Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q03018 (ESP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Separin

EC=3.4.22.49
Alternative name(s):
Separase
Gene names
Name:ESP1
Ordered Locus Names:YGR098C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1630 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.6 Ref.7

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.

Enzyme regulation

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

Subunit structure

May bind calcium. Interacts with PDS1. Interacts with MCD1. Ref.4

Subcellular location

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centerspindle pole body. Cytoplasm. 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. Ref.6

Sequence similarities

Contains 1 peptidase C50 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDC55Q003622EBI-6657,EBI-1942

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16301630Separin
PRO_0000205904

Regions

Domain1443 – 1542100Peptidase C50

Sites

Active site15311 By similarity

Experimental info

Mutagenesis1568 – 15703DKD → AKA: Reduces function. Loss of function. Ref.6
Sequence conflict1361F → S in AAB03897. Ref.1
Sequence conflict250 – 2534TVEC → IRRV in AAB03897. Ref.1
Sequence conflict5401V → L in AAB03897. Ref.1
Sequence conflict6361S → Y in AAB03897. Ref.1
Sequence conflict7821K → E in AAB03897. Ref.1
Sequence conflict8001A → E in AAB03897. Ref.1
Sequence conflict11461I → T in AAB03897. Ref.1
Sequence conflict12951K → R in AAB03897. Ref.1
Sequence conflict1333 – 13364QEID → ARKSI in AAB03897. Ref.1
Sequence conflict14431E → Q in AAB03897. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q03018 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: FBAFD33FF706C6BA

FASTA1,630187,447
        10         20         30         40         50         60 
MMVKQEEPLN EISPNTPMTS KSYLLNDTLS KVHHSGQTRP LTSVLSGDAS SNSIGILAMH 

        70         80         90        100        110        120 
NNIIRDFTKI ASNNIDLAIE DITTVDHSLN SIYSLLKSHH MWGHINSTVK QHLMIIVKLI 

       130        140        150        160        170        180 
NNNALGLASS EIIFLFNETN LFQAHSLKNI LLADFSTWND YYLSNLKILA LQIILKRKLV 

       190        200        210        220        230        240 
DEYLPHILEL FSHDKRYLLK DPNLKAHALT KIVLSFFSVT TSCKVLFGLK FLQYIKQFKL 

       250        260        270        280        290        300 
PFKKFISNIT VECFSKNLLH KNYLEMGPNK IYLNSFYLSY SMLYDGLDKI MLLDILSYEE 

       310        320        330        340        350        360 
TTEVQRAIKS KKEFNEYCNM SENRLLWSCI SVDDLNVILE NATNFLQNKG KHISATLKCL 

       370        380        390        400        410        420 
VCLWSTIRLE GLPKNKDILR QFDCTVIYIN SNIKSINDES AAALLSELLG VLSEICIDYK 

       430        440        450        460        470        480 
EPKRLSNIIS VLFNASVLFK SHSFLLKTAN LEISNVLISN DSKTSHRTIL KFEKFISSAQ 

       490        500        510        520        530        540 
SAQKKIEIFS CLFNVYCMLR NDTLSFVFDF CQNAFIHCFT RLKITKFIEF SNSSEIMLSV 

       550        560        570        580        590        600 
LYGNSSIENI PSENWSQLSR MIFCSLRGIF DLDPLELNNT FDKLHLLNKY ELLIRIVYLL 

       610        620        630        640        650        660 
NLDMSKHLTT NLSKITKLYI NKWLQKSDEK AERISSFEMD FVKMLLCYLN FNNFDKLSIE 

       670        680        690        700        710        720 
LSLCIKSKEK YYSSIVPYAD NYLLEAYLSL YMIDDALMMK NQLQKTMNLS TAKIEQALLH 

       730        740        750        760        770        780 
ASSLINVHLW DSDLTAFQIY FGKTLPAMKP ELFDINNDHN LPMSLYIKVI LLNIKIFNES 

