GenomeNet

Database: UniProt
Entry: LMP1_EBVA8
LinkDB: LMP1_EBVA8
Original site: LMP1_EBVA8 
ID   LMP1_EBVA8              Reviewed;         371 AA.
AC   Q1HVB3;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   11-DEC-2019, entry version 42.
DE   RecName: Full=Latent membrane protein 1;
DE            Short=LMP-1;
DE   AltName: Full=Protein p63;
GN   Name=LMP1; ORFNames=BNLF1;
OS   Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Herpesvirales; Herpesviridae; Gammaherpesvirinae;
OC   Lymphocryptovirus.
OX   NCBI_TaxID=82830;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [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: Acts as a CD40 functional homolog to prevent apoptosis of
CC       infected B-lymphocytes and drive their proliferation. Functions as a
CC       constitutively active tumor necrosis factor receptor that induces the
CC       activation of several signaling pathways, including those of the NF-
CC       kappa-B family. LMP1 signaling leads to up-regulation of antiapoptotic
CC       proteins and provide growth signals in latently infected cells.
CC       Interacts with host UBE2I and subsequently affects the sumoylation
CC       state of several cellular proteins. For example, induces the
CC       sumoylation of host IRF7 thereby limiting its transcriptional activity
CC       and modulating the activation of innate immune responses.
CC       {ECO:0000250|UniProtKB:P03230}.
CC   -!- SUBUNIT: Interacts (via PXQXT motif) with host tumor necrosis factor
CC       receptor-associated factor (TRAF) proteins TRAF1, TRAF2, TRAF3 and
CC       TRAF5. Interacts with human protein ZMYND11; leading to negatively
CC       regulate NF-kappa-B activation. Interacts with host UBE2I; this
CC       interaction induces the sumoylation of various cellular proteins.
CC       Interacts with host IRF7. {ECO:0000250|UniProtKB:P03230}.
CC   -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: Two regions, C-terminal-activating region 1 (CTAR1) and CTAR2,
CC       have been identified within the cytoplasmic carboxy terminal domain
CC       that activates NF-kappa-B. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated on the N-terminus. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the herpesviridae LMP-1 family. {ECO:0000305}.
DR   EMBL; DQ279927; ABB89294.1; -; Genomic_DNA.
DR   RefSeq; YP_001129515.1; NC_009334.1.
DR   PRIDE; Q1HVB3; -.
DR   GeneID; 5176215; -.
DR   KEGG; vg:5176215; -.
DR   KO; K19459; -.
DR   Proteomes; UP000007639; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039652; P:activation by virus of host NF-kappaB transcription factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0039547; P:suppression by virus of host TRAF activity; IEA:UniProtKB-KW.
DR   GO; GO:0039574; P:suppression by virus of host TYK2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro.
DR   InterPro; IPR007961; Herpes_LMP1.
DR   Pfam; PF05297; Herpes_LMP1; 1.
PE   3: Inferred from homology;
KW   Activation of host NF-kappa-B by virus; Host cell membrane; Host membrane;
KW   Host-virus interaction; Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host RLR pathway by virus; Inhibition of host TRAFs by virus;
KW   Inhibition of host TYK2 by virus; Membrane; Oncogene; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation;
KW   Viral immunoevasion.
FT   CHAIN           1..371
FT                   /note="Latent membrane protein 1"
FT                   /id="PRO_0000375961"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..51
FT                   /note="Extracellular"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..75
FT                   /note="Cytoplasmic"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..106
FT                   /note="Extracellular"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..139
FT                   /note="Cytoplasmic"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..163
FT                   /note="Extracellular"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..371
FT                   /note="Cytoplasmic"
FT   REGION          194..232
FT                   /note="CTAR1"
FT   REGION          337..371
FT                   /note="CTAR2"
FT   MOTIF           204..208
FT                   /note="Interaction with host TRAF proteins"
SQ   SEQUENCE   371 AA;  40473 MW;  E9DCE7BF5F174DC9 CRC64;
     MEHDLERGPP GPRRPPRGPP LSSSLGLALL LLLLALLFWL YIVMSDWTGG ALLVLYSFAL
     ILIIIILIIF IFRRDLLCPL GALCLLLLMI TLLLIALWNL HGQALYLGIV LFIFGCLLVL
     GLWIYLLEIL WRLGATIWQL LAFFLAFFLD LILLIIALYL QQNWWTLLVD LLWLLLFLAI
     LIWMYYHGQR HSDEHHHDDS LPHPQQATDD SGHESDSNSN EGRHHLLVTG AGDGPPLCSQ
     NLGAPGGGPD NGPQDPDNTD DNGPQDPDNT DDNGPQDPDN TDDNGPQDPD NTADNGPHDP
     LPHNPSDSAG NDGGPPNLTE EVENKGGDRG PPSMTDGGGG DPHLPTLLLG TSGSGGDDDD
     PHGPVQLSYY D
//
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