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UniProtKB - P60330 (ESPL1_MOUSE)

Protein

Separin

Gene

Espl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the SCC1/RAD21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by different mechanisms (By similarity).By similarity

Catalytic activityi

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.

Activity regulationi

Regulated by at least two independent mechanisms. First, it is inactivated via its interaction with securin/PTTG1, which probably covers its active site. The association with PTTG1 is not only inhibitory, since PTTG1 is also required for activating it, the enzyme being inactive in cells in which PTTG1 is absent. PTTG1 degradation at anaphase, liberates it and triggers RAD21 cleavage. Second, phosphorylation at Ser-1121 inactivates it. The complete phosphorylation during mitosis, is removed when cells undergo anaphase. Activation of the enzyme at the metaphase-anaphase transition probably requires the removal of both securin and inhibitory phosphate (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei2025By similarity1

GO - Molecular functioni

  • cysteine-type endopeptidase activity Source: GO_Central
  • cysteine-type peptidase activity Source: MGI
  • peptidase activity Source: MGI
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • chromosome segregation Source: MGI
  • homologous chromosome segregation Source: MGI
  • meiosis I Source: MGI
  • meiotic chromosome separation Source: GO_Central
  • meiotic spindle organization Source: MGI
  • mitotic cell cycle Source: MGI
  • mitotic sister chromatid segregation Source: MGI
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionHydrolase, Protease, Thiol protease
Biological processChromosome partition

Enzyme and pathway databases

BRENDAi3.4.22.49 3474
ReactomeiR-MMU-2467813 Separation of Sister Chromatids

Protein family/group databases

MEROPSiC50.002

Names & Taxonomyi

Protein namesi
Recommended name:
Separin (EC:3.4.22.49)
Alternative name(s):
Caspase-like protein ESPL1
Extra spindle poles-like 1 protein
Separase
Gene namesi
Name:Espl1
Synonyms:Esp1, Kiaa0165
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2146156 Espl1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002059011 – 2118SeparinAdd BLAST2118

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1121PhosphoserineBy similarity1
Modified residuei1391PhosphoserineBy similarity1
Modified residuei1394PhosphoserineBy similarity1
Modified residuei1504PhosphoserineCombined sources1

Post-translational modificationi

Autocleaves. This function, which is not essential for its protease activity, is unknown (By similarity).By similarity
Phosphorylated by CDK1. There is 8 Ser/Thr phosphorylation sites. Among them, only Ser-1121 phosphorylation is the major site, which conducts to the enzyme inactivation (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1502 – 1503Cleavage; by autolysisBy similarity2
Sitei1531 – 1532Cleavage; by autolysisBy similarity2

Keywords - PTMi

Autocatalytic cleavage, Phosphoprotein

Proteomic databases

EPDiP60330
MaxQBiP60330
PaxDbiP60330
PRIDEiP60330

PTM databases

iPTMnetiP60330
PhosphoSitePlusiP60330

Expressioni

Gene expression databases

BgeeiENSMUSG00000058290 Expressed in 182 organ(s), highest expression level in primary oocyte
CleanExiMM_ESPL1
GenevisibleiP60330 MM

Interactioni

Subunit structurei

Interacts with PTTG1. Interacts with RAD21 (By similarity).By similarity

Protein-protein interaction databases

BioGridi222968, 26 interactors
IntActiP60330, 26 interactors
STRINGi10090.ENSMUSP00000064465

Structurei

3D structure databases

SMRiP60330
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1941 – 2036Peptidase C50Add BLAST96

Phylogenomic databases

eggNOGiKOG1849 Eukaryota
COG5155 LUCA
GeneTreeiENSGT00390000004990
HOGENOMiHOG000290657
HOVERGENiHBG051510
InParanoidiP60330
KOiK02365
OMAiLWLYICT
OrthoDBiEOG091G03VI
PhylomeDBiP60330
TreeFamiTF101169

