Version 5.4
Mus musculus Protein: Pepd
Summary
InnateDB Protein IDBP-173588.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Pepd
Protein Name peptidase D
Synonyms Pep-4; Pep4;
Species Mus musculus
Ensembl Protein ENSMUSP00000075683
InnateDB Gene IDBG-173586 (Pepd)
Protein Structure
UniProt Annotation
Function Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because of the high level of iminoacids in collagen.
Subcellular Localization
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 7 interaction(s) predicted by orthology.
Predicted by orthology
Total 7 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004177 aminopeptidase activity
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0016805 dipeptidase activity
GO:0030145 manganese ion binding
Biological Process
GO:0006508 proteolysis
GO:0030574 collagen catabolic process
Cellular Component
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID MGI:97542
InterPro IPR000994 Peptidase M24, structural domain
IPR007865 Aminopeptidase P, N-terminal
IPR028980 Creatinase/Aminopeptidase P, N-terminal
PFAM PF00557
PF05195
PRINTS
PIRSF
SMART SM01011
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q11136
PhosphoSite PhosphoSite-Q11136
TrEMBL A2RS23
UniProt Splice Variant
Entrez Gene 18624
UniGene Mm.69751
RefSeq NP_032846
MGI ID
MGI Symbol Pepd
OMIM
CCDS CCDS21143
HPRD
IMGT
EMBL AK010581 AK145843 AK168384 BC086644 BC131945 BC131973 CH466618 D82983 U51014
GenPept AAA92975 AAH86644 AAI31946 AAI31974 BAB11685 BAB27043 BAE26691 BAE40312 EDL03029

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