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M14 family carboxypeptidase N/E

M14 family zinc carboxypeptidase N/E relies on its substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell; it contains an extra C-terminal domain which may assist in folding of the carboxypeptidase domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes

Arch. IDVersionDate PublishedReview Level
1333915722021-08-26
curated
Arch. ID13339157
Version2
Date Published2021-08-26
Review Level
curated
PHA03247: large tegument protein UL36PHA03247FA58C: Coagulation factor 5/8 C-terminal domain, discoidin domainFA58CM14_CPX_like: Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroupM14_CPX_likePeptidase_M14NE-CP-C_like: Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domainPeptidase_M14NE-CP-C_like
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Sequences with this architecture
This architecture currently does not link to any protein sequence records.
Name, label and taxonomic scope
Taxonomic scopeNameLabel
All organismsM14 family carboxypeptidase N/EM14 family zinc carboxypeptidase N/E relies on its substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell; it contains an extra C-terminal domain which may assist in folding of the carboxypeptidase domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes
Name, label and taxonomic scope
Tax. ExpAll organisms
NameM14 family carboxypeptidase N/E
LabelM14 family zinc carboxypeptidase N/E relies on its substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell; it contains an extra C-terminal domain which may assist in folding of the carboxypeptidase domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes
Supporting evidence
Comments
  • also contains N-terminal TonB domain, and coagulation factor 5/8 C-terminal domain (discoidin domain) assumed to have horizontally transferred to eubacterial genomes
  • such as carboxypeptidase (CP)-like protein X (CPX) or adipocyte enhancer binding protein-1 (AEBP1) which are enzymatically non-active towards standard CP substrates because they lack one or more critical active site and substrate-binding residues needed for activity; they may function as binding proteins or display catalytic activity toward other substrates
Gene IDs
CDD
  • cd00057: FA58C
  • cd03869: M14_CPX_like
  • cd03865: M14_CPE
  • cd11308: Peptidase_M14NE-CP-C_like
  • pfam00246: Peptidase_M14 : Zinc carboxypeptidase
  • cd03864: M14_CPN : Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase N subgroup
Protein Accession
  • Q8N436: RecName: Full=Inactive carboxypeptidase-like protein X2; Flags: Precursor
  • AAI37493: Carboxypeptidase X (M14 family), member 2 [Homo sapiens]
Publications
  • PMID 31651348: Overexpression of carboxypeptidase X M14 family member 2 predicts an unfavorable prognosis and promotes proliferation and migration of osteosarcoma.
  • PMID 9809751: Identification of mouse CPX-2, a novel member of the metallocarboxypeptidase gene family: cDNA cloning, mRNA distribution, and protein expression and characterization.
Conserved domains in this architecture
AccessionShort nameTitle
cd00057FA58CCoagulation factor 5/8 C-terminal domain, discoidin domain
cd03869M14_CPX_likePeptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup
cd11308Peptidase_M14NE-CP-C_likePeptidase associated domain
cl33720PHA03247large tegument protein UL36
Functional sites in this architecture
TitleTypeSource domain
sugar binding sitechemical bindingcd00057
Zn binding siteion bindingcd03869
active siteactivecd03869

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