H
IPR008969

Carboxypeptidase-like, regulatory domain superfamily

InterPro entry
Short nameCarboxyPept-like_regulatory
Overlapping entries
 

Description

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
[1]
.

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.

References

1.Dual interaction of synaptotagmin with mu2- and alpha-adaptin facilitates clathrin-coated pit nucleation. Haucke V, Wenk MR, Chapman ER, Farsad K, De Camilli P. EMBO J. 19, 6011-9, (2000). View articlePMID: 11080148

Cross References

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.