GB_GPCMV
ID GB_GPCMV Reviewed; 901 AA.
AC Q69024; E9RH71;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 29-SEP-2021, entry version 82.
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 Guinea pig cytomegalovirus (strain 22122) (GPCMV).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Quwivirus.
OX NCBI_TaxID=103920;
OH NCBI_TaxID=10141; Cavia porcellus (Guinea pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8009831; DOI=10.1006/viro.1994.1333;
RA Schleiss M.R.;
RT "Cloning and characterization of the guinea pig cytomegalovirus
RT glycoprotein B gene.";
RL Virology 202:173-185(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19014498; DOI=10.1186/1743-422x-5-139;
RA Schleiss M.R., McGregor A., Choi K.Y., Date S.V., Cui X., McVoy M.A.;
RT "Analysis of the nucleotide sequence of the guinea pig cytomegalovirus
RT (GPCMV) genome.";
RL Virol. J. 5:139-139(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22122/ATCC-P5;
RX PubMed=21270288; DOI=10.1099/vir.0.027789-0;
RA Kanai K., Yamada S., Yamamoto Y., Fukui Y., Kurane I., Inoue N.;
RT "Re-evaluation of the genome sequence of guinea pig cytomegalovirus.";
RL J. Gen. Virol. 92:1005-1020(2011).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22122;
RX PubMed=23516193; DOI=10.1128/genomea.00054-13;
RA Yang D., Tamburro K., Dittmer D., Cui X., McVoy M.A.,
RA Hernandez-Alvarado N., Schleiss M.R.;
RT "Complete genome sequence of pathogenic Guinea pig cytomegalovirus from
RT salivary gland homogenates of infected animals.";
RL Genome Announc. 1:E0005413-E0005413(2013).
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; KC503762; AGE11534.1; -; Genomic_DNA.
DR EMBL; AB592928; BAJ78523.1; -; Genomic_DNA.
DR RefSeq; YP_007417830.1; NC_020231.1.
DR SMR; Q69024; -.
DR PRIDE; Q69024; -.
DR GeneID; 14536657; -.
DR KEGG; vg:14536657; -.
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..34
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 35..901
FT /note="Envelope glycoprotein B"
FT /id="PRO_0000038191"
FT TOPO_DOM 35..736
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 737..757
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 758..901
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 141..147
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 226..233
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 683..734
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 714..734
FT /note="Hydrophobic membrane proximal region"
FT REGION 794..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 890..893
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT SITE 451..452
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 372
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 406
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 84..533
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 101..489
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 174..239
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 331..380
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 559..596
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 901 AA; 102240 MW; 43ABCA7D45A197AA CRC64;
MRPVRGIARS RILSCSWRGT WTSALTILYL GVYCESTTVT PTTVEDTTVS NGNHSDASRN
NTVIRNLTAS VDFSQRKLYP YRICSMSMGT DLVRFARTIQ CVPFNPRVNS EEGIMLIYKR
NILPYVFTAY TYQKELLFQR SYKYVTYDYL LGYSREFVAL PMWEIFLVNS RGQCYTSHQR
VIGADRYIAY HNDNEVNETM WLMRDDMGND DTYRYITVKE HARTPGSVWL YKETCSMNCI
VTKTKGKSKF PYDMFVLPSG VIVNISPFYN GSNGKTFREQ REKFHIWSNY SILKDFGSRA
LEARIVPKMA FYEREDVVIG WEVNDQSNVT CEMILWETVD RAIRTEYENA FHYVARTLTS
TFVENKYSPD NNLTEDDIKC FKNDAQKKIE EVFLRDYNET YDMDGNATYH VTTGGLVIVW
QGLKQKSLKA LEIAANESAV SATGSNSRRK RSLPDESTGD ISYAQLQFAY DTLRTYINQA
LGHIAEAWCL DQKRTAEVLH ELSKINPSNI LSAIFGVPVA ARVVGDVISL AKCIEVNQST
VLIKGDMRKF SDDGKLEGCY SRPVVWFSMK NSTEVRLGQL GEDNEILLGT HRMETCQTQD
YRIFVAGDIG YEFQQYVFTK KINLSEIDII DTMIALKTEP LENIDFKVLE LYSRDELAQA
NVFDLESIMR EYNYQKKRLD FVVERVINPI PPALKGLDEM MNGMGAIGKG IGEAVGAVGG
AIGSFIGALV TFVTNPFGAF VVFLFCVGCI TLVITVYRRQ RRAMQRPFDY FFPYASQTIT
SSVADSSIAV AYPGPEGTSG DAPPPYPGEA PYGYKDLSVD ADTRVSSSSA GAGADFNEED
AVRMLRAIKR LDDKKRQEIE KSSKDSASNK NSETRRRPGI MDRLRRRGGY QKLNTEDDVH
V
