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Envelope glycoprotein B (gB)

 GB_ALHV1                Reviewed;         854 AA.
O36362;
08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
28-MAR-2018, entry version 61.
RecName: Full=Envelope glycoprotein B {ECO:0000255|HAMAP-Rule:MF_04032};
Short=gB {ECO:0000255|HAMAP-Rule:MF_04032};
Flags: Precursor;
Name=gB {ECO:0000255|HAMAP-Rule:MF_04032}; Synonyms=8;
Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal
fever virus).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Gammaherpesvirinae; Macavirus.
NCBI_TaxID=654901;
NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest).
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=9261371;
Ensser A., Pflanz R., Fleckenstein B.;
"Primary structure of the alcelaphine herpesvirus 1 genome.";
J. Virol. 71:6517-6525(1997).
-!- FUNCTION: Envelope glycoprotein that forms spikes at the surface
of virion envelope. Essential for the initial attachment to
heparan sulfate moities of the host cell surface proteoglycans.
Involved in fusion of viral and cellular membranes leading to
virus entry into the host cell. Following initial binding to its
host receptors, membrane fusion is mediated by the fusion
machinery composed at least of gB and the heterodimer gH/gL. May
be involved in the fusion between the virion envelope and the
outer nuclear membrane during virion egress. {ECO:0000255|HAMAP-
Rule:MF_04032}.
-!- SUBUNIT: Homotrimer; disulfide-linked. Binds to heparan sulfate
proteoglycans. Interacts with gH/gL heterodimer.
{ECO:0000255|HAMAP-Rule:MF_04032}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04032}; Single-pass type I membrane protein
{ECO:0000255|HAMAP-Rule:MF_04032}. Host cell membrane
{ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane
{ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi apparatus
membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I
membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Note=During
virion morphogenesis, this protein probably accumulates in the
endosomes and trans-Golgi where secondary envelopment occurs. It
is probably transported to the cell surface from where it is
endocytosed and directed to the trans-Golgi network (TGN).
{ECO:0000255|HAMAP-Rule:MF_04032}.
-!- PTM: A proteolytic cleavage by host furin generates two subunits
that remain linked by disulfide bonds. {ECO:0000305}.
-!- SIMILARITY: Belongs to the herpesviridae glycoprotein B family.
{ECO:0000255|HAMAP-Rule:MF_04032}.
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EMBL; AF005370; AAC58059.1; -; Genomic_DNA.
PIR; T03107; T03107.
RefSeq; NP_065511.1; NC_002531.1.
SMR; O36362; -.
GeneID; 911747; -.
KEGG; vg:911747; -.
KO; K19255; -.
OrthoDB; VOG0900002K; -.
Proteomes; UP000000941; Genome.
GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
Gene3D; 2.30.29.100; -; 1.
HAMAP; MF_04032; HSV_GB; 1.
InterPro; IPR035377; Glycoprot_B_PH1.
InterPro; IPR035381; Glycoprot_B_PH2.
InterPro; IPR038631; Glycoprot_B_PH2_sf.
InterPro; IPR000234; Herpes_Glycoprot_B.
Pfam; PF17416; Glycoprot_B_PH1; 1.
Pfam; PF17417; Glycoprot_B_PH2; 1.
3: Inferred from homology;
Complete proteome; Disulfide bond; Glycoprotein; Host cell membrane;
Host endosome; Host Golgi apparatus; Host membrane;
Host-virus interaction; Membrane; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Virion; Virus entry into host cell.
SIGNAL 1 22 {ECO:0000255|HAMAP-Rule:MF_04032}.
CHAIN 23 854 Envelope glycoprotein B.
{ECO:0000255|HAMAP-Rule:MF_04032}.
/FTId=PRO_0000405745.
TOPO_DOM 23 732 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04032}.
TRANSMEM 733 753 Helical. {ECO:0000255|HAMAP-
Rule:MF_04032}.
TOPO_DOM 754 854 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04032}.
REGION 125 131 Involved in fusion and/or binding to host
membrane. {ECO:0000255|HAMAP-
Rule:MF_04032}.
REGION 209 217 Involved in fusion and/or binding to host
membrane. {ECO:0000255|HAMAP-
Rule:MF_04032}.
REGION 679 730 Hydrophobic membrane proximal region.
{ECO:0000255|HAMAP-Rule:MF_04032}.
MOTIF 839 842 Internalization motif.
{ECO:0000255|HAMAP-Rule:MF_04032}.
COMPBIAS 425 432 Poly-Thr.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04032}.
CARBOHYD 180 180 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04032}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04032}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04032}.
CARBOHYD 364 364 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04032}.
CARBOHYD 379 379 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04032}.
CARBOHYD 385 385 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04032}.
CARBOHYD 424 424 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04032}.
CARBOHYD 564 564 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04032}.
CARBOHYD 630 630 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04032}.
DISULFID 69 527 {ECO:0000255|HAMAP-Rule:MF_04032}.
DISULFID 86 483 {ECO:0000255|HAMAP-Rule:MF_04032}.
DISULFID 158 223 {ECO:0000255|HAMAP-Rule:MF_04032}.
DISULFID 315 362 {ECO:0000255|HAMAP-Rule:MF_04032}.
DISULFID 552 589 {ECO:0000255|HAMAP-Rule:MF_04032}.
SEQUENCE 854 AA; 97060 MW; 480D7CF352D5B59C CRC64;
MAHTGSTVCA FLIFAVLKNV FCQTPTSSSE VEDVIPEANT VSDNIIRQQR NNTAKGIHSD
PSAFPFRVCS ASNIGDIFRF QTSHSCPNTK DKEHNEGILL IFKENIVPYV FKVRKYRKIV
TTSTIYNGIY ADAVTNQHVF SKSVPIYETR RMDTIYQCYN SLDVTVGGNL LVYTDNDGSN
MTVDLQPVDG LSNSVRRYHS QPEIHAEPGW LLGGYRRRTT VNCEVTETDA RAVPPFRYFI
TNIGDTIEMS PFWSKAWNET EFSGEPDRTL TVAKDYRVVD YKFRGTQPQG HTRIFVDKEE
YTLSWAQQFR NISYCRWAHW KSFDNAIKTE HGKSLHFVAN DITASFYTPN TQTREVLGKH
VCLNNTIESE LKSRLAKVND THSPNGTAQY YLTNGGLLLV WQPLVQQKLL DAKGLLDAVK
KQQNTTTTTT TTRSRRQRRS VSSGIDDVYT AESTILLTQI QFAYDTLRAQ INNVLEELSR
AWCREQHRAS LMWNELSKIN PTSVMSSIYG RPVSAKRIGD VISVSHCVVV DQDSVSLHRS
MRVPGRDKTH ECYSRPPVTF KFINDSHLYK GQLGVNNEIL LTTTAVEICH ENTEHYFQGG
NNMYFYKNYR HVKTMPVGDV ATLDTFMVLN LTLVENIDFQ VIELYSREEK RMSTAFDIET
MFREYNYYTQ RVTGLRRDLT DLATNRNQFV DAFGSLMDDL GVVGKTVLNA VSSVATLFSS
IVSGIINFIK NPFGGMLLFG LIAAVVITVI LLNRKAKRFA QNPVQMIYPD IKTITSQREE
LQVDPISKHE LDRIMLAMHD YHASKQPESK QDEEQGSTTS GPADWLNKAK NVLRRRAGYK
PLKRTDSFES TGVP


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