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Protein

Separin

Gene

ESP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the MCD1/SCC1 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by securin/PDS1 protein. It also promotes anaphase spindle elongation. A component of the FEAR (CDC14 early anaphase release) network which promotes CDC14 release from the nucleolus during early anaphase. Cleaves SLK19.4 Publications

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.

Enzyme regulationi

It is inactivated via its interaction with PDS1, which probably covers its active site. PDS1 degradation at anaphase, liberates it and triggers MCD1 cleavage.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1531By similarity1

GO - Molecular functioni

  • cysteine-type endopeptidase activity Source: SGD

GO - Biological processi

  • apoptotic process Source: SGD
  • meiotic chromosome separation Source: GO_Central
  • mitotic sister chromatid segregation Source: SGD
  • negative regulation of phosphoprotein phosphatase activity Source: SGD
  • positive regulation of exit from mitosis Source: SGD
  • regulation of exit from mitosis Source: SGD
  • regulation of mitotic spindle elongation Source: SGD

Keywordsi

Molecular functionHydrolase, Protease, Thiol protease
Biological processChromosome partition
LigandCalcium

Enzyme and pathway databases

BioCyciYEAST:G3O-30808-MONOMER.
BRENDAi3.4.22.49. 984.
ReactomeiR-SCE-2467813. Separation of Sister Chromatids.

Protein family/group databases

MEROPSiC50.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Separin (EC:3.4.22.49)
Alternative name(s):
Separase
Gene namesi
Name:ESP1
Ordered Locus Names:YGR098C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR098C.
SGDiS000003330. ESP1.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasmcytoskeletonmicrotubule organizing centerspindle pole body 1 Publication
  • Cytoplasm 1 Publication

  • Note: Accumulates in the nucleus in G2 and is mobilized onto the spindle pole bodies and spindle midzone at anaphase onset, where it persists into midanaphase. The association with MCD1 may be important for its nuclear targeting.

GO - Cellular componenti

  • cytoplasm Source: SGD
  • mitotic spindle Source: GO_Central
  • nucleus Source: SGD
  • spindle Source: SGD
  • spindle pole body Source: UniProtKB-SubCell

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1568 – 1570DKD → AKA: Reduces function. Loss of function. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002059041 – 1630SeparinAdd BLAST1630

Proteomic databases

MaxQBiQ03018.
PRIDEiQ03018.

PTM databases

iPTMnetiQ03018.

Interactioni

Subunit structurei

May bind calcium. Interacts with PDS1. Interacts with MCD1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC55Q003622EBI-6657,EBI-1942

Protein-protein interaction databases

BioGridi33341. 278 interactors.
DIPiDIP-2933N.
IntActiQ03018. 7 interactors.
MINTiMINT-614508.
STRINGi4932.YGR098C.

