Zinc carboxypeptidases, zinc-binding region 2
IPR057247
Definition
There are two conserved sites matching these three zinc-ligands - this entry and [interpro:IPR057246]. If a protein includes both, the probability of it being a eukaryotic zinc carboxypeptidase is very high. There are a number of different types of zinc-dependent carboxypeptidases (EC 3.4.17.-) [[cite:PMID:2753907], [cite:PMID:2584208]]. All these enzymes seem to be structurally and functionally related. Some enzymes that belong to this family are listed below. Carboxypeptidase A1 (EC 3.4.17.1), a pancreatic digestive enzyme that can remove all C-terminal amino acids with the exception of Arg, Lys and Pro. Carboxypeptidase A2 (EC 3.4.17.15), a pancreatic digestive enzyme with a specificity similar to that of carboxypeptidase A1, but with a preference for bulkier C-terminal residues. Carboxypeptidase B (EC 3.4.17.2), also a pancreatic digestive enzyme, but that preferentially removes C-terminal Arg and Lys. Carboxypeptidase N (EC 3.4.17.3) (also known as arginine carboxypeptidase), a plasma enzyme which protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation. Carboxypeptidase H (EC 3.4.17.10) (also known as enkephalin convertase or carboxypeptidase E), an enzyme located in secretory granules of pancreatic islets, adrenal gland, pituitary and brain. This enzyme removes residual C-terminal Arg or Lys remaining after initial endoprotease cleavage during prohormone processing. Carboxypeptidase M (EC 3.4.17.12), a membrane bound Arg and Lys specific enzyme. Mast cell carboxypeptidase (EC 3.4.17.1), an enzyme with a specificity to carboxypeptidase A, but found in the secretory granules of mast cells. Streptomyces griseus carboxypeptidase (Cpase SG) (EC 3.4.17.-) PMID:2118139, which combines the specificities of mammalian carboxypeptidases A and B. Thermoactinomyces vulgaris carboxypeptidase T (EC 3.4.17.18) (CPT) PMID:1521526, which also combines the specificities of carboxypeptidases A and B. All of these enzymes bind an atom of zinc. Three conserved residues are implicated in the binding of the zinc atom: two histidines and a glutamic acid.
13 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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