GB_SHV21
ID GB_SHV21 Reviewed; 808 AA.
AC P24905;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 29-SEP-2021, entry version 90.
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=KCRF1; ORFNames=8;
OS Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=10383;
OH NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2154888; DOI=10.1016/0042-6822(90)90107-3;
RA Albrecht J.-C., Fleckenstein B.;
RT "Structural organization of the conserved gene block of Herpesvirus saimiri
RT coding for DNA polymerase, glycoprotein B, and major DNA binding protein.";
RL Virology 174:533-542(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA Honess R.W.;
RT "Primary structure of the herpesvirus saimiri genome.";
RL J. Virol. 66:5047-5058(1992).
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; X64346; CAA45631.1; -; Genomic_DNA.
DR EMBL; M31122; AAA46164.1; -; Genomic_DNA.
DR RefSeq; NP_040210.1; NC_001350.1.
DR SMR; P24905; -.
DR PRIDE; P24905; -.
DR GeneID; 1682521; -.
DR KEGG; vg:1682521; -.
DR Proteomes; UP000000587; 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; 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; -; 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 3: Inferred from homology;
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..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 20..808
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038182"
FT TOPO_DOM 20..701
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 723..808
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 101..107
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 187..195
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 647..699
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 658..698
FT /note="Hydrophobic membrane proximal region"
FT SITE 410..411
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 344
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 361
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 45..498
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 62..454
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 136..201
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 291..338
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 520..557
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 808 AA; 91695 MW; FA1BCB89B9D5672E CRC64;
MVPNKHLLLI ILSFSTACGQ TTPTTAVEKN KTQAIYQEYF KYRVCSASTT GELFRFDLDR
TCPSTEDKVH KEGILLVYKK NIVPYIFKVR RYKKITTSVR IFNGWTREGV AITNKWELSR
AVPKYEIDIM DKTYQCHNCM QIEVNGMLNS YYDRDGNNKT VDLKPVDGLT GAITRYISQP
KVFADPGWLW GTYRTRTTVN CEIVDMFARS ADPYTYFVTA LGDTVEVSPF CDVDNSCPNA
TDVLSVQIDL NHTVVDYGNR ATSQQHKKRI FAHTLDYSVS WEAVNKSASV CSMVFWKSFQ
RAIQTEHDLT YHFIANEITA GFSTVKEPLA NFTSDYNCLM THINTTLEDK IARVNNTHTP
NGTAEYYQTE GGMILVWQPL IAIELEEAML EATTSPVTPS APTSSSRSKR AIRSIRDVSA
GSENNVFLSQ IQYAYDKLRQ SINNVLEELA ITWCREQVRQ TMVWYEIAKI NPTSVMTAIY
GKPVSRKALG DVISVTECIN VDQSSVSIHK SLKTENNDIC YSRPPVTFKF VNSSQLFKGQ
LGARNEILLS ESLVENCHQN AETFFTAKNE TYHFKNYVHV ETLPVNNIST LDTFLALNLT
FIENIDFKAV ELYSSGERKL ANVFDLETMF REYNYYAQSI SGLRKDFDNS QRNNRDRIIQ
DFSEILADLG SIGKVIVNVA SGAFSLFGGI VTGILNFIKN PLGGMFTFLL IGAVIILVIL
LVRRTNNMSQ APIRMIYPDV EKSKSTVTPM EPETIKQILL GMHNMQQEAY KKKEEQRAAR
PSIFRQAAET FLRKRSGYKQ ISTEDKIV