Structurei

Secondary structure

11630
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi54 – 73Combined sources20
Helixi75 – 80Combined sources6
Helixi82 – 98Combined sources17
Helixi103 – 121Combined sources19
Helixi125 – 137Combined sources13
Helixi147 – 151Combined sources5
Turni157 – 162Combined sources6
Helixi163 – 176Combined sources14
Helixi180 – 192Combined sources13
Helixi194 – 197Combined sources4
Turni198 – 200Combined sources3
Helixi206 – 219Combined sources14
Helixi224 – 237Combined sources14
Helixi242 – 244Combined sources3
Helixi251 – 259Combined sources9
Turni261 – 264Combined sources4
Helixi267 – 271Combined sources5
Helixi273 – 284Combined sources12
Beta strandi286 – 288Combined sources3
Helixi292 – 295Combined sources4
Helixi298 – 308Combined sources11
Helixi320 – 322Combined sources3
Beta strandi324 – 326Combined sources3
Helixi332 – 347Combined sources16
Helixi353 – 370Combined sources18
Helixi376 – 391Combined sources16
Helixi399 – 418Combined sources20
Helixi422 – 438Combined sources17
Helixi442 – 459Combined sources18
Turni462 – 464Combined sources3
Helixi465 – 478Combined sources14
Helixi482 – 492Combined sources11
Helixi495 – 498Combined sources4
Helixi504 – 517Combined sources14
Helixi519 – 522Combined sources4
Helixi535 – 543Combined sources9
Helixi552 – 554Combined sources3
Helixi557 – 567Combined sources11
Helixi574 – 577Combined sources4
Helixi586 – 590Combined sources5
Helixi591 – 606Combined sources16
Helixi612 – 622Combined sources11
Helixi624 – 626Combined sources3
Helixi627 – 630Combined sources4
Helixi636 – 651Combined sources16
Helixi655 – 667Combined sources13
Helixi669 – 672Combined sources4
Turni673 – 675Combined sources3
Helixi676 – 689Combined sources14
Helixi693 – 706Combined sources14
Beta strandi709 – 712Combined sources4
Helixi714 – 723Combined sources10
Helixi727 – 729Combined sources3
Beta strandi730 – 732Combined sources3
Helixi734 – 742Combined sources9
Helixi744 – 748Combined sources5
Helixi750 – 753Combined sources4
Helixi763 – 786Combined sources24
Helixi790 – 809Combined sources20
Beta strandi810 – 812Combined sources3
Helixi816 – 839Combined sources24
Helixi843 – 859Combined sources17
Helixi863 – 879Combined sources17
Helixi883 – 897Combined sources15
Turni902 – 904Combined sources3
Helixi906 – 915Combined sources10
Helixi919 – 925Combined sources7
Helixi927 – 930Combined sources4
Helixi931 – 933Combined sources3
Helixi939 – 946Combined sources8
Helixi953 – 955Combined sources3
Helixi958 – 960Combined sources3
Helixi961 – 980Combined sources20
Helixi984 – 989Combined sources6
Beta strandi994 – 997Combined sources4
Helixi1046 – 1062Combined sources17
Helixi1065 – 1067Combined sources3
Helixi1070 – 1088Combined sources19
Helixi1096 – 1106Combined sources11
Helixi1109 – 1122Combined sources14
Helixi1126 – 1130Combined sources5
Helixi1145 – 1161Combined sources17
Beta strandi1165 – 1173Combined sources9
Turni1175 – 1177Combined sources3
Beta strandi1180 – 1186Combined sources7
Turni1187 – 1190Combined sources4
Beta strandi1191 – 1197Combined sources7
Helixi1214 – 1232Combined sources19
Helixi1234 – 1237Combined sources4
Helixi1243 – 1271Combined sources29
Turni1272 – 1275Combined sources4
Helixi1276 – 1279Combined sources4
Helixi1286 – 1303Combined sources18
Helixi1305 – 1309Combined sources5
Helixi1313 – 1315Combined sources3
Helixi1321 – 1328Combined sources8
Helixi1337 – 1354Combined sources18
Helixi1361 – 1363Combined sources3
Helixi1366 – 1381Combined sources16
Beta strandi1390 – 1396Combined sources7
Helixi1398 – 1400Combined sources3
Helixi1405 – 1407Combined sources3
Turni1409 – 1413Combined sources5
Beta strandi1416 – 1420Combined sources5
Helixi1422 – 1431Combined sources10
Turni1432 – 1434Combined sources3
Beta strandi1436 – 1441Combined sources6
Beta strandi1446 – 1450Combined sources5
Helixi1457 – 1470Combined sources14
Beta strandi1478 – 1483Combined sources6
Helixi1487 – 1495Combined sources9
Beta strandi1498 – 1505Combined sources8
Turni1509 – 1511Combined sources3
Helixi1514 – 1517Combined sources4
Beta strandi1526 – 1528Combined sources3
Turni1531 – 1534Combined sources4
Beta strandi1537 – 1539Combined sources3
Beta strandi1542 – 1545Combined sources4
Helixi1547 – 1553Combined sources7
Beta strandi1557 – 1564Combined sources8
Helixi1568 – 1582Combined sources15
Helixi1598 – 1605Combined sources8
Helixi1606 – 1608Combined sources3
Beta strandi1609 – 1611Combined sources3
Turni1612 – 1617Combined sources6
Beta strandi1619 – 1623Combined sources5
Beta strandi1626 – 1629Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5U1SX-ray3.00A51-1630[»]
5U1TX-ray2.60A51-1630[»]
ProteinModelPortaliQ03018.
SMRiQ03018.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1443 – 1542Peptidase C50Add BLAST100

Phylogenomic databases

GeneTreeiENSGT00390000004990.
HOGENOMiHOG000065988.
InParanoidiQ03018.
KOiK02365.
OMAiLFHGEEN.
OrthoDBiEOG092C03KT.

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.

Sequencei

Sequence statusi: Complete.

