLSNPFGA LAVGLLVLAG LVAAFFAMRY IMRLRANPMR ALYPLTTSGI
KAEARAALGS GGDKGGAGDG AAGVEDFDEA KLEAARDMIR YMTLVSAMER TAHKAKKRGT
SARISAHLTD MVLAAQGAEY QPLSKDDEDG ADP
