Summary for peptidase C50.001: separase (yeast-type)

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Literature Human EST Mouse EST Substrates

 

Names
MEROPS Nameseparase (yeast-type)
Other namesBimB g.p. (Aspergillus nidulans ), Cut1 g.p. (Schizosaccharomyces pombe), Esp1 g.p. (Saccharomyces cerevisiae), ESPL1, separin, EXTRA SPINDLE POLES
Domain architecture
MEROPS Classification
Classification Clan CD >> Subclan (none) >> Family C50 >> Subfamily (none) >> C50.001
Holotypeseparase (yeast-type) (Saccharomyces cerevisiae), Uniprot accession Q03018 (peptidase unit: 996-1629), MERNUM MER0010982
History Identifier created: MEROPS 5.0 (17 April 2000)
Activity
Catalytic typeCysteine
PeplistIncluded in the Peplist with identifier PL00119
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.22 (Cysteine endopeptidases) >> Peptidase 3.4.22.49
EnzymologyBRENDA database
Proteolytic eventsCutDB database (12 cleavages)
Activity statushuman: active (Peters & Nasmyth, 2004)
mouse: active (Terret et al., 2003)
PhysiologyIn cell division, prior to anaphase, the pairs of sister chromatids are bound together by a protein called cohesin. Separin is the endopeptidase that can cleave cohesin (at arginine residues). The activity of separin is inhibited by securin, but this is destroyed at the start of anaphase, allowing separin to cleave cohesin, and the chromosomes to separate towards the poles of the spindle. This is a vital function in the division of eukaryotic cells (Nasmyth et al., 2000). It has also been shown that the cleavage of Rec8 by separin during meiosis of yeast is necessary for the resolution of chiasmata and the disjunction of homologous chromosomes (Buonomo et al., 2000). A mutation in separase is responsible for cell cycle defects in zebrafish (Shepard et al., 2007).
Pathways KEGGCell cycle - yeast
KEGGMeiosis - yeast
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage patternE/-/Glm/RScissile bond-/-/-/- (based on 12 cleavages)
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Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 0 0 7 0 1 1 1 1
Pro 0 1 0 0 0 0 2 1
Ala 0 1 0 0 0 2 2 2
Val 0 2 0 0 0 0 0 1
Leu 0 1 2 0 2 1 0 1
Ile 0 3 0 0 0 1 0 0
Met 0 0 2 0 0 0 0 0
Phe 0 0 0 0 0 1 1 0
Tyr 0 2 0 0 0 0 0 0
Trp 0 0 0 0 0 0 0 0
Ser 0 0 1 0 1 3 3 2
Thr 0 0 0 0 1 0 0 0
Cys 0 0 0 0 0 0 0 0
Asn 0 0 0 0 1 0 0 0
Gln 0 1 0 0 0 1 1 0
Asp 1 0 0 0 1 1 1 0
Glu 11 0 0 0 1 0 1 2
Lys 0 0 0 0 2 0 0 0
Arg 0 1 0 12 2 1 0 1
His 0 0 0 0 0 0 0 1