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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

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

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
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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