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 09-APR-2025, entry version 58.
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; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Gammaherpesvirinae; Lymphocryptovirus;
OC Lymphocryptovirus humangamma4; Epstein-Barr virus (strain GD1).
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. Also inhibits
CC host IFN-alpha-stimulated STAT2 nuclear translocation and interferon-
CC stimulated response element transcriptional activity by interacting
CC with and inhibiting host TYK2. Induces SUMO expression during viral
CC latency thereby dysregulating the host sumoylation processes.
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. Interacts with host TYK2.
CC {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}.
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DR EMBL; DQ279927; ABB89294.1; -; Genomic_DNA.
DR RefSeq; YP_001129515.1; NC_009334.1.
DR SMR; Q1HVB3; -.
DR KEGG; vg:5176215; -.
DR Proteomes; UP000007639; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0085033; P:symbiont-mediated activation of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR GO; GO:0039574; P:symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity; IEA:UniProtKB-KW.
DR GO; GO:0039527; P:symbiont-mediated suppression of host TRAF-mediated signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:symbiont-mediated suppression of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0019087; P:symbiont-mediated transformation of host cell; 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; Interferon antiviral system evasion;
KW Membrane; Oncogene; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation; 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..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT COMPBIAS 210..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..292
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..351
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
//