Q03018-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMVKQEEPLN EISPNTPMTS KSYLLNDTLS KVHHSGQTRP LTSVLSGDAS
60 70 80 90 100
SNSIGILAMH NNIIRDFTKI ASNNIDLAIE DITTVDHSLN SIYSLLKSHH
110 120 130 140 150
MWGHINSTVK QHLMIIVKLI NNNALGLASS EIIFLFNETN LFQAHSLKNI
160 170 180 190 200
LLADFSTWND YYLSNLKILA LQIILKRKLV DEYLPHILEL FSHDKRYLLK
210 220 230 240 250
DPNLKAHALT KIVLSFFSVT TSCKVLFGLK FLQYIKQFKL PFKKFISNIT
260 270 280 290 300
VECFSKNLLH KNYLEMGPNK IYLNSFYLSY SMLYDGLDKI MLLDILSYEE
310 320 330 340 350
TTEVQRAIKS KKEFNEYCNM SENRLLWSCI SVDDLNVILE NATNFLQNKG
360 370 380 390 400
KHISATLKCL VCLWSTIRLE GLPKNKDILR QFDCTVIYIN SNIKSINDES
410 420 430 440 450
AAALLSELLG VLSEICIDYK EPKRLSNIIS VLFNASVLFK SHSFLLKTAN
460 470 480 490 500
LEISNVLISN DSKTSHRTIL KFEKFISSAQ SAQKKIEIFS CLFNVYCMLR
510 520 530 540 550
NDTLSFVFDF CQNAFIHCFT RLKITKFIEF SNSSEIMLSV LYGNSSIENI
560 570 580 590 600
PSENWSQLSR MIFCSLRGIF DLDPLELNNT FDKLHLLNKY ELLIRIVYLL
610 620 630 640 650
NLDMSKHLTT NLSKITKLYI NKWLQKSDEK AERISSFEMD FVKMLLCYLN
660 670 680 690 700
FNNFDKLSIE LSLCIKSKEK YYSSIVPYAD NYLLEAYLSL YMIDDALMMK
710 720 730 740 750
NQLQKTMNLS TAKIEQALLH ASSLINVHLW DSDLTAFQIY FGKTLPAMKP
760 770 780 790 800
ELFDINNDHN LPMSLYIKVI LLNIKIFNES AKLNIKAGNV ISAVIDCRKA
810 820 830 840 850
QNLALSLLKK KNKLSQGSRL ALLKSLSFSF FQLIKIHIRI GSARDCEFYS
860 870 880 890 900
KELSRIISDL EEPIIVYRCL HFLHRYYMIT EQTCLQNITL GKANKAFDYL
910 920 930 940 950
DAEADITSLT MFLYDNKEFV KLEQSLVLYF GDQLEKTFLP NLWKLHLGKD
960 970 980 990 1000
IDDSICLSEY MPKNVINRVH NMWQKVMSQL EEDPFFKGMF ESTLGIPSSL
1010 1020 1030 1040 1050
PVIPSTMPNN ILKTPSKHST GLKLCDSPRS SSMTPRGKNI RQKFDRIAAI
1060 1070 1080 1090 1100
SKLKQMKELL ESLKLDTLDN HELSKISSLS SLTLTILSNI TSIHNAESSL
1110 1120 1130 1140 1150
ITNFSLTDLP RHMPLLFDKV LNNIDNKNYR EFRVSSLIAP NNISTITESI
1160 1170 1180 1190 1200
RVSAAQKDLM ESNLNINVIT IDFCPITGNL LLSKLEPRRK RRTHLRLPLI
1210 1220 1230 1240 1250
RSNSRDLDEV HLSFPEATKK LLSIINESNQ TTSVEVTNKI KTREERKSWW
1260 1270 1280 1290 1300
TTRYDLDKRM QQLLNNIENS WFNGVQGFFS PEVVDNSLFE KFKDKFYEIL
1310 1320 1330 1340 1350
HQNLPSRKLY GNPAMFIKVE DWVIELFLKL NPQEIDFLSK MEDLIYFVLD
1360 1370 1380 1390 1400
ILLFHGEENA YDEIDFSMLH VQLEEQIKKY RATMTTNSIF HTFLVVSSSC
1410 1420 1430 1440 1450
HLFPWECLSF LKDLSITRVP SYVCLNKLLS RFHYQLPLQV TIEDNISMIL
1460 1470 1480 1490 1500
NPNGDLSRTE SKFKGMFQKI IDAKPSSQLV MNEKPEEETL LKMLQNSNLF
1510 1520 1530 1540 1550
VYIGHGGGEQ YVRSKEIKKC TKIAPSFLLG CSSAAMKYYG KLEPTGTIYT
1560 1570 1580 1590 1600
YLLGGCPMVL GNLWDVTDKD IDKFSEELFE KMGFRCNTDD LNGNSLSVSY
1610 1620 1630
AVSKSRGVCH LRYLNGAAPV IYGLPIKFVS
Length:1,630
Mass (Da):187,447
Last modified:October 1, 1996 - v2
Checksum:iFBAFD33FF706C6BA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti136F → S in AAB03897 (PubMed:1493337).Curated1
Sequence conflicti250 – 253TVEC → IRRV in AAB03897 (PubMed:1493337).Curated4
Sequence conflicti540V → L in AAB03897 (PubMed:1493337).Curated1
Sequence conflicti636S → Y in AAB03897 (PubMed:1493337).Curated1
Sequence conflicti782K → E in AAB03897 (PubMed:1493337).Curated1
Sequence conflicti800A → E in AAB03897 (PubMed:1493337).Curated1
Sequence conflicti1146I → T in AAB03897 (PubMed:1493337).Curated1
Sequence conflicti1295K → R in AAB03897 (PubMed:1493337).Curated1
Sequence conflicti1333 – 1336QEID → ARKSI in AAB03897 (PubMed:1493337).Curated4
Sequence conflicti1443E → Q in AAB03897 (PubMed:1493337).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07289 Genomic DNA. Translation: AAB03897.1.
Z72883 Genomic DNA. Translation: CAA97101.1.
BK006941 Genomic DNA. Translation: DAA08191.1.
PIRiS64403.
RefSeqiNP_011612.3. NM_001181227.3.

Genome annotation databases

EnsemblFungiiYGR098C; YGR098C; YGR098C.
GeneIDi852990.
KEGGisce:YGR098C.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiESP1_YEAST
AccessioniPrimary (citable) accession number: Q03018
Secondary accession number(s): D6VUN0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: July 5, 2017
This is version 151 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names