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GB_GAHVR
ID   GB_GAHVR                Reviewed;         865 AA.
AC   P18538;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   02-JUN-2021, entry version 92.
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};
OS   Gallid herpesvirus 2 (strain RB-1b) (GaHV-2) (Marek's disease herpesvirus
OS   type 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX   NCBI_TaxID=33707;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2544666; DOI=10.1099/0022-1317-70-7-1789;
RA   Ross L.J.N., Sanderson M., Scott S.D., Binns M.M., Doel T., Milne B.;
RT   "Nucleotide sequence and characterization of the Marek's disease virus
RT   homologue of glycoprotein B of herpes simplex virus.";
RL   J. Gen. Virol. 70:1789-1804(1989).
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; D13713; BAA02866.1; -; Genomic_DNA.
DR   RefSeq; YP_001033956.1; NC_002229.3.
DR   SMR; P18538; -.
DR   PRIDE; P18538; -.
DR   GeneID; 4811501; -.
DR   KEGG; vg:4811501; -.
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..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   CHAIN           22..865
FT                   /note="Envelope glycoprotein B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT                   /id="PRO_0000038176"
FT   TOPO_DOM        22..731
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   TRANSMEM        732..752
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   TOPO_DOM        753..865
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   REGION          106..112
FT                   /note="Involved in fusion and/or binding to host membrane"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   REGION          191..198
FT                   /note="Involved in fusion and/or binding to host membrane"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   REGION          676..729
FT                   /note="Hydrophobic membrane proximal region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   REGION          683..729
FT                   /note="Hydrophobic membrane proximal region"
FT   REGION          843..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           809..812
FT                   /note="Golgi targeting"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   MOTIF           850..853
FT                   /note="Internalization motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   SITE            434..435
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   CARBOHYD        364
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        425
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   CARBOHYD        631
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   DISULFID        49..530
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   DISULFID        66..486
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   DISULFID        140..204
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   DISULFID        298..346
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT   DISULFID        553..590
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ   SEQUENCE   865 AA;  98092 MW;  B30E93C1AC65C6C3 CRC64;
     MHYFRRNCIF FLIVILYGTN SSPSTQNVTS REVVSSVQLS EEESTFYLCP PPVGSTVIRL
     EPPRKCPEPR KATEWGEGIA ILFKENISPY KFKVTLYYKN IIQTTTWTGT TYRQITNRYT
     DRTPVSIEEI TDLIDGKGRC SSKARYLRNN VYVEAFDRDA GEKQVLLKPS KFNTPESRAW
     HTTNETYTVW GSPWIYRTGT SVNCIVEEMD ARSVFPYSYF AMANGDIANI SPFYGLSPPE
     AAAEPMGYPQ DNFKQLDSYF SMDLDKRRKA SLPVKRNFLI TSHFTVGWDW APKTTRVCSM
     TKWKEVTEML RATVNGRYRF MARELSATFI SNTTEFDPNR IILGQCIKRE AEAAIEQIFR
     TKYNDSHVKV GHVQYFLALG GFIVAYQPVL SKSLAHMYLR ELMRDNRTDE MLDLVNNKHA
     IYKKNATSLS RLRRDIRNAP NRKITLDDTT AIKSTSSVQF AMLQFLYDHI QTHINDMFSR
     IATAWCELQN RELVLWHEGI KINPSATASA TLGRRVAAKM LGDVAAVSSC TAIDAESVTL
     QNSMRVITST NTCYSRPLVL FSYGENQGNI QGQLGENNEL LPTLEAVEPC SANHRRYFLF
     GSGYALFENY NFVKMVDAAD IQIASTFVEL NLTLLEDREI LPLSVYTKEE LRDVGVLDYA
     EVARRNQLHE LKFYDINKVI EVDTNYAFMN GLAELFNGMG QVGQAIGKVV VGAAGAIVST
     ISGVSAFMSN PFGALAIGLI IIAGLVAAFL AYRYVNKLKS NPMKALYPMT TEVLKAQATR
     ELHGEESDDL ERTSIDERKL EEAREMIKYM ALVSAEERHE KKLRRKRRGT TAVLSDHLAK
     MRIKNSNPKY DKLPTTYSDS EDDAV
 
 
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