Carboxypeptidase-like, regulatory domain superfamily
IPR008969
Definition
This domain superfamily identifies a number of eukaryotic carboxypeptidases, these include carboxypeptidase D, E (H), N, X, X2 and Z. These are metallopeptidases belong to MEROPS peptidase family M14 (clan MC), subfamily M14B. Carboxypeptidase D (CPD) is a new B-type metallocarboxypeptidase that is membrane bound and has an acidic pH optimum. A hydrophobic region at the N terminus represents the signal peptide, and one near the C terminus that probably represents the transmembrane anchor. A regulatory domain within the protein has been identified as a β-sandwich, comprising 7 strands in 2 sheets in a greek-key topology. Some family members have an additional 1-2 strands to the common fold PMID:11080148. The bacterial and archaeal sequences having this signature are variously annotated, examples are: Hypothetical/conserved/membrane/cell surface protein N-acetylglucosamine deacetylase Side tail fibre protein homologue from lambdoid prophage Rac Hypothetical tonB-linked outer membrane receptor OmpA-related protein Putative outer membrane protein, probably involved in nutrient binding TonB-dependent receptor This entry also includes the teneurin family members, which may function as cellular signal transducers.
16 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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