LAP_LSDV
ID LAP_LSDV Reviewed; 162 AA.
AC Q91T40;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=E3 ubiquitin-protein ligase LAP;
DE EC=2.3.2.27;
DE AltName: Full=Leukemia associated protein;
DE Short=LAP;
DE AltName: Full=RING-type E3 ubiquitin transferase LAP {ECO:0000305};
GN Name=LW010;
OS Lumpy skin disease virus (LSDV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Capripoxvirus.
OX NCBI_TaxID=59509;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Neethling;
RA Stipinovich C., Vreede F.T., Kara P.D., Wallace D.B., Nel L.H.,
RA Viljoen G.J.;
RT "Molecular characterization of important regions of the Lumpy skin disease
RT virus genome.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12827464; DOI=10.1007/s00705-003-0102-0;
RA Kara P.D., Afonso C.L., Wallace D.B., Kutish G.F., Abolnik C., Lu Z.,
RA Vreede F.T., Taljaard L.C.F., Zsak A., Viljoen G.J., Rock D.L.;
RT "Comparative sequence analysis of the South African vaccine strain and two
RT virulent field isolates of Lumpy skin disease virus.";
RL Arch. Virol. 148:1335-1356(2003).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which promotes ubiquitination and
CC subsequent degradation of host MHC-I and CD4 molecules, presumably to
CC prevent lysis of infected cells by cytotoxic T-lymphocytes and NK cell.
CC Binds target molecules through transmembrane interaction. The result of
CC this ubiquitination is the enhancement of the endocytosis of the target
CC chain and the delivery to the lysosome, where it is proteolytically
CC destroyed (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Host Golgi apparatus, host trans-Golgi network
CC membrane. Host early endosome membrane {ECO:0000250}.
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
CC -!- SIMILARITY: Belongs to the poxviridae LAP protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF336128; AAK43550.1; -; Genomic_DNA.
DR EMBL; AF409138; AAN02734.1; -; Genomic_DNA.
DR SMR; Q91T40; -.
DR PRIDE; Q91T40; -.
DR GO; GO:0044174; C:host cell endosome; IEA:UniProtKB-KW.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0046776; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 3: Inferred from homology;
KW Host endosome; Host Golgi apparatus; Host membrane; Host-virus interaction;
KW Inhibition of host adaptive immune response by virus;
KW Inhibition of host MHC class I molecule presentation by virus; Membrane;
KW Metal-binding; Modulation of host ubiquitin pathway by viral E3 ligase;
KW Modulation of host ubiquitin pathway by virus; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Viral immunoevasion; Zinc;
KW Zinc-finger.
FT CHAIN 1..162
FT /note="E3 ubiquitin-protein ligase LAP"
FT /id="PRO_0000396003"
FT TOPO_DOM 1..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..121
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 3..61
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
SQ SEQUENCE 162 AA; 18782 MW; 5F914A4080F729EE CRC64;
MEGSDNTNTH CWICKDEYNV STNFCNCKNE FKIVHKNCLE EWINFSHNTK CKICNGKYNI
KKNKKSCLRW KCSFMYCNVP AICVSLICLL LLPLTILLVK FNLKSMLENI ENRDLIALIS
AMAYSLPCVV GFITVVHILI ALYDYYLAAK SDNTTYQVYE YI