Family and domain databases

InterProiView protein in InterPro
IPR005314 Peptidase_C50
IPR030397 SEPARIN_core_dom
PANTHERiPTHR12792 PTHR12792, 1 hit
PROSITEiView protein in PROSITE
PS51700 SEPARIN, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P60330-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRNFKGVNFA TLLCSKEETQ QLLPDLKEFL SRSRTDFPSS RTDAERRQIC 
        60         70         80         90        100
DTILRACTQQ LTAKLDCPGH LRSILDLAEL ACDGYLLSTP QRPPLYLERI 
       110        120        130        140        150
LFILLRNGST QGSPDTVLRL AQPLHACLVQ NSGEAAPQDY EAVTRGSFSL 
       160        170        180        190        200
FWKGAEALLE RRAAFSTRLN ALSFLVLLED GSVPCEVPHF ASPTACRLVA 
       210        220        230        240        250
AYQLYDATGQ GLDEADADFL YEVLSRHLIR VLVGEGGSSP GPLSPQRALC 
       260        270        280        290        300
LLEITLEHCR RLCWNHHHRQ AARAVERARN HLEKTSVAPS LQLCQMGVEL 
       310        320        330        340        350
LEAVEERPGA VAQLLRKAAA VLINSIEAPS PPLRALYDSC QFFLSGLERG 
       360        370        380        390        400
IRRHCGLDAI LSLFAFLGGY SSLVRHLREV SEASSKQQQC LLQMHFQGFH 
       410        420        430        440        450
LFTGIVYDFA QGCQATELAQ LVDGCRSAAV WMLEALEGLS GGELADYLSM 
       460        470        480        490        500
TASYTSNLAY SFFSQKLYEE ACVISEPVCQ HLGSATSGAC PEVPPEKLHR 
       510        520        530        540        550
CFRLHVESLK KLGKQAQGCK MVTLWLAALK PYSLEHMVEP VTFWVRVKMD 
       560        570        580        590        600
ASRAGDKELQ LQTLRDSLSC WDPETQSLLL REELRAYKSV RADTGQERFN 
       610        620        630        640        650
IICDLLELSP EETAAGAWAR ATYLVELAQV LCYHNFTQQT NCSALDAVQE 
       660        670        680        690        700
ALQLLESVSP EAQEQDRLLD DKAQALLWLY ICTLEAKMQE GIERDRRAQA 
       710        720        730        740        750
PSNLEEFEVN DLNYEDKLQE DRFLYSSIAF NLAADAAQSK CLDQALTLWK 
       760        770        780        790        800
EVLTKGRAPA VRCLQQTAAS LQILAAVYQL VAKPLQALET LLLLQIVSKR 
       810        820        830        840        850
LQDHAKAASS SCQLTQLLLN LGCPSYAQLY LEEAESSLRS LDQTSDACQL 
       860        870        880        890        900
LSLTCALLGS QLCWACQKVT AGVSLLLSVL RDPALQKSSK AWYLLRVQAL 
       910        920        930        940        950
QVLAFYLSLS SNLLSSALRE QLWDQGWQTP ETALIDAHKL LRSIIILLMG 
       960        970        980        990       1000
SDVLSIQKAA TESPFLDYGE NLVQKWQVLT EVLTCSERLV GRLGRLGNVS 
      1010       1020       1030       1040       1050
EAKAFCLEAL KLTTKLQIPR QCALFLVLKG ELELARGDID LCQSDLQQVL 
      1060       1070       1080       1090       1100
FLLESSTEFG VVTQHPDSVK KVHTQKGKHK AQGPCFPPLS EEEPFLKGPA 
      1110       1120       1130       1140       1150
LELVDTVLNE PGPIQSSVNS SPVLKTKPPP NPGFLSHLPS CDCLLCASPA 
      1160       1170       1180       1190       1200
LSAVCLRWVL VTAGVRLATG HKAQGLDLLQ AVLTRCPAAT KRFTQSLQAS 
      1210       1220       1230       1240       1250
LNHRTTPSCV PSLFDEIMAQ VYTHLALEFL NQTSEKSLGK VLASGLKFVA 
      1260       1270       1280       1290       1300
TRIQSLEIWR AHLLLVQALA KLAHFSCCTS ELFASSWGWH PPLVKSLPVL 
      1310       1320       1330       1340       1350
EPAKIRRQKC SGRGRRRIAS VPPPLHNSSQ KGLEEEGPPC TPKPPGRARQ 
      1360       1370       1380       1390       1400
AGPRVPFTIF EEVHPTKSKL QVPLAPRVHR RAQTRLKVIF SDDSDLEDLV 
      1410       1420       1430       1440       1450
SADTQLVEEP KRRGTASRTR GQTRKGRSLK TDAVVAIEST PGHSSVSGRT 
      1460       1470       1480       1490       1500
RRARKVASRN CEEESPKAPL CVWASQGPEI MRSIPEEEPV DNHLEKSFEI 
      1510       1520       1530       1540       1550
LRGSDGEDSA SGEKAAAADT GLPVGECEVL RRDSSKAERP VLYSDTEANS 
      1560       1570       1580       1590       1600
DPSPWLPPFS VPAPIDLSTL DSISDSLSIA FRGVSHCPPS GLYAHLCRFL 
      1610       1620       1630       1640       1650
ALCLGHRDPY ATAFLVAESI SITCRHQLLT HLHRQLSKAQ KQQESPELAE 
      1660       1670       1680       1690       1700
HLQRLDLKER PGGVPLARIQ RLFSFKALGS GCFPQAEKES FQERLALIPS 
      1710       1720       1730       1740       1750
GVTVCVLALA TLQPGTLSNT LLLTRLEKDN PPITVKIPTA QNKLPLSAVL 
      1760       1770       1780       1790       1800
KEFDAIQKDQ KENSSCTEKR VWWTGRLALD QRMEALITAL EEQVLGCWRG 
      1810       1820       1830       1840       1850
LLLPCSADPS LAQEASKLQE LLRECGWEYP DSTLLKVILS GARILTSQDV 
      1860       1870       1880       1890       1900
QALACGLCPA QPDRAQVLLS EAVGQVQSQE APRSQHLVLV LDKDLQKLPW 
      1910       1920       1930       1940       1950
ESTPILQAQP VTRLPSFRFL LSYTVTKEAG ASSVLSQGVD PQNTFYVLNP 
      1960       1970       1980       1990       2000
HSNLSSTEER FRASFSSETG WKGVIGEVPS LDQVQAALTE RDLYIYAGHG 
      2010       2020       2030       2040       2050
AGARFLDGQA VLRLSCRAVA LLFGCSSAAL AVHGNLEGAG IVLKYIMAGC 
      2060       2070       2080       2090       2100
PLFLGNLWDV TDRDIDRYTE ALLQGWLGAG PGAPFLYYAS QARQAPRLKY 
      2110 
LIGAAPVAYG LPISLQTP
Length:2,118
Mass (Da):233,035
Last modified:February 2, 2004 - v1
Checksum:i484FCE178C0984B6
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2R8VI27A0A2R8VI27_MOUSE
Separin
Espl1
110Annotation score:
A0A2R8VHG0A0A2R8VHG0_MOUSE
Separin
Espl1
165Annotation score:
A0A2R8VHV9A0A2R8VHV9_MOUSE
Separin
Espl1
99Annotation score:

