prolyl-4-hydroxylase; proline hydroxylase; protocollagen prolyl hydroxylase; proline, 2-oxoglutarate dioxygenase

Function: - catalyzes post-translational formation of 4-hydroxyproline in -Xaa-Pro-gly- sequences in collagens & other proteins procollagen L-proline + 2-oxoglutarate + O₂ procollagen trans-4-hydroxy-L-proline + succinate + CO₂ Structure: - heterotetramer of two alpha-2 chains & two beta chains (the beta chain is the multi-functional PDI)

General

dioxygenase hydroxylase; monooxygenase multisubunit protein

Properties

MOTIF: active site SUBUNITS: prolyl 4-hydroxylase alpha subunit MOTIF: glycosylation site membrane region protein disulfide isomerase MOTIF: signal sequence {1-17} thioredoxin domain SITE: 25-134 MOTIF: cysteine residue {C53} MODIFICATION: cysteine residue {C56} cysteine residue {C53} Contributes to redox potential value {54-54} Contributes to redox potential value {55-55} cysteine residue {C56} cysteine residue {C56} MODIFICATION: cysteine residue {C53} Lowers pKa of C-terminal Cys of first active site {120-120} thioredoxin domain SITE: 368-475 MOTIF: cysteine residue {C397} MODIFICATION: cysteine residue {C400} cysteine residue {C397} Contributes to redox potential value {398-398} Contributes to redox potential value {399-399} cysteine residue {C400} cysteine residue {C400} MODIFICATION: cysteine residue {C397} Lowers pKa of C-terminal Cys of second active site {461-461} Prevents secretion from ER {505-508}

References

UniProt :accession O15460

Components

prolyl 4-hydroxylase alpha subunit protein disulfide isomerase (cellular thyroid hormone binding protein, prolyl 4-hydroxylase subunit beta, P4HB, ERBA2L, PDI, PDIA1, PO4DB)