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InterPro: IPR014766 Carboxypeptidase, regulatory domain

Protein matchesHelp
UniProtKB
Matches:
1165 proteins
AccessionHelp IPR014766 CarboxyPept_regulatory_dom
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR008969 Carboxypeptidase-like, regulatory domain
Found in IPR012103 Peptidase S8A, bacillopeptidase F
IPR014501 Uncharacterised conserved protein UCP019317
IPR015567 Peptidase M14B, caboxypeptidase D unit2
GO Term annotationHelp
Function GO:0004180 carboxypeptidase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This domain 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 beta-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

Structural linksHelp
SCOP: b.3.2.1
CATH: 2.60.40.1120

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR014766 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O89001 Carboxypeptidase D

P03764 Side tail fiber protein

P14384 Carboxypeptidase M

P16397 Bacillopeptidase F

P42787 Carboxypeptidase D

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR012103 Peptidase S8A, bacillopeptidase F
IPR015567 Peptidase M14B, caboxypeptidase D unit2
IPR005068 Phage tail fiber repeat 2
IPR008757 Peptidase M6, immune inhibitor A
IPR000209 Peptidase S8/S53, subtilisin/kexin/sedolisin
IPR010259 Proteinase inhibitor I9, subtilisin propeptide
IPR000834 Peptidase M14, carboxypeptidase A
IPR015500 Peptidase S8, subtilisin-related
IPR014766 Carboxypeptidase, regulatory domain
IPR011083 Phage tail collar
IPR008969 Carboxypeptidase-like, regulatory domain
IPR013609 Prophage tail fibre N-terminal
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Haucke V, Wenk MR, Chapman ER, Farsad K, De Camilli P.
Dual interaction of synaptotagmin with mu2- and alpha-adaptin facilitates clathrin-coated pit nucleation.
EMBO J. 19 6011-9 2000 [PubMed: 11080148]
http://dx.doi.org/10.1093/emboj/19.22.6011

Additional ReadingHelp
Reverter D, Maskos K, Tan F, Skidgel RA, Bode W.
Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.
J. Mol. Biol. 338 2004 257-69 [PubMed: 15066430]
http://dx.doi.org/10.1016/j.jmb.2004.02.058
Aloy P, Companys V, Vendrell J, Aviles FX, Fricker LD, Coll M, Gomis-Ruth FX.
The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases.
J. Biol. Chem. 276 2001 16177-84 [PubMed: 11278909]
http://dx.doi.org/10.1074/jbc.M011457200
Gomis-Ruth FX, Companys V, Qian Y, Fricker LD, Vendrell J, Aviles FX, Coll M.
Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily.
EMBO J. 18 1999 5817-26 [PubMed: 10545093]
http://dx.doi.org/10.1093/emboj/18.21.5817
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InterPro 24.0