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Database: UniProt
Entry: LMP1_EBVG
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Original site: LMP1_EBVG 
ID   LMP1_EBVG               Reviewed;         366 AA.
AC   P0C741;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   09-APR-2025, entry version 41.
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 GD1) (HHV-4) (Human gammaherpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Gammaherpesvirinae; Lymphocryptovirus;
OC   Lymphocryptovirus humangamma4.
OX   NCBI_TaxID=10376;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16306603; DOI=10.1128/jvi.79.24.15323-15330.2005;
RA   Zeng M.-S., Li D.-J., Liu Q.-L., Song L.-B., Li M.-Z., Zhang R.-H.,
RA   Yu X.-J., Wang H.-M., Ernberg I., Zeng Y.-X.;
RT   "Genomic sequence analysis of Epstein-Barr virus strain GD1 from a
RT   nasopharyngeal carcinoma patient.";
RL   J. Virol. 79:15323-15330(2005).
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. {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; AY961628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PDB; 8XH6; EM; 3.52 A; A/B=24-185.
DR   PDB; 8XH7; EM; 3.52 A; A/B/C/D/E/F=24-185.
DR   PDBsum; 8XH6; -.
DR   PDBsum; 8XH7; -.
DR   SMR; P0C741; -.
DR   Proteomes; UP000007641; 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   1: Evidence at protein level;
KW   3D-structure; Activation of host NF-kappa-B by virus; Host cell membrane;
KW   Host membrane; Host-virus interaction;
KW   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; Transmembrane; Transmembrane helix;
KW   Ubl conjugation; Viral immunoevasion.
FT   CHAIN           1..366
FT                   /note="Latent membrane protein 1"
FT                   /id="PRO_0000375962"
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..366
FT                   /note="Cytoplasmic"
FT   REGION          194..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..232
FT                   /note="CTAR1"
FT   REGION          332..366
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..267
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..346
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   366 AA;  39763 MW;  9B4809D51CCBD887 CRC64;
     MERDLERGPP GPPRPPLGPP LSSSIGLALL LLLLALLFWL YIVLSNWTGG ALLVLYSFAL
     MLIIIILIIF IFRRDLLCPL GGLGLLLLMV TLLLIALWNL HGQALYLGIV LFIFGCLLVL
     GLWIYFLEIL WRLGATIWQL LAFILAFFLA IILLIIALYL QQNWWTLLVD LLWLLLFMAI
     LIWMYFHGPR HTDEHHHDDS LPHPQQATDD SSHESDSNSN EGRHHLLVSG AGDGPPLCSQ
     NLGAPGGGPD NGPQDPDNTD DNGPQDPDNT DDNGNTDDNG PQDPDNTDDN GPHDPLPHNP
     SDSAGNDGGP PNLTEEVENK GGDRGPPSMT DGGGGDPHLP TLLLGTSGSG GDDDDPHGPV
     QLSYYD
//
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