LMP1_EBVR
ID LMP1_EBVR Reviewed; 386 AA.
AC P13198;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 23-FEB-2022, entry version 74.
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 Raji) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10378;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2835854; DOI=10.1016/0042-6822(88)90546-6;
RA Hatfull G., Bankier A.T., Barrell B.G., Farrell P.J.;
RT "Sequence analysis of Raji Epstein-Barr virus DNA.";
RL Virology 164:334-340(1988).
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. Inhibits also
CC host IFN-alpha-stimulated STAT2 nuclear translocation and interferon-
CC stimulated response element transcriptional activity by interacting
CC with and inhibiting host TYK2. {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; M20868; AAA66532.1; -; Genomic_DNA.
DR PIR; C28918; LABERJ.
DR PDB; 1ZMS; X-ray; 2.80 A; B=203-210.
DR PDBsum; 1ZMS; -.
DR SMR; P13198; -.
DR EvolutionaryTrace; P13198; -.
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:induction by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR GO; GO:0039574; P:suppression by virus of host JAK-STAT cascade via inhibition of host TYK2 activity; IEA:UniProtKB-KW.
DR GO; GO:0039547; P:suppression by virus of host TRAF 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 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; Membrane; Oncogene; Phosphoprotein;
KW Transmembrane; Transmembrane helix; Ubl conjugation; Viral immunoevasion.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..386
FT /note="Latent membrane protein 1"
FT /id="PRO_0000116181"
FT TOPO_DOM 2..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..51
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..106
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..163
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 194..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..232
FT /note="CTAR1"
FT /evidence="ECO:0000250"
FT REGION 342..386
FT /note="CTAR2"
FT /evidence="ECO:0000250"
FT MOTIF 204..208
FT /note="Interaction with host TRAF proteins"
FT /evidence="ECO:0000250"
FT COMPBIAS 205..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 386 AA; 42062 MW; 119A03B574455CF4 CRC64;
MDLDLERGPP GPRRPPRGPP LSSSIGLALL LLLLALLFWL YIIMSNWTGG ALLVLYAFAL
MLVIIILIIF IFRRDLLCPL GALCLLLLMI TLLLIALWNL HGQALYLGIV LFIFGCLLVL
GLWIYLLEIL WRLGATIWQL LAFFLAFFLD IILLIIALYL QQNWWTLLVD LLWLLLFLAI
LIWMYYHGQR HSDEHHHDDS LPHPQQATDD SSNQSDSNSN EGRHLLLVSG AGDGPPLCSQ
NLGAPGGGPN NGPQDPDNTD DNGPQDPDNT DDNGPHDPLP QDPDNTDDNG PQDPDNTDDN
GPHDPLPHNP SDSAGNDGGP PQLTEEVENK GGDQGPPLMT DGGGGHSHDS GHDGIDPHLP
TLLLGTSGSG GDDDDPHGPV QLSYYD
