Summary for peptidase M14.016: metallocarboxypeptidase D peptidase unit 2

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Literature Human EST Mouse EST Substrates Inhibitors

 

Names
MEROPS Namemetallocarboxypeptidase D peptidase unit 2
Other namescarboxypeptidase D peptidase unit 2, metallocarboxypeptidase D domain B
Domain architecture
MEROPS Classification
Parent M14.016 is one peptidase unit of the compound peptidase XM14-001. Other units of XM14-001 are M14.011, M14.950
Classification Clan MC >> Subclan (none) >> Family M14 >> Subfamily B >> M14.016
Holotypemetallocarboxypeptidase D peptidase unit 2 (Anas platyrhynchos) (peptidase unit: 502-906), MERNUM MER0004959
History Identifier created: MEROPS 5.2 (31 August 2000)
Activity
Catalytic typeMetallo
PeplistIncluded in the Peplist with identifier PL00216
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.17 (Metallocarboxypeptidases) >> Peptidase 3.4.17.22
EnzymologyBRENDA database
Activity statushuman: active (Fricker, 2004)
mouse: putative
SpecificitySpecific for C-terminal basic residues (Lys, Arg) (Song & Fricker, 1995)
pH optimum5-6 (Song & Fricker, 1995)
Substrate commentsDansyl-Phe-Ala-Arg (Song & Fricker, 1995)
Inhibitor commentsChelating agents such as 1,10-phenanthroline. Also guanidinoethylmercaptosuccinic acid (Song & Fricker, 1995).
LocationIn the secretory pathway, primarily within the transGolgi network. Also cycles to cell surface (active domain facing the extracellular space) and back to the Golgi (Varlamov & Fricker, 1998).
PhysiologyThought to function in the processing of proteins and peptides that transit the secretory pathway (Varlamov et al., 1999).
Biological aspectsProperties are similar to domain 1 of carboxypeptidase D, except that the pH optimum is more acidic. There may also be differences in the relative activity towards Lys and Arg residues for the two domains (Novikova et al., 1999).
KnockoutMouse CPD knockouts have not been successfully generated. Drosophila with point mutations within domain 2, which cause this domain to be inactive, are viable but have altered wing shape (Sidyelyeva et al., 2010).
Distinguishing featuresCarboxypeptidase D is the only metallocarboxypeptidase with multiple catalytic domains, containing 3 CP-like domains (1 and 2 are active, domain 3 is not) (Kuroki et al., 1995).
Contributing authorsLloyd D. Fricker, Departments of Molecular Pharmacology and Neuroscience, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Other databases TREEFAMhttp://www.treefam.org/family/TF315592
Human genetics
Gene symbol Locus Megabases Ensembl Entrez gene Gene Cards OMIM
CPD 17p11.1-q11.2 ENSG00000108582 1362 CPD 603102
Mouse genetics
Gene symbol Position Megabases Ensembl Entrez gene MGI
Cpd 11:B5 ENSMUSG00000020841 12874 MGI:107265