neurotrypsin (serine protease 12, motopsin, Leydin, PRSS12)

Function: 1) role in neuronal plasticity 2) proteolytic action may subserve structural reorganizations associated with learning & memory operations Structure: 1) belongs to the peptidase S1 family 2) contains 1 kringle domain - contains 1 peptidase S1 domain - contains 4 SRCR domains Compartment: secreted Expression: expressed in brain & Leydig cells of testis Pathology: - defects in PRSS12 are a cause of autosomal recessive nonsyndromic mental retardation

General

glycoprotein secreted protein serine protease

Properties

SIZE: MW = 97 kD entity length = 875 aa COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-20} proline-rich region SITE: 23-92 MOTIF: proline residue (SEVERAL) N-glycosylation site {N26} Kringle {93-165} MOTIF: cysteine residue {C109} MODIFICATION: cysteine residue {C149} cysteine residue {C138} MODIFICATION: cysteine residue {C163} cysteine residue {C149} MODIFICATION: cysteine residue {C109} cysteine residue {C163} MODIFICATION: cysteine residue {C138} SRCR 1 {170-271} MOTIF: cysteine residue {C195} MODIFICATION: cysteine residue {C259} cysteine residue {C208} MODIFICATION: cysteine residue {C269} cysteine residue {C239} MODIFICATION: cysteine residue {C249} cysteine residue {C249} MODIFICATION: cysteine residue {C239} cysteine residue {C259} MODIFICATION: cysteine residue {C195} cysteine residue {C269} MODIFICATION: cysteine residue {C208} SRCR 2 {280-381} MOTIF: cysteine residue {C305} MODIFICATION: cysteine residue {C369} cysteine residue {C318} MODIFICATION: cysteine residue {C379} cysteine residue {C349} MODIFICATION: cysteine residue {C359} cysteine residue {C359} MODIFICATION: cysteine residue {C349} cysteine residue {C369} MODIFICATION: cysteine residue {C305} cysteine residue {C379} MODIFICATION: cysteine residue {C318} SRCR 3 {387-487} MOTIF: cysteine residue {C412} MODIFICATION: cysteine residue {C475} cysteine residue {C425} MODIFICATION: cysteine residue {C485} cysteine residue {C455} MODIFICATION: cysteine residue {C465} cysteine residue {C465} MODIFICATION: cysteine residue {C455} cysteine residue {C475} MODIFICATION: cysteine residue {C412} cysteine residue {C485} MODIFICATION: cysteine residue {C425} SRCR 4 {500-601} MOTIF: cysteine residue {C525} MODIFICATION: cysteine residue {C589} cysteine residue {C538} MODIFICATION: cysteine residue {C599} cysteine residue {C569} MODIFICATION: cysteine residue {C579} cysteine residue {C579} MODIFICATION: cysteine residue {C569} cysteine residue {C589} MODIFICATION: cysteine residue {C525} cysteine residue {C599} MODIFICATION: cysteine residue {C538} Zymogen activation {619-630} MOTIF: cysteine residue {C619} MODIFICATION: cysteine residue {C750} REACTIVE BOND HOMOLOG (POTENTIAL) {630-631} S1 domain {631-874} MOTIF: cysteine residue {C661} MODIFICATION: cysteine residue {C677} histidine residue {H676} cysteine residue {C677} MODIFICATION: cysteine residue {C661} N-glycosylation site {N683} aspartate residue {D726} cysteine residue {C750} MODIFICATION: cysteine residue {C619} cysteine residue {C765} MODIFICATION: cysteine residue {C831} cysteine residue {C794} MODIFICATION: cysteine residue {C808} cysteine residue {C808} MODIFICATION: cysteine residue {C794} cysteine residue {C821} MODIFICATION: cysteine residue {C850} serine residue {S825} cysteine residue {C831} MODIFICATION: cysteine residue {C765} cysteine residue {C850} MODIFICATION: cysteine residue {C821}

Database Correlations

OMIM correlations UniProt P56730 PFAM correlations

References

UniProt :accession P56730