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GH_BHV1C
ID   GH_BHV1C                Reviewed;         842 AA.
AC   P27599;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Envelope glycoprotein H {ECO:0000255|HAMAP-Rule:MF_04033};
DE            Short=gH {ECO:0000255|HAMAP-Rule:MF_04033};
DE   Flags: Precursor;
GN   Name=gH {ECO:0000255|HAMAP-Rule:MF_04033}; ORFNames=UL22;
OS   Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine
OS   rhinotracheitis virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10323;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1657187; DOI=10.1016/0167-4781(91)90116-4;
RA   Meyer A.L., Petrovskis E.A., Duffus W.P., Thomsen D.R., Post L.E.;
RT   "Cloning and sequence of an infectious bovine rhinotracheitis virus (BHV-1)
RT   gene homologous to glycoprotein H of herpes simplex virus.";
RL   Biochim. Biophys. Acta 1090:267-269(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Schwyzer M., Paces V., Letchworth G.J., Misra V., Buhk H.J., Lowery D.E.,
RA   Simard C., Bello L.J., Thiry E., Vlcek C.;
RT   "Complete DNA sequence of bovine herpesvirus 1.";
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The heterodimer glycoprotein H-glycoprotein L is required for
CC       the fusion of viral and plasma membranes leading to virus entry into
CC       the host cell. Following initial binding to host receptor, membrane
CC       fusion is mediated by the fusion machinery composed of gB and the
CC       heterodimer gH/gL. May also be involved in the fusion between the
CC       virion envelope and the outer nuclear membrane during virion
CC       morphogenesis. {ECO:0000255|HAMAP-Rule:MF_04033}.
CC   -!- SUBUNIT: Interacts with glycoprotein L (gL); this interaction is
CC       necessary for the correct processing and cell surface expression of gH.
CC       The heterodimer gH/gL seems to interact with gB trimers during fusion.
CC       {ECO:0000255|HAMAP-Rule:MF_04033}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04033}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04033};
CC       Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}.
CC       Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass
CC       type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. 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_04033}.
CC   -!- PTM: N-glycosylated, O-glycosylated, and sialylated.
CC       {ECO:0000255|HAMAP-Rule:MF_04033}.
CC   -!- SIMILARITY: Belongs to the herpesviridae glycoprotein H family.
CC       {ECO:0000255|HAMAP-Rule:MF_04033}.
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DR   EMBL; X58867; CAA41677.1; -; Genomic_DNA.
DR   EMBL; Z78205; CAB01604.1; -; Genomic_DNA.
DR   EMBL; AJ004801; CAA06112.1; -; Genomic_DNA.
DR   PIR; S18462; S18462.
DR   RefSeq; NP_045337.1; NC_001847.1.
DR   SMR; P27599; -.
DR   PRIDE; P27599; -.
DR   GeneID; 4783417; -.
DR   KEGG; vg:4783417; -.
DR   GO; GO:0044175; C:host cell endosome 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:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0016032; P:viral process; IMP:AgBase.
DR   Gene3D; 2.60.40.3190; -; 1.
DR   HAMAP; MF_04033; HSV_GH; 1.
DR   InterPro; IPR003493; Herpes_gH.
DR   InterPro; IPR035305; Herpes_glycoH_C.
DR   InterPro; IPR038172; Herpes_glycoH_C_sf.
DR   Pfam; PF17488; Herpes_glycoH_C; 1.
PE   3: Inferred from homology;
KW   Fusion of virus membrane with host cell membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein;
KW   Host cell membrane; Host endosome; Host membrane; Membrane; Sialic acid;
KW   Signal; Transmembrane; Transmembrane helix; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CHAIN           21..842
FT                   /note="Envelope glycoprotein H"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT                   /id="PRO_0000436647"
FT   TOPO_DOM        21..802
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   TRANSMEM        803..823
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   TOPO_DOM        824..842
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   REGION          240..303
FT                   /note="Interaction with gL"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        617
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        666
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        760
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        783
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
SQ   SEQUENCE   842 AA;  88375 MW;  BA90759A74715F98 CRC64;
     MRRPLCAALL AAAVLALAAG APAAARGGAG GRSREHRDAR YEIEEWEMVV GAGPAVHTFT
     IRCLGPRGIE RVAHIANLSR LLDGYIAVHV DVARTSGLRD TMFFLPRAAV DNASAADIPD
     TPAVQSHPGL FGAAFSWSYL QTRHLVDYDL VPSRPLQDWY FSQARAESNA ARPPPAPRVT
     PTPAGRVAAF DINDVLASGP EHFFVPVRAD RKRRERHVAD FAAVWPVSYI PAGRAVLSCE
     RAAARLAVGL GFLSVSVTSR DLLPLEFMVA PADANVRMIT AFNGGGAFPP PGPAAGPQRR
     AYVIGYGNSR LDSHMYLTMR EVASYANEPA DFRAHLTAAH REAFLMLREA AAARRGPSAG
     PAPNAAYHAY RVAARLGLAL SALTEGALAD GYVLAEELVD LDYHLKLLSR VLLGAGLGCA
     ANGRVRARTI AQLAVPRELR PDAFIPEPAG AALESVVARG RKLRAVYAFS GPDAPLAARL
     LAHGVVSDLY DAFLRGELTW GPPMRHALFF AVAASAFPAD AQALELARDV TRKCTAMCTA
     GHATAAALDL EEVYAHVGGG AGGDAGFELL DAFSPCMASF RLDLLEEAHV LDVLSAVPAR
     AALDAWLEAQ PAAAAPNLSA AALGMLGRGG LFGPAHAAAL APELFAAPCG GWGAGAAVAI
     VPVAPNASYV ITRAHPRRGL TYTLQGIDVA NPLLVTFVRG TSCVSASGAV EARRLAVPGP
     LDACAYCGSV FVRYLPSGAV MDIVLIADKR TEVEFSRGAN SSMPVFNPRL HSGRSRAMLL
     FPNGTVVSVL AFAGHEAPTF SPAYVWASVG GALVAGTTIY AIAKMLCSSV PLARGYSSVP
     VF
 
 
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