GB_MUHVS
ID GB_MUHVS Reviewed; 928 AA.
AC P27171;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 29-SEP-2021, entry version 80.
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=UL55;
OS Murid herpesvirus 1 (strain Smith) (MuHV-1) (Mouse cytomegalovirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Muromegalovirus.
OX NCBI_TaxID=10367;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1318410; DOI=10.1128/jvi.66.7.4399-4406.1992;
RA Rapp M., Messerle M., Buehler B., Tannheimer M., Keil G.M.,
RA Koszinowski U.H.;
RT "Identification of the murine cytomegalovirus glycoprotein B gene and its
RT expression by recombinant vaccinia virus.";
RL J. Virol. 66:4399-4406(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-280.
RX PubMed=1329325; DOI=10.1016/0042-6822(92)90198-x;
RA Messerle M., Keil G.M., Schneider K., Koszinowski U.H.;
RT "Characterization of the murine cytomegalovirus genes encoding the major
RT DNA binding protein and the ICP18.5 homolog.";
RL Virology 191:355-367(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8971012; DOI=10.1128/jvi.70.12.8833-8849.1996;
RA Rawlinson W.D., Farrell H.E., Barrell B.G.;
RT "Analysis of the complete DNA sequence of murine cytomegalovirus.";
RL J. Virol. 70:8833-8849(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 514-928.
RX PubMed=1718083; DOI=10.1016/0042-6822(91)90765-4;
RA Elliott R., Clark C., Jaquish D., Spector D.H.;
RT "Transcription analysis and sequence of the putative murine cytomegalovirus
RT DNA polymerase gene.";
RL Virology 185:169-186(1991).
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:0000250}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein B family.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
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DR EMBL; M86302; AAA45936.1; -; Genomic_DNA.
DR EMBL; X67021; CAA47416.1; -; Genomic_DNA.
DR EMBL; U68299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M73549; AAA45939.1; -; Genomic_DNA.
DR PIR; A41992; VGBEMC.
DR SMR; P27171; -.
DR Proteomes; UP000008774; 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..37
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 38..928
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038195"
FT TOPO_DOM 38..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..928
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 40..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..173
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 252..259
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 729..781
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 740..780
FT /note="Hydrophobic membrane proximal region"
FT REGION 826..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 916..919
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT SITE 497..498
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 111..581
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 127..537
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 200..265
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 357..411
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 606..643
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CONFLICT 522
FT /note="K -> R (in Ref. 4; AAA45939)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="D -> E (in Ref. 4; AAA45939)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="S -> T (in Ref. 4; AAA45939)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="I -> V (in Ref. 4; AAA45939)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="K -> Q (in Ref. 4; AAA45939)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="S -> K (in Ref. 4; AAA45939)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="I -> V (in Ref. 4; AAA45939)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="E -> D (in Ref. 4; AAA45939)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="D -> Q (in Ref. 4; AAA45939)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="R -> RQRSAAAR (in Ref. 4; AAA45939)"
FT /evidence="ECO:0000305"
FT CONFLICT 890
FT /note="N -> T (in Ref. 4; AAA45939)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 928 AA; 104109 MW; 0EDBF3FE7A43810D CRC64;
MSRRNERGCR SSSWYAMSTA LAVTIWCLLA CTSEVIAAAS TPGTTPKAKT DTSSETASAE
TETATSGAAT GKKEATPTQA SKITGTTIVP FVNETEDMVS VDIDKYPYRV CMAVSTDLVR
FGKSIDCINH TPKTPVQEGI MVVYKENIVA YTFEVITYHK DAIFQRSYAD TTTNYFLGTS
VTKMAFPIWE LDEVNRNNRC YSAASRILNG EVYVAYHEDS YRNYTMVLVE DDYRSKNSKR
YVTTKSRYHK GAWTWRYTES CNMNCVVVVT KARSNTPYEF FVLSSGEVVE ISPFYNGENS
EPFEEDTRNF WIRKNYTMKT YFGELAAPKK VVPLMAFLER EDMTIGWEIF PKQNVTCDWK
KWQTVSRAIR TDTNTGYHFV SKGLTATFVA SKRKIDYNTT TEGKNYNTFR CVYDEFVEEV
NRVFEDEYNE THVKDGELEM YRTTGGLIVL WQGLKAKSLH NLEKFAALNN VSVATASPPV
TTAATENGTT VRSRRKRSFD NLDDVVTDIS YAQLQFTYDV LKDYINDALR NIMDAWCRDQ
KRTAEMLKEL SKINPSNILS AIYERPVTAK LAGDVIAMSE CVKVDQSSVK VLKDMRIFQD
GKVVNCYSRP LVVFQFINST KLESGQLGEN NEIMLGTFRT ENCDTNSRKI FVVGTVGYEY
RDYRFRNVTS LEHIDLVDTL IGLDIEPLEN TDFKVLELYS KGELRASNVF SLDEIMREYN
SQKQHIRTLS AKVNDNTPSY LLGLDTFMQG LGVAGKGIGV AIGAVGGAVS SVVNAVTGFL
TNPFGGFTTI LLVIGVLAVV YLIFTRPVEY FFPYATQTAV QYAPPGGAHG GLESGPPGAP
GLHRRVNAGG SDDSGKAWTS DKKGLERTYT EQDALLILRA LKQLDDSQRN EKAQQKATRL
PTGILDRLKG NDTSGYQRLP AEDSDFEY
