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Database: UniProt
Entry: LMP1_EBVG
LinkDB: LMP1_EBVG
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   11-DEC-2019, entry version 28.
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 herpesvirus 4).
OC   Viruses; Herpesvirales; Herpesviridae; Gammaherpesvirinae;
OC   Lymphocryptovirus.
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.
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; AY961628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Proteomes; UP000007641; 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   Transmembrane; Transmembrane helix; 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..232
FT                   /note="CTAR1"
FT   REGION          332..366
FT                   /note="CTAR2"
FT   MOTIF           204..208
FT                   /note="Interaction with host TRAF proteins"
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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