LAP_SWPVK
ID LAP_SWPVK Reviewed; 155 AA.
AC P32225;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=LAP; ORFNames=C7L;
OS Swinepox virus (strain Kasza) (SWPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Suipoxvirus.
OX NCBI_TaxID=10277;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8249275; DOI=10.1006/viro.1993.1625;
RA Massung R.F., Jayarama V., Moyer R.W.;
RT "DNA sequence analysis of conserved and unique regions of swinepox virus:
RT identification of genetic elements supporting phenotypic observations
RT including a novel G protein-coupled receptor homologue.";
RL Virology 197:511-528(1993).
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. {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}.
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DR EMBL; L22013; AAC37864.1; -; Unassigned_RNA.
DR SMR; P32225; -.
DR PRIDE; P32225; -.
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..155
FT /note="E3 ubiquitin-protein ligase LAP"
FT /id="PRO_0000099751"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..115
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 1..55
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 5
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
SQ SEQUENCE 155 AA; 18461 MW; 4D478213CCA8FB44 CRC64;
MDPVCWICKD DYSIEKNYCN CKNEYKVVHD ECMKKWIQYS RERSCKLCNK EYNIISVRKP
FSQWVFSIKD CKKSAILYAT LFLCTFIISL VLTRINITKI IDTSKNDVSF KLVTMIFYLL
PFVITCISFI TLIVYLYKYC KISAKNNTYD TIYEL
