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E3 ubiquitin-protein ligase LAP (EC (Leukemia associated protein) (LAP) (RING-type E3 ubiquitin transferase LAP)

 LAP_LSDV                Reviewed;         162 AA.
10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
05-DEC-2018, entry version 80.
RecName: Full=E3 ubiquitin-protein ligase LAP;
AltName: Full=Leukemia associated protein;
AltName: Full=RING-type E3 ubiquitin transferase LAP {ECO:0000305};
Lumpy skin disease virus (LSDV).
Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
NCBI_TaxID=9913; Bos taurus (Bovine).
Stipinovich C., Vreede F.T., Kara P.D., Wallace D.B., Nel L.H.,
Viljoen G.J.;
"Molecular characterization of important regions of the Lumpy skin
disease virus genome.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
PubMed=12827464; DOI=10.1007/s00705-003-0102-0;
Kara P.D., Afonso C.L., Wallace D.B., Kutish G.F., Abolnik C., Lu Z.,
Vreede F.T., Taljaard L.C.F., Zsak A., Viljoen G.J., Rock D.L.;
"Comparative sequence analysis of the South African vaccine strain and
two virulent field isolates of Lumpy skin disease virus.";
Arch. Virol. 148:1335-1356(2003).
-!- FUNCTION: E3 ubiquitin-protein ligase which promotes
ubiquitination and subsequent degradation of host MHC-I and CD4
molecules, presumably to prevent lysis of infected cells by
cytotoxic T-lymphocytes and NK cell. Binds target molecules
through transmembrane interaction. The result of this
ubiquitination is the enhancement of the endocytosis of the target
chain and the delivery to the lysosome, where it is
proteolytically destroyed (By similarity). {ECO:0000250}.
Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-
cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.; EC=;
-!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}. Host Golgi apparatus, host trans-
Golgi network membrane. Host early endosome membrane
-!- DOMAIN: The RING-CH-type zinc finger domain is required for E3
ligase activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
-!- SIMILARITY: Belongs to the poxviridae LAP protein family.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; AF336128; AAK43550.1; -; Genomic_DNA.
EMBL; AF409138; AAN02734.1; -; Genomic_DNA.
ProteinModelPortal; Q91T40; -.
GO; GO:0044174; C:host cell endosome; IEA:UniProtKB-KW.
GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
GO; GO:0039504; P:suppression by virus of host adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0046776; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
Gene3D;; -; 1.
InterPro; IPR033275; MARCH-like.
InterPro; IPR011016; Znf_RING-CH.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR23012; PTHR23012; 1.
Pfam; PF12906; RINGv; 1.
SMART; SM00744; RINGv; 1.
3: Inferred from homology;
Host endosome; Host Golgi apparatus; Host membrane;
Host-virus interaction;
Inhibition of host adaptive immune response by virus;
Inhibition of host MHC class I molecule presentation by virus;
Membrane; Metal-binding;
Modulation of host ubiquitin pathway by viral E3 ligase;
Modulation of host ubiquitin pathway by virus; Transferase;
Transmembrane; Transmembrane helix; Ubl conjugation pathway;
Viral immunoevasion; Zinc; Zinc-finger.
CHAIN 1 162 E3 ubiquitin-protein ligase LAP.
TOPO_DOM 1 78 Cytoplasmic. {ECO:0000255}.
TRANSMEM 79 99 Helical. {ECO:0000255}.
TOPO_DOM 100 121 Lumenal. {ECO:0000255}.
TRANSMEM 122 142 Helical. {ECO:0000255}.
TOPO_DOM 143 162 Cytoplasmic. {ECO:0000255}.
ZN_FING 3 61 RING-CH-type. {ECO:0000255|PROSITE-
COMPBIAS 89 94 Poly-Leu.
SEQUENCE 162 AA; 18782 MW; 5F914A4080F729EE CRC64;

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