R4XPW1 · R4XPW1_PICAB

Function

Catalytic activity

  • All bonds known to be hydrolyzed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by a hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage.
    EC:3.4.22.49 (UniProtKB | ENZYME | Rhea)

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentmitotic spindle
Cellular Componentnucleus
Molecular Functioncysteine-type endopeptidase activity
Biological Processmeiotic chromosome separation
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    separase
  • EC number

Gene names

    • Name
      separase

Organism names

Accessions

  • Primary accession
    R4XPW1

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2063-2158Peptidase C50

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,307
  • Mass (Da)
    258,627
  • Last updated
    2013-07-24 v1
  • Checksum
    601EA3E834790EDF
MEPATILAKAEGYDVAGLHKQVAGYLKALLGFINGKENKKNTPEIHRLAKKYVPNFLVPLLKVCCNNLTKGISETDELSQNRADELFKTLKLALDCLEALRPCLVGSPYEIETQRYWMVRRLMAWKRFTEAREECWNTLDKLKRNLFPAAKEKDKYGVNLYGEQAAGSDPSLAGLILGLVMDLIICIGESRPKDAEVLEKVPLLVDQLTPWRRVLDNNSAEKHNSMLFKGLQKCIEFMAKEPSNFNPKLIRNISVLALKNCACSSVKDQFINVTCRICHQLASGGSQLSSTVDNIYKVALIILFKDGQLFGEYEALKVIEYYFRYCEANPKLRKDAKQFLNGIADNLGQGSTFPLAAVLHIYAISLGFEDIEVSGSCNDDAIYIEDDVSEAPKIPIHVENQDSVLLSNSVQIIQTTIEKFKWRSGELVVQRHGNNVALCDGKSKSYEVSNNNQKCIGGSLISISKALEFLWKVFSGYVQQEWDIFIASSTTIKASVWHPSLEKAFHLFTQVFIVGFSSNFVSVEEKKELRKVCQTLLLAASAALKLSLMHQEAVQECFETISTLISGSWIEVKELKWLISYMYNIGVAMFNMKQYDGACGPLKLAYKAAWTRVSLLKNLSSDESTASGFGCSMSDNISESVSDACGKSVVLVDALQRSGRKEARENITDCLLQWTKVDTQLSSPNNLRSLVKLWVKMVCADYKEIDIDEASVQSLTLYKVLSSNGCSLPMGTLGTLLEEELLAYSKIETELSRFMRKGILELLLDDVYVAKEFSLERSRVLLEQTKIDRLSGAAGLGRCMDCLSDAILLLRNVLNEDYNPNGNSSFLDRVRHQLAITYCVHAICTQEANANSEVICDDISLAMKLWEQIDSFQCLELNGEKDWLTDTSIPLLLNMLELLALKGFTYLQSKLQELVLTIFKSWKKMASEECCALLWRENRLSHALCCVSVSQKSLSILMEKFGIAVNSINFWENCVKDNPGSVLEFQQKLMYDEFLEVQSDRGLETSSLSSSVCTVEVLKERALTLVSNGLKTRESAFLASSMFYMLSKKYRRKGQLLAALRYSKEALLIRTKVLHRKFKFLDKKSIQVARDNSAEFKNESNEVGGIYLEALGSVTTNVWPTFSDAEKDGEYWPSQWVVLGNYLENLMQVGVLCEMVGDGDEAENIFQEGLKISNAQDLPLGQAAFGSCLGEIYRKRHSWEKAEEILKNAKQVFHRQDLKLVCKLCQVTVEATLDMRIGDLVRRCPKEKTNVHFPENPTSAIDVYTLARENLCKEMSKAQLAESLGYTAIDVKKKRGTGQRGQKSSRRVDLDESIIEVRDYLKDSESTCRKTRSRSKAGNNCDLVVEGTEHLSLSKTPRQSTGSLIARDDIDKTSYSLRKKTQHKPRSVVHIGSRNNSEELSHDKDCSGLCEIERDKVHSMQELIAFCWECHTRSVLSRLLLQIGKCYKASEELHKVHEIFLQNISLLFFHNGRSPCLCSFGTAHCCQLECSGKRNPVDIFLIERAALLYHISWLSLSKIDCSLSWMQCCKFAENQTSLVLGWLQHAFFICSQMPALFQKVSMLLAILHLPLESGGLFSLPMRHGSNLSTSHWAAYFHQASLGTALRQRHLIVLDSKLESLASDSEEHHHSSKDVITRVQQALRLIPETVEDLEHFVTDFFKNVPLSTIICVSLLDSKHVSLLGDLPFNNSSPAWMFLTRFGSKGQPVVLLLPILSNFEGSSKDDAGGSMVSCPYTIDLDCEDSEGNDIDSSSEAKKLIYGSSKTVVDLVAEEFGLVLEESRLSTSNSLPVPSNEDKCRWWQWRIELDKRLAKLLRGIEDSWFGPWKCFLLGEPLEATINNAVDARIQDVKQMLGLAATSAGVETHVPVDEGLLKVLLAGSTSLRYNEIEKGVSCLLWRNFNILQSYGSDNLERSQREEIVGKAAKALSSVFQNSEADKIADQKVHNNEPGMSLHQEKQEDFTGSNMTYIQREPVVLVLDANSQVLPWESLPILRKHEVYRMPSVSSILAVMASRFNADSVDVFDKGEKTMLKGRKNTKQERSSRKTIKSSILEQPARLPIVDPYNTFYLLNPSGDLGSTQAAFEDWFKNQKGWEGKMGVVPSPEECISALQKHDLFIYFGHGSGEQYLSGRNIRRLDHCAAAVLMGCSSGRLSCRGDYEPVGVPLSYLIAGCPSIIANLWDVTDGDIDRFSRILLNGWLESVSSHCSELEMLEEFQNLTIAGHKGAKKVKEPMQKGKDDEVQSMQVKQAVSEKVFDISRRPKSTRGTVRTGSFIGEGRSTCRLPYLIGASPVCYGVPTTIKTKRTSV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HE793991
EMBL· GenBank· DDBJ
CCG89179.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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