Sequence cautioni

The sequence BAC97882 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129072 mRNA Translation: BAC97882.1 Different initiation.
BC145846 mRNA Translation: AAI45847.1
CCDSiCCDS27878.1
RefSeqiNP_001014976.1, NM_001014976.2
XP_006520320.1, XM_006520257.3
XP_006520321.1, XM_006520258.3
XP_006520322.1, XM_006520259.3
XP_011243698.1, XM_011245396.2
UniGeneiMm.288324

Genome annotation databases

EnsembliENSMUST00000064924; ENSMUSP00000064465; ENSMUSG00000058290
ENSMUST00000229050; ENSMUSP00000155304; ENSMUSG00000058290
GeneIDi105988
KEGGimmu:105988
UCSCiuc007xvf.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129072 mRNA Translation: BAC97882.1 Different initiation.
BC145846 mRNA Translation: AAI45847.1
CCDSiCCDS27878.1
RefSeqiNP_001014976.1, NM_001014976.2
XP_006520320.1, XM_006520257.3
XP_006520321.1, XM_006520258.3
XP_006520322.1, XM_006520259.3
XP_011243698.1, XM_011245396.2
UniGeneiMm.288324

3D structure databases

SMRiP60330
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222968, 26 interactors
IntActiP60330, 26 interactors
STRINGi10090.ENSMUSP00000064465

Protein family/group databases

MEROPSiC50.002

PTM databases

iPTMnetiP60330
PhosphoSitePlusiP60330

Proteomic databases

EPDiP60330
MaxQBiP60330
PaxDbiP60330
PRIDEiP60330

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064924; ENSMUSP00000064465; ENSMUSG00000058290
ENSMUST00000229050; ENSMUSP00000155304; ENSMUSG00000058290
GeneIDi105988
KEGGimmu:105988
UCSCiuc007xvf.2 mouse

Organism-specific databases

CTDi9700
MGIiMGI:2146156 Espl1
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1849 Eukaryota
COG5155 LUCA
GeneTreeiENSGT00390000004990
HOGENOMiHOG000290657
HOVERGENiHBG051510
InParanoidiP60330
KOiK02365
OMAiLWLYICT
OrthoDBiEOG091G03VI
PhylomeDBiP60330
TreeFamiTF101169

Enzyme and pathway databases

BRENDAi3.4.22.49 3474
ReactomeiR-MMU-2467813 Separation of Sister Chromatids

Miscellaneous databases

PROiPR:P60330
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000058290 Expressed in 182 organ(s), highest expression level in primary oocyte
CleanExiMM_ESPL1
GenevisibleiP60330 MM

Family and domain databases

InterProiView protein in InterPro
IPR005314 Peptidase_C50
IPR030397 SEPARIN_core_dom
PANTHERiPTHR12792 PTHR12792, 1 hit
PROSITEiView protein in PROSITE
PS51700 SEPARIN, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiESPL1_MOUSE
AccessioniPrimary (citable) accession number: P60330
Secondary accession number(s): A6H6E3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: October 10, 2018
This is version 116 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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