Procollagen C-endopeptidase enhancer 1; Procollagen COOH-terminal proteinase enhancer 1; PCPE-1; Procollagen C-proteinase enhancer 1; type 1 procollagen C-proteinase enhancer protein; type I procollagen COOH-terminal proteinase enhancer (PCOLCE, PCPE1)

Function: - binds to the C-terminal propeptide of type I procollagen & enhances procollagen C-proteinase activity - C-terminal processed part of PCPE (CT-PCPE) may have an metalloproteinase inhibitory activity - C-terminally processed at multiple positions Structure: - contains 2 CUB domains - contains 1 NTR domain Compartment: secreted

General

glycoprotein secreted protein

Properties

SIZE: entity length = 449 aa MW = 48 kD COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-25} N-glycosylation site {N29} CUB domain {37-149} MOTIF: cysteine residue {C37} MODIFICATION: cysteine residue {C63} cysteine residue {C63} MODIFICATION: cysteine residue {C37} cysteine residue {C90} MODIFICATION: cysteine residue {C112} cysteine residue {C112} MODIFICATION: cysteine residue {C90} CUB domain {159-273} MOTIF: cysteine residue {C159} MODIFICATION: cysteine residue {C186} cysteine residue {C186} MODIFICATION: cysteine residue {C159} cysteine residue {C213} MODIFICATION: cysteine residue {C236} cysteine residue {C236} MODIFICATION: cysteine residue {C213} proteolytic site {287-288} proteolytic site {288-289} proteolytic site {293-294} proteolytic site {299-300} proteolytic site {303-304} NTR {318-437} MOTIF: cysteine residue {C318} MODIFICATION: cysteine residue {C386} cysteine residue {C322} MODIFICATION: cysteine residue {C389} cysteine residue {C333} MODIFICATION: cysteine residue {C437} cysteine residue {C386} MODIFICATION: cysteine residue {C318} cysteine residue {C389} MODIFICATION: cysteine residue {C322} N-glycosylation site {N431} cysteine residue {C437} MODIFICATION: cysteine residue {C333}

Database Correlations

OMIM 600270 UniProt Q15113 PFAM correlations Entrez Gene 5118 Kegg hsa:5118

References

UniProt :accession Q15113