9.B.387.2.1 Latent membrane protein 2, LMP2, of 497 aas and 12 TMSs. Isoform LMP2A maintains EBV latent infection of B-lymphocyte, by preventing lytic
reactivation of the virus in response to surface immunoglobulin (sIg)
cross-linking. It acts like a dominant negative inhibitor of the
sIg-associated protein tyrosine kinases, LYN and SYK. It also blocks
translocation of the B-cell antigen receptor (BCR) into lipid rafts,
preventing the subsequent signaling and accelerated internalization of
the BCR upon BCR cross-linking. It serves as a molecular scaffold to
recruit SYK, LYN and E3 protein-ubiquitin ligases, such as ITCH and
NEDD4L, leading to ubiquitination and potential degradation of both
tyrosine kinases. It possesses a constitutive signaling activity in
non-transformed cells, inducing bypass of normal B lymphocyte
developmental checkpoints allowing immunoglobulin-negative cells to
colonize peripheral lymphoid organs (Cen and Longnecker 2015).
|
Accession Number: | P13285 |
Protein Name: | Latent membrane protein 2 |
Length: | 497 |
Molecular Weight: | 53011.00 |
Species: | Epstein-Barr virus (strain B95-8) (HHV-4) [10377] |
Number of TMSs: | 12 |
Location1 / Topology2 / Orientation3: |
Host endomembrane system1 / Multi-pass membrane protein2 |
Substrate |
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1: MGSLEMVPMG AGPPSPGGDP DGYDGGNNSQ YPSASGSSGN TPTPPNDEER ESNEEPPPPY
61: EDPYWGNGDR HSDYQPLGTQ DQSLYLGLQH DGNDGLPPPP YSPRDDSSQH IYEEAGRGSM
121: NPVCLPVIVA PYLFWLAAIA ASCFTASVST VVTATGLALS LLLLAAVASS YAAAQRKLLT
181: PVTVLTAVVT FFAICLTWRI EDPPFNSLLF ALLAAAGGLQ GIYVLVMLVL LILAYRRRWR
241: RLTVCGGIMF LACVLVLIVD AVLQLSPLLG AVTVVSMTLL LLAFVLWLSS PGGLGTLGAA
301: LLTLAAALAL LASLILGTLN LTTMFLLMLL WTLVVLLICS SCSSCPLSKI LLARLFLYAL
361: ALLLLASALI AGGSILQTNF KSLSSTEFIP NLFCMLLLIV AGILFILAIL TEWGSGNRTY
421: GPVFMCLGGL LTMVAGAVWL TVMSNTLLSA WILTAGFLIF LIGFALFGVI RCCRYCCYYC
481: LTLESEERPP TPYRNTV