polyserase-2 (polyserine protease 2, serine protease 36, PRSS36)

Function: 1) serine protease 2) hydrolyzes the peptides N-t-Boc-Gln-Ala-Arg-AMC & N-t-Boc-Gln-Gly-Arg-AMC > N-t-Boc-Ala-Phe-Lys-AMC & N-t-Boc-Val-Leu-Lys-AMC 3) preference for substrates with Arg instead of Lys residue in position P1 Inhibition: - inhibited by serine proteinase inhibitor 4-(2-aminoethyl)-benzenesulfonyl fluoride (AEBSF), but not by EDTA or E-64 Structure: - 1st serine protease domain is catalytically active, 2nd domain lacks the essential His of catalytic triad at position 363, thus inactive 3rd domain lacks essential Asp of catalytic triad at position 679, thus inactive - the 3 protease domains are not proteolytically cleaved - N-glycosylated - belongs to the peptidase S1 family Compartment: extracellular matrix Expression: - expressed in fetal kidney, skeletal muscle, liver, placenta, heart Pathology: - expressed in tumor cell lines derived from lung & colon adenocarcinomas

General

glycoprotein secreted protein serine protease

Properties

SIZE: MW = 92 kD entity length = 855 aa COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-22} S1 domain {47-291} MOTIF: cysteine residue {C72} MODIFICATION: cysteine residue {C88} histidine residue {H87} cysteine residue {C88} MODIFICATION: cysteine residue {C72} N-glycosylation site {N92} N-glycosylation site {N130} aspartate residue {D139} cysteine residue {C173} MODIFICATION: cysteine residue {C249} cysteine residue {C206} MODIFICATION: cysteine residue {C228} N-glycosylation site {N217} cysteine residue {C228} MODIFICATION: cysteine residue {C206} cysteine residue {C239} MODIFICATION: cysteine residue {C267} serine residue {S243} cysteine residue {C249} MODIFICATION: cysteine residue {C173} cysteine residue {C267} MODIFICATION: cysteine residue {C239} N-glycosylation site {N317} S1 domain {323-555} MOTIF: cysteine residue {C348} MODIFICATION: cysteine residue {C364} cysteine residue {C364} MODIFICATION: cysteine residue {C348} N-glycosylation site {N369} N-glycosylation site {N402} N-glycosylation site {N407} N-glycosylation site {N421} cysteine residue {C444} MODIFICATION: cysteine residue {C516} cysteine residue {C506} MODIFICATION: cysteine residue {C534} N-glycosylation site {N508} cysteine residue {C516} MODIFICATION: cysteine residue {C444} cysteine residue {C534} MODIFICATION: cysteine residue {C506} S1 domain {590-808} MOTIF: cysteine residue {C615} MODIFICATION: cysteine residue {C631} cysteine residue {C631} MODIFICATION: cysteine residue {C615} cysteine residue {C711} MODIFICATION: cysteine residue {C772} cysteine residue {C739} MODIFICATION: cysteine residue {C751} cysteine residue {C751} MODIFICATION: cysteine residue {C739} cysteine residue {C772} MODIFICATION: cysteine residue {C711}

Database Correlations

UniProt Q5K4E3 Pfam PF00089

References

UniProt :accession Q5K4E3