Version 5.4
Mus musculus Protein: Agmat
Summary
InnateDB Protein IDBP-202366.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Agmat
Protein Name agmatine ureohydrolase (agmatinase)
Synonyms 5033405N08Rik;
Species Mus musculus
Ensembl Protein ENSMUSP00000040853
InnateDB Gene IDBG-202364 (Agmat)
Protein Structure
UniProt Annotation
Function
Subcellular Localization Mitochondrion {ECO:0000250}.
Disease Associations
Tissue Specificity Detected only in liver. {ECO:0000269PubMed:11914032}.
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 9 interaction(s) predicted by orthology.
Predicted by orthology
Total 9 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0008783 agmatinase activity
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0046872 metal ion binding
Biological Process
GO:0008150 biological_process
GO:0008295 spermidine biosynthetic process
GO:0033388 putrescine biosynthetic process from arginine
Cellular Component
GO:0005575 cellular_component
GO:0005739 mitochondrion
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID MGI:1923236
InterPro IPR005925 Agmatinase-related
IPR006035 Ureohydrolase
PFAM PF00491
PRINTS PR00116
PIRSF PIRSF036979
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt A2AS89
PhosphoSite PhosphoSite-A2AS89
TrEMBL Q8R0Z1
UniProt Splice Variant
Entrez Gene 75986
UniGene Mm.30032
RefSeq NP_001074877
MGI ID
MGI Symbol Agmat
OMIM
CCDS CCDS38941
HPRD
IMGT
EMBL AL928577 BC025916 BC115693
GenPept AAH25916 AAI15694 CAM23129

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