transmembrane serine protease 9; polyserase-1; polyserine protease 1 [Contains: serase-1; serase-2; serase-3] (TMPRSS9)

Function: - precusor for serase-1, serase-2 & serase-3 - proteolytically cleaved to generate 3 independent serine protease chains Structure: - serine protease 1 & 2 domains are catalytically active - serine protease 3 domain lacks the essential Ser catalytic triad at position 1009, thus is predicted to be inactive - proteolytically cleaved to generate 3 independent serine protease chain - cleaved chains may remain attached to the membrane via disufide bonds - unclear whether cleavage always takes place - belongs to the peptidase S1 family - contains 1 LDL-receptor class A domain - contains 3 peptidase S1 domains Compartment: cell membrane Alternative splicing: named isoforms=2 Expression: - expressed in fetal human tissues, including kidney, liver, lung, brain - weakly expressed in adult tissues, including skeletal muscle, liver, placenta, heart Pathology: - expressed in a variety of tumor cell lines

General

glycoprotein transmembrane serine protease

Properties

SIZE: MW = 114 kD entity length = 1059 aa COMPARTMENT: cellular membrane MOTIF: transmembrane domain {30-50} LDL-receptor class A {153-190} MOTIF: cysteine residue {C154} MODIFICATION: cysteine residue {C166} cysteine residue {C161} MODIFICATION: cysteine residue {C180} cysteine residue {C166} MODIFICATION: cysteine residue {C154} cysteine residue {C174} MODIFICATION: cysteine residue {C189} cysteine residue {C180} MODIFICATION: cysteine residue {C161} cysteine residue {C189} MODIFICATION: cysteine residue {C174} proteolytic site {202-203} S1 domain {203-436} MOTIF: cysteine residue {C228} MODIFICATION: cysteine residue {C244} histidine residue {H243} cysteine residue {C244} MODIFICATION: cysteine residue {C228} aspartate residue {D292} cysteine residue {C326} MODIFICATION: cysteine residue {C393} cysteine residue {C358} MODIFICATION: cysteine residue {C372} cysteine residue {C372} MODIFICATION: cysteine residue {C358} cysteine residue {C383} MODIFICATION: cysteine residue {C412} serine residue {S387} cysteine residue {C393} MODIFICATION: cysteine residue {C326} cysteine residue {C412} MODIFICATION: cysteine residue {C383} proteolytic site {503-504} S1 domain {504-736} MOTIF: cysteine residue {C529} MODIFICATION: cysteine residue {C545} histidine residue {H544} cysteine residue {C545} MODIFICATION: cysteine residue {C529} N-glycosylation site {N547} aspartate residue {D592} cysteine residue {C626} MODIFICATION: cysteine residue {C693} N-glycosylation site {N638} cysteine residue {C658} MODIFICATION: cysteine residue {C672} N-glycosylation site {N663} cysteine residue {C672} MODIFICATION: cysteine residue {C658} cysteine residue {C683} MODIFICATION: cysteine residue {C712} serine residue {S687} cysteine residue {C693} MODIFICATION: cysteine residue {C626} cysteine residue {C712} MODIFICATION: cysteine residue {C683} N-glycosylation site {N786} proteolytic site {826-827} S1 domain {827-1058} MOTIF: cysteine residue {C853} MODIFICATION: cysteine residue {C869} cysteine residue {C869} MODIFICATION: cysteine residue {C853} cysteine residue {C949} MODIFICATION: cysteine residue {C1015} cysteine residue {C980} MODIFICATION: cysteine residue {C994} cysteine residue {C994} MODIFICATION: cysteine residue {C980} cysteine residue {C1005} MODIFICATION: cysteine residue {C1034} cysteine residue {C1015} MODIFICATION: cysteine residue {C949} cysteine residue {C1034} MODIFICATION: cysteine residue {C1005}

Database Correlations

UniProt Q7Z410 PFAM correlations

References

UniProt :accession Q7Z410