Version 5.4
Mus musculus Protein: Elac2
Summary
InnateDB Protein IDBP-185771.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Elac2
Protein Name elaC homolog 2 (E. coli)
Synonyms 1110017O07Rik; D11Wsu80e; Hpc2;
Species Mus musculus
Ensembl Protein ENSMUSP00000071788
InnateDB Gene IDBG-185767 (Elac2)
Protein Structure
UniProt Annotation
Function Zinc phosphodiesterase, which displays mitochondrial tRNA 3'-processing endonuclease activity. Involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA (By similarity). {ECO:0000250}.
Subcellular Localization Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=Mainly mitochondrial. {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 10 interaction(s) predicted by orthology.
Predicted by orthology
Total 10 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004519 endonuclease activity
GO:0016787 hydrolase activity
GO:0044822 poly(A) RNA binding
GO:0046872 metal ion binding
Biological Process
GO:0072684 mitochondrial tRNA 3'-trailer cleavage, endonucleolytic
Cellular Component
GO:0005634 nucleus
GO:0005739 mitochondrion
Protein Structure and Domains
PDB ID MGI:1890496
InterPro IPR001279 Beta-lactamase-like
PFAM PF00753
PRINTS
PIRSF
SMART SM00849
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q80Y81
PhosphoSite PhosphoSite-Q80Y81
TrEMBL Q3U0M8
UniProt Splice Variant
Entrez Gene 68626
UniGene Mm.157711
RefSeq NP_075968
MGI ID
MGI Symbol Elac2
OMIM
CCDS CCDS24841
HPRD
IMGT
EMBL AF308696 AF348157 AK003759 AK004136 AK156730 AL663045 BC048235
GenPept AAG24918 AAH48235 AAK29420 AAK29421 BAB22981 BAB23185 BAE33824 CAI24609

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca