Latent membrane protein 1 - Epstein-Barr virus (strain B95-8) (HHV-4)

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P03230 (LMP1_EBVB9) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 70. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Latent membrane protein 1
Short name=LMP-1

Alternative name(s):
Protein p63

Cleaved into the following chain:

Protein p25

Gene names

Name:	LMP1
ORF Names:	BNLF1

Organism

Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)

Taxonomic identifier

10377 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Lymphocryptovirus

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a CD40 functional homolog to prevent apoptosis of infected B-lymphocytes and drive their proliferation. Functions as a constitutively active tumor necrosis factor receptor that induces the activation of several signaling pathways, including those of the nuclear factor-kappa-B family. LMP1 signaling leads to up-regulation of antiapoptotic proteins and provide growth signals in latently infected cells. It is a short-lived protein probably degraded by the proteasome.
Subunit structure	Interacts (via PXQXT motif) with host tumor necrosis factor receptor-associated factor (TRAF) proteins TRAF1, TRAF2, TRAF3 and TRAF5.
Subcellular location	Host cell membrane; Multi-pass membrane protein Ref.8.
Domain	Two regions, C-terminal-activating region 1 (CTAR1) and CTAR2, have been identified within the cytoplasmic carboxy terminal domain that activates NF-kappa-B. Ref.7
Post-translational modification	Ubiquitinated on the N-terminus. Ref.8
Sequence similarities	Belongs to the herpesviridae LMP-1 family.

Ontologies

Keywords
Biological process	Activation of host NF-kappa-B by virus Host-virus interaction Inhibition of host IFN-mediated response initiation by virus Inhibition of host TRAFs by virus Inhibition of host TYK2 by virus Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Viral immunoevasion
Cellular component	Host cell membrane Host membrane Membrane
Disease	Oncogene
Domain	Transmembrane Transmembrane helix
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	evasion by virus of host immune response Inferred from electronic annotation. Source: UniProtKB-KW transformation of host cell by virus Inferred from electronic annotation. Source: InterPro
Cellular component	host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 386

385

Latent membrane protein 1

PRO_0000038310

Chain

242 – 386

145

Protein p25

PRO_0000038311

Regions

Topological domain

2 – 23

Cytoplasmic

Transmembrane

24 – 44

Helical; Potential

Topological domain

45 – 51

Extracellular

Transmembrane

52 – 72

Helical; Potential

Topological domain

73 – 75

Cytoplasmic

Transmembrane

76 – 96

Helical; Potential

Topological domain

97 – 106

Extracellular

Transmembrane

107 – 127

Helical; Potential

Topological domain

128 – 139

Cytoplasmic

Transmembrane

140 – 160

Helical; Potential

Topological domain

161 – 163

Extracellular

Transmembrane

164 – 184

Helical; Potential

Topological domain

185 – 386

202

Cytoplasmic

Region

194 – 232

CTAR1

Region

351 – 386

CTAR2

Motif

204 – 208

Interaction with host TRAF proteins

Amino acid modifications

Modified residue

N-acetylglutamate; by host

Experimental info

Mutagenesis

330

K → R: No effect on ubiquitination and proteasomal degradation. Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

P03230 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 1E19446E857DB8A3
Show »

FASTA

386

41,982

        10         20         30         40         50         60 
MEHDLERGPP GPRRPPRGPP LSSSLGLALL LLLLALLFWL YIVMSDWTGG ALLVLYSFAL 

        70         80         90        100        110        120 
MLIIIILIIF IFRRDLLCPL GALCILLLMI TLLLIALWNL HGQALFLGIV LFIFGCLLVL 

       130        140        150        160        170        180 
GIWIYLLEML WRLGATIWQL LAFFLAFFLD LILLIIALYL QQNWWTLLVD LLWLLLFLAI 

       190        200        210        220        230        240 
LIWMYYHGQR HSDEHHHDDS LPHPQQATDD SGHESDSNSN EGRHHLLVSG AGDGPPLCSQ 

       250        260        270        280        290        300 
NLGAPGGGPD NGPQDPDNTD DNGPQDPDNT DDNGPHDPLP QDPDNTDDNG PQDPDNTDDN 

       310        320        330        340        350        360 
GPHDPLPHSP SDSAGNDGGP PQLTEEVENK GGDQGPPLMT DGGGGHSHDS GHGGGDPHLP 

       370        380 
TLLLGSSGSG GDDDDPHGPV QLSYYD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of an mRNA transcribed in latent growth-transforming virus infection indicates that it may encode a membrane protein." Fennewald S., van Santen V., Kieff E. J. Virol. 51:411-419(1984) [PubMed: 6086953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Two related but differentially expressed potential membrane proteins encoded by the EcoRI Dhet region of Epstein-Barr virus B95-8." Hudson G.S., Farrell P.J., Barrell B.G. J. Virol. 53:528-535(1985) [PubMed: 2982035] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"DNA sequence and expression of the B95-8 Epstein-Barr virus genome." Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J., Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C., Tuffnell P.S., Barrell B.G. Nature 310:207-211(1984) [PubMed: 6087149] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Posttranslational processing of an Epstein-Barr virus-encoded membrane protein expressed in cells transformed by Epstein-Barr virus." Baichwal V.R., Sudgen B. J. Virol. 61:866-875(1987) [PubMed: 3027413] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Transformation of Balb 3T3 cells by the BNLF-1 gene of Epstein-Barr virus." Baichwal V.R., Sudgen B. Oncogene 2:461-467(1988) [PubMed: 2836780] [Abstract] Cited for: TRANSFORMING PROPERTIES.
[6]	"Processing of the Epstein-Barr virus-encoded latent membrane protein p63/LMP." Moorthy R., Thorley-Lawson D.A. J. Virol. 64:829-837(1990) [PubMed: 2153246] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[7]	"The Epstein-Barr virus latent membrane protein-1 (LMP1) mediates activation of NF-kappa B and cell surface phenotype via two effector regions in its carboxy-terminal cytoplasmic domain." Huen D.S., Henderson S.A., Croom-Carter D., Rowe M. Oncogene 10:549-560(1995) [PubMed: 7845680] [Abstract] Cited for: DOMAIN CTAR1 AND CTAR2.
[8]	"Degradation of the epstein-barr virus latent membrane protein 1 (LMP1) by the ubiquitin-proteasome pathway. Targeting via ubiquitination of the N-terminal residue." Aviel S., Winberg G., Massucci M., Ciechanover A. J. Biol. Chem. 275:23491-23499(2000) [PubMed: 10807912] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-330, UBIQUITINATION.
[9]	"Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation." Richardson J.S., Richardson D.C. Proc. Natl. Acad. Sci. U.S.A. 99:2754-2759(2002) [PubMed: 11880627] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 204-210.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X01995 Genomic DNA. Translation: CAA26023.1.
K02165 Genomic DNA. Translation: AAA45888.1.
V01555 Genomic DNA. No translation available.
AJ507799 Genomic DNA. Translation: CAD53472.1.

PIR

QQBE50. D43045.

RefSeq

YP_401722.1. NC_007605.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CZY	X-ray	2.00	D/E	204-210	[»]

ProteinModelPortal

P03230.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29603N.
DIP-43767N.

MINT

MINT-1509916.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3783750.

Phylogenomic databases

ProtClustDB

CLSP2512943.

Family and domain databases

InterPro

IPR007961. Herpes_LMP1.
[Graphical view]

Pfam

PF05297. Herpes_LMP1. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

LMP1_EBVB9

Accession

Primary (citable) accession number: P03230
Secondary accession number(s): Q777A4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 16, 2011
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following chain:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents