位置:首页 > 蛋白库 > GH_EBVA8
GH_EBVA8
ID   GH_EBVA8                Reviewed;         706 AA.
AC   Q1HVD2;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 50.
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=BXLF2;
OS   Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=82830;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16490228; DOI=10.1016/j.virol.2006.01.015;
RA   Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.;
RT   "The genome of Epstein-Barr virus type 2 strain AG876.";
RL   Virology 350:164-170(2006).
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. The heterodimer gH/gL targets also host EPHA2 to promote
CC       viral entry. {ECO:0000250|UniProtKB:P03231, ECO:0000255|HAMAP-
CC       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       The heterodimer gH/gL interacts with host EPHA2 to facilitate virus
CC       internalization and fusion. Interacts with glycoprotein 42/BZLF2.
CC       {ECO:0000250|UniProtKB:P03231, 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ279927; ABB89276.1; -; Genomic_DNA.
DR   RefSeq; YP_001129496.1; NC_009334.1.
DR   SMR; Q1HVD2; -.
DR   PRIDE; Q1HVD2; -.
DR   GeneID; 5176171; -.
DR   KEGG; vg:5176171; -.
DR   Proteomes; UP000007639; Genome.
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   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   Disulfide bond; 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;
KW   Reference proteome; Sialic acid; Signal; Transmembrane;
KW   Transmembrane helix; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CHAIN           19..706
FT                   /note="Envelope glycoprotein H"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT                   /id="PRO_0000436648"
FT   TOPO_DOM        19..682
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   TRANSMEM        683..703
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   TOPO_DOM        704..706
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   REGION          165..229
FT                   /note="Interaction with gL"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        549
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        604
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        664
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   DISULFID        278..335
FT                   /evidence="ECO:0000250|UniProtKB:P03231"
FT   DISULFID        454..478
FT                   /evidence="ECO:0000250|UniProtKB:P03231"
FT   DISULFID        534..587
FT                   /evidence="ECO:0000250|UniProtKB:P03231"
FT   DISULFID        612..615
FT                   /evidence="ECO:0000250|UniProtKB:P03231"
SQ   SEQUENCE   706 AA;  78334 MW;  8D14BDB4E0E189AA CRC64;
     MQLLCVFCLV LLWEVGAASL SEVKLHLDIE GHASHYTIPW TELMAKVPGL SPEALWREAN
     VTEDLASMLN RYKLIYKTSG TLGIALAEPV DIPAVSEGSM QVDASKVHPG VISGLNSPAC
     MLSAPLEKQL FYYIGTMLPN TRPHSYVFYQ LRCHLSYVAL SINGDKFQYT GAMTSKFLMG
     TYKRVTEKGD EHVLSLIFGK TKDLPDLRGP FSYPSLTSAQ SGDYSLVIVT TFVHYANFHN
     YFVPNLKDMF SRAVTMTAAS YARYVLQKLV LLEMKGGCRE PELDTETLTT MFEVSVAFFK
     VGHAVGETGN GCVDLRWLAK SFFELTVLKD IIGICYGATV KGMQSYGLER LAAVLMATVK
     MEELGHLTTE KQEYALRLAT VGYPKAGVYS GLIGGATSVL LSAYNRHPLF QPLHTVMRET
     LFIGSHVVLR ELRLNVTTQG PNLALYQLLS TALCSALEIG EVLRGLALGT ESGLFSPCYL
     SLRFDLTRDK LLSMAPQEAM LDQAAVSNAV DGFLGRLSLE REDRDAWHLP AYKCVDRLDK
     VLMIIPLINV TFIISSDREV RGSALYEAST TYLSSSLFLS PVIMNKCSQG AVAGEPRQIP
     KIQNFTRTQK SCIFCGFALL SYDEKEGLET TTYITSQEVQ NSILSSNYFD FDNLHVHYLL
     LTTNGTVMEI AGLYEERAHV VLAIILYFIA FALGIFLVHK IVMFFL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024