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InterPro: IPR002344 Lupus La protein

Protein matchesHelp
UniProtKB
Matches:
292 proteins
AccessionHelp IPR002344 Lupus_La
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR000504 RNA recognition motif, RNP-1
IPR006630 RNA-binding protein Lupus La
GO Term annotationHelp
Process GO:0006396 RNA processing
Function GO:0003723 RNA binding
Component GO:0005634 nucleus
GO:0030529 ribonucleoprotein complex
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The La protein is a 47 kDa polypeptide that often acts as an autoantigen in systemic lupus erythematosus and Sjogren's syndrome patients [1]. It occurs in both the nucleus and the cytoplasm, where it takes on different roles [2]. In the nucleus, La facilitates the production of tRNAs, acting as a RNA polymerase III (RNAP III) transcription factor by binding to the U-rich 3'UTR of nascent transcripts, assisting in their folding and maturation [3]. In the cytoplasm, La facilitates the translation of specific mRNAs, acting as a translation factor. As a RNA binding protein (RBP), La associates with subsets of mRNAs that contain a 5'-terminal oligopyrimidine (5'TOP) motif known to control protein synthesis. The binding of La to specific classes of RNA molecules regulates their downstream processing, protects them from endonuclease digestion, and organises their export from the nucleus [4, 5, 6, 7].

Structural linksHelp
SCOP: a.4.5.46 , d.58.7.1
Database linksHelp
Blocks: IPB002344

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR002344 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P05455 Lupus La protein

P10881 Lupus La protein homolog

P32067 Lupus La protein homolog

P33399 La protein homolog

P40796 La protein homolog

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR011991 Winged helix repressor DNA-binding
IPR012677 Nucleotide-binding, alpha-beta plait
IPR014886 RNA binding motif
IPR002344 Lupus La protein
IPR000504 RNA recognition motif, RNP-1
IPR006630 RNA-binding protein Lupus La
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Izumi RE, Das S, Barat B, Raychaudhuri S, Dasgupta A.
A peptide from autoantigen La blocks poliovirus and hepatitis C virus cap-independent translation and reveals a single tyrosine critical for La RNA binding and translation stimulation.
J. Virol. 78 3763-76 2004 [PubMed: 15016896]
http://dx.doi.org/10.1128/JVI.78.7.3763-3776.2004
2. Intine RV, Tenenbaum SA, Sakulich AL, Keene JD, Maraia RJ.
Differential phosphorylation and subcellular localization of La RNPs associated with precursor tRNAs and translation-related mRNAs.
Mol. Cell 12 1301-7 2003 [PubMed: 14636586]
http://dx.doi.org/10.1016/S1097-2765(03)00429-5
3. Alfano C, Sanfelice D, Babon J, Kelly G, Jacks A, Curry S, Conte MR.
Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein.
Nat. Struct. Mol. Biol. 11 323-9 2004 [PubMed: 15004549]
http://dx.doi.org/10.1038/nsmb747
4. Keene JD.
Posttranscriptional generation of macromolecular complexes.
Mol. Cell 12 1347-9 2003 [PubMed: 14690589]
http://dx.doi.org/10.1016/S1097-2765(03)00496-9
5. Keene JD, Tenenbaum SA.
Eukaryotic mRNPs may represent posttranscriptional operons.
Mol. Cell 9 1161-7 2002 [PubMed: 12086614]
http://dx.doi.org/10.1016/S1097-2765(02)00559-2
6. Keene JD.
Organizing mRNA export.
Nat. Genet. 33 111-2 2003 [PubMed: 12560814]
http://dx.doi.org/10.1038/ng0203-111
7. Keene JD.
Ribonucleoprotein infrastructure regulating the flow of genetic information between the genome and the proteome.
Proc. Natl. Acad. Sci. U.S.A. 98 7018-24 2001 [PubMed: 11416181]
http://dx.doi.org/10.1073/pnas.111145598

Additional ReadingHelp
Pruijn GJ, Slobbe RL, Van Venrooij WJ.
Structure and function of La and Ro RNPs.
Mol. Biol. Rep. 14 1990 43-8 [PubMed: 2194109]
http://dx.doi.org/10.1007/BF00360410
Jacks A, Babon J, Kelly G, Manolaridis I, Cary PD, Curry S, Conte MR.
Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element.
Structure 11 2003 833-43 [PubMed: 12842046]
http://dx.doi.org/10.1016/S0969-2126(03)00121-7
Kotik-Kogan O, Valentine ER, Sanfelice D, Conte MR, Curry S.
Structural analysis reveals conformational plasticity in the recognition of RNA 3' ends by the human La protein.
Structure 16 2008 852-62 [PubMed: 18547518]
http://dx.doi.org/10.1016/j.str.2008.02.021
Dong G, Chakshusmathi G, Wolin SL, Reinisch KM.
Structure of the La motif: a winged helix domain mediates RNA binding via a conserved aromatic patch.
EMBO J. 23 2004 1000-7 [PubMed: 14976553]
http://dx.doi.org/10.1038/sj.emboj.7600115
Teplova M, Yuan YR, Phan AT, Malinina L, Ilin S, Teplov A, Patel DJ.
Structural basis for recognition and sequestration of UUU(OH) 3' temini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen.
Mol. Cell 21 2006 75-85 [PubMed: 16387655]
http://dx.doi.org/10.1016/j.molcel.2005.10.027
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InterPro 23.1