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GB_EHV1B
ID   GB_EHV1B                Reviewed;         980 AA.
AC   Q6DLH8; P28922;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   02-JUN-2021, entry version 83.
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=GP14;
GN   OrderedLocusNames=33;
OS   Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31520;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA   Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus-1.";
RL   Virology 189:304-316(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; AY665713; AAT67290.1; -; Genomic_DNA.
DR   PIR; G36798; VGBEC6.
DR   RefSeq; YP_053078.1; NC_001491.2.
DR   SMR; Q6DLH8; -.
DR   GeneID; 1487545; -.
DR   KEGG; vg:1487545; -.
DR   Proteomes; UP000001189; 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; -; 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   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..86
FT                   /evidence="ECO:0000255"
FT   CHAIN           87..980
FT                   /note="Envelope glycoprotein B"
FT                   /id="PRO_0000038172"
FT   TOPO_DOM        87..849
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   TRANSMEM        850..870
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   TOPO_DOM        871..980
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..203
FT                   /note="Involved in fusion and/or binding to host membrane"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   REGION          282..290
FT                   /note="Involved in fusion and/or binding to host membrane"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   REGION          505..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..847
FT                   /note="Hydrophobic membrane proximal region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   REGION          823..843
FT                   /note="Hydrophobic membrane proximal region"
FT   MOTIF           925..928
FT                   /note="Golgi targeting"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   MOTIF           965..968
FT                   /note="Internalization motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   COMPBIAS        95..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..529
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            521..522
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   CARBOHYD        380
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   CARBOHYD        497
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   CARBOHYD        514
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   CARBOHYD        515
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   CARBOHYD        560
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   CARBOHYD        727
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   CARBOHYD        749
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   DISULFID        140..647
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   DISULFID        157..603
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   DISULFID        231..296
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   DISULFID        389..437
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   DISULFID        668..708
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ   SEQUENCE   980 AA;  109805 MW;  A6DDFA8CA5550FF5 CRC64;
     MSSGCRSVGG STWGNWRGDG GDLRQRRVLS PVCSAPAAGS WIGSQLGNVG NLLATPHPLG
     KPASSRVGTI VLACLLLFGS CVVRAVPTTP SPPTSTPTSM STHSHGTVDP TLLPTETPDP
     LRLAVRESGI LAEDGDFYTC PPPTGSTVVR IEPPRTCPKF DLGRNFTEGI AVIFKENIAP
     YKFRANVYYK DIVVTRVWKG YSHTSLSDRY NDRVPVSVEE IFGLIDSKGK CSSKAEYLRD
     NIMHHAYHDD EDEVELDLVP SKFATPGARA WQTTNDTTSY VGWMPWRHYT STSVNCIVEE
     VEARSVYPYD SFALSTGDIV YASPFYGLRA AARIEHNSYA QERFRQVEGY RPRDLDSKLQ
     AEEPVTKNFI TTPHVTVSWN WTEKKVEACT LTKWKEVDEL VRDEFRGSYR FTIRSISSTF
     ISNTTQFKLE SAPLTECVSK EAKEAIDSIY KKQYESTHVF SGDVEYYLAR GGFLIAFRPM
     LSNELARLYL NELVRSNRTY DLKNLLNPNA NNNNNTTRRR RSLLSVPEPQ PTQDGVHREQ
     ILHRLHKRAV EATAGTDSSN VTAKQLELIK TTSSIEFAML QFAYDHIQSH VNEMLSRIAT
     AWCTLQNKER TLWNEMVKIN PSAIVSATLD ERVAARVLGD VIAITHCAKI EGNVYLQNSM
     RSMDSNTCYS RPPVTFTITK NANNRGSIEG QLGEENEIFT ERKLIEPCAL NQKRYFKFGK
     EYVYYENYTF VRKVPPTEIE VISTYVELNL TLLEDREFLP LEVYTRAELE DTGLLDYSEI
     QRRNQLHALR FYDIDSVVNV DNTAVIMQGI ASFFKGLGKV GEAVGTLVLG AAGAVVSTVS
     GIASFLNNPF GGLAIGLLVI AGLVAAFFAY RYVMQIRSNP MKALYPITTK ALKNKAKTSY
     GQNEEDDGSD FDEAKLEEAR EMIKYMSMVS ALEKQEKKAI KKNSGVGLIA SNVSKLALRR
     RGPKYTRLQQ NDTMENEKMV
 
 
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