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InterPro: IPR014766 Carboxypeptidase, regulatory domain
Protein matches
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UniProtKB Matches: 1165 proteins |
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Accession
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IPR014766 CarboxyPept_regulatory_dom |
Type
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Domain |
Signatures
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InterPro Relationships
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Parent
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IPR008969 Carboxypeptidase-like, regulatory domain
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Found in
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IPR012103 Peptidase S8A, bacillopeptidase F
IPR014501 Uncharacterised conserved protein UCP019317
IPR015567 Peptidase M14B, caboxypeptidase D unit2
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GO Term annotation
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Function
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GO:0004180 carboxypeptidase activity
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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
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Structural links
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Additional Reading
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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
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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
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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
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