Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q997C2 (LAP_MYXVL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase LAP
EC=6.3.2.-
Alternative name(s):
Leukemia associated protein
Short name=LAP
Gene names
Name:LAP
Ordered Locus Names:m153R
OrganismMyxoma virus (strain Lausanne) (MYXV) [Reference proteome]
Taxonomic identifier31530 [NCBI]
Taxonomic lineageViruses › dsDNA viruses, no RNA stage › Poxviridae › Chordopoxvirinae › Leporipoxvirus ›
Virus hostOryctolagus cuniculus (Rabbit) [TaxID: 9986]

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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. Ref.3 Ref.4

Subcellular location

Host membrane; Multi-pass membrane protein Potential. Host Golgi apparatus › host trans-Golgi network membrane. Host early endosome membrane Ref.4.

Domain

The RING-CH-type zinc finger domain is required for E3 ligase activity By similarity.

Sequence similarities

Belongs to the poxviridae LAP protein family.

Contains 1 RING-CH-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 206206E3 ubiquitin-protein ligase LAP
PRO_0000396001

Regions

Topological domain1 – 9393Cytoplasmic Potential
Transmembrane94 – 11421Helical; Potential
Topological domain115 – 12915Lumenal Potential
Transmembrane130 – 15021Helical; Potential
Topological domain151 – 20656Cytoplasmic Potential
Zinc finger15 – 7561RING-CH-type

Sequences

Sequence LengthMass (Da)Tools
Q997C2 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: AFC6FD51B1D19957

FASTA20623,258
        10         20         30         40         50         60 
MATVVNMDTV VNLDDVSLAD KCCWICKEAC DIVPNYCKCR GDNKIVHKEC LEEWINTDVV 

        70         80         90        100        110        120 
KNKSCAICES PYNLKRRYKK ITKWRCYKRD CHDSLLVNMS LCLIVGGMGG YLLISTEIVK 

       130        140        150        160        170        180 
LIASEEVSNI AKVFLVSASM GPFMVSALTM VRACIDCRTY FIATRERNTI HEVAEMEDVE 

       190        200 
EVEEVNDDDG DEYVDAVEEI VVESPA

« Hide

References

« Hide 'large scale' references
[1]"Myxoma virus leukemia-associated protein is responsible for major histocompatibility complex class I and Fas-CD95 down-regulation and defines scrapins, a new group of surface cellular receptor abductor proteins."
Guerin J.L., Gelfi J., Boullier S., Delverdier M., Bellanger F.A., Bertagnoli S., Drexler I., Sutter G., Messud-Petit F.
J. Virol. 76:2912-2923(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Toulouse 1.
[2]"The complete DNA sequence of myxoma virus."
Cameron C., Hota-Mitchell S., Chen L., Barrett J.W., Cao J.-X., Macaulay C., Willer D.O., Evans D.H., McFadden G.
Virology 264:298-318(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The PHD/LAP-domain protein M153R of myxomavirus is a ubiquitin ligase that induces the rapid internalization and lysosomal destruction of CD4."
Mansouri M., Bartee E., Gouveia K., Hovey Nerenberg B.T., Barrett J., Thomas L., Thomas G., McFadden G., Fruh K.
J. Virol. 77:1427-1440(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"The poxviral scrapin MV-LAP requires a myxoma viral infection context to efficiently downregulate MHC-I molecules."
Collin N., Guerin J.L., Drexler I., Blanie S., Gelfi J., Boullier S., Foucras G., Sutter G., Messud-Petit F.
Virology 343:171-178(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF170726 Genomic DNA. Translation: AAF15041.2.
AF229033 Genomic DNA. Translation: AAK00734.1.
RefSeqNP_051866.2. NC_001132.2.

3D structure databases

ProteinModelPortalQ997C2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID932099.

Phylogenomic databases

ProtClustDBPHA2825.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF12906. RINGv. 1 hit.
[Graphical view]
SMARTSM00744. RINGv. 1 hit.
[Graphical view]
PROSITEPS51292. ZF_RING_CH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLAP_MYXVL
AccessionPrimary (citable) accession number: Q997C2
Secondary accession number(s): Q9Q8F2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: June 1, 2001
Last modified: April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents