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GN_HHV7J
ID   GN_HHV7J                Reviewed;          86 AA.
AC   P52366;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Envelope glycoprotein N {ECO:0000255|HAMAP-Rule:MF_04037};
DE   Flags: Precursor;
GN   Name=gN {ECO:0000255|HAMAP-Rule:MF_04037}; ORFNames=U46;
OS   Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=57278;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA   Nicholas J.;
RT   "Determination and analysis of the complete nucleotide sequence of human
RT   herpesvirus.";
RL   J. Virol. 70:5975-5989(1996).
CC   -!- FUNCTION: Envelope glycoprotein necessary for proper maturation of gM
CC       and modulation of its membrane fusion activity. Also plays a critical
CC       role in virion morphogenesis. {ECO:0000255|HAMAP-Rule:MF_04037}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with gM (via N-terminus). The gM-gN
CC       heterodimer forms the gCII complex. {ECO:0000255|HAMAP-Rule:MF_04037}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04037}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04037}. Host membrane {ECO:0000255|HAMAP-Rule:MF_04037};
CC       Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04037}.
CC       Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-
CC       Rule:MF_04037}. Note=When coexpressed with gM, localizes in the host
CC       trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04037}.
CC   -!- SIMILARITY: Belongs to the herpesviridae glycoprotein N family.
CC       {ECO:0000255|HAMAP-Rule:MF_04037}.
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DR   EMBL; U43400; AAC54708.1; -; Genomic_DNA.
DR   PIR; T41948; T41948.
DR   RefSeq; YP_073786.1; NC_001716.2.
DR   PRIDE; P52366; -.
DR   DNASU; 3289504; -.
DR   GeneID; 3289504; -.
DR   KEGG; vg:3289504; -.
DR   Proteomes; UP000009246; Genome.
DR   GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   HAMAP; MF_04037; HSV_GN; 1.
DR   InterPro; IPR005211; Herpes_glycoprotein_N_domain.
DR   InterPro; IPR034707; HSV_GN.
DR   Pfam; PF03554; Herpes_UL73; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Host Golgi apparatus; Host membrane; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW   Viral envelope protein; Virion.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   CHAIN           30..86
FT                   /note="Envelope glycoprotein N"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT                   /id="PRO_0000116217"
FT   TOPO_DOM        30..47
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   TOPO_DOM        69..86
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   DISULFID        38
FT                   /note="Interchain (with gM)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
SQ   SEQUENCE   86 AA;  10196 MW;  E1006BAC5266E1B5 CRC64;
     MTLYKIVSKP IILLAFFFTR VVFTNEVDGE ELFYKPTCHS DTYEIILKKF SSIWILVNTF
     ILLCSFSLFL KYWCFKTLAK ETVKGY
 
 
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