       790        800        810        820        830        840 
AKLNIKAGNV ISAVIDCRKA QNLALSLLKK KNKLSQGSRL ALLKSLSFSF FQLIKIHIRI 

       850        860        870        880        890        900 
GSARDCEFYS KELSRIISDL EEPIIVYRCL HFLHRYYMIT EQTCLQNITL GKANKAFDYL 

       910        920        930        940        950        960 
DAEADITSLT MFLYDNKEFV KLEQSLVLYF GDQLEKTFLP NLWKLHLGKD IDDSICLSEY 

       970        980        990       1000       1010       1020 
MPKNVINRVH NMWQKVMSQL EEDPFFKGMF ESTLGIPSSL PVIPSTMPNN ILKTPSKHST 

      1030       1040       1050       1060       1070       1080 
GLKLCDSPRS SSMTPRGKNI RQKFDRIAAI SKLKQMKELL ESLKLDTLDN HELSKISSLS 

      1090       1100       1110       1120       1130       1140 
SLTLTILSNI TSIHNAESSL ITNFSLTDLP RHMPLLFDKV LNNIDNKNYR EFRVSSLIAP 

      1150       1160       1170       1180       1190       1200 
NNISTITESI RVSAAQKDLM ESNLNINVIT IDFCPITGNL LLSKLEPRRK RRTHLRLPLI 

      1210       1220       1230       1240       1250       1260 
RSNSRDLDEV HLSFPEATKK LLSIINESNQ TTSVEVTNKI KTREERKSWW TTRYDLDKRM 

      1270       1280       1290       1300       1310       1320 
QQLLNNIENS WFNGVQGFFS PEVVDNSLFE KFKDKFYEIL HQNLPSRKLY GNPAMFIKVE 

      1330       1340       1350       1360       1370       1380 
DWVIELFLKL NPQEIDFLSK MEDLIYFVLD ILLFHGEENA YDEIDFSMLH VQLEEQIKKY 

      1390       1400       1410       1420       1430       1440 
RATMTTNSIF HTFLVVSSSC HLFPWECLSF LKDLSITRVP SYVCLNKLLS RFHYQLPLQV 

      1450       1460       1470       1480       1490       1500 
TIEDNISMIL NPNGDLSRTE SKFKGMFQKI IDAKPSSQLV MNEKPEEETL LKMLQNSNLF 

      1510       1520       1530       1540       1550       1560 
VYIGHGGGEQ YVRSKEIKKC TKIAPSFLLG CSSAAMKYYG KLEPTGTIYT YLLGGCPMVL 

      1570       1580       1590       1600       1610       1620 
GNLWDVTDKD IDKFSEELFE KMGFRCNTDD LNGNSLSVSY AVSKSRGVCH LRYLNGAAPV 

      1630 
IYGLPIKFVS 

« Hide

References

« Hide 'large scale' references
[1]"Requirement for ESP1 in the nuclear division of Saccharomyces cerevisiae."
McGrew J.T., Goetsch L., Byers B.E., Baum P.
Mol. Biol. Cell 3:1443-1454(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-1630.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"An ESP1/PDS1 complex regulates loss of sister chromatid cohesion at the metaphase to anaphase transition in yeast."
Ciosk R., Zachariae W., Michaelis C., Shevchenko A., Mann M., Nasmyth K.
Cell 93:1067-1076(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PDS1.
[5]"Sister-chromatid separation at anaphase onset is promoted by cleavage of the cohesin subunit Scc1."
Uhlmann F., Lottspeich F., Nasmyth K.
Nature 400:37-42(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE OF MCD1, FUNCTION.
[6]"A novel role of the budding yeast separin Esp1 in anaphase spindle elongation: evidence that proper spindle association of Esp1 is regulated by Pds1."
Jensen S., Segal M., Clarke D.J., Reed S.I.
J. Cell Biol. 152:27-40(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 1568-ASP--ASP-1570.
[7]"Separase, polo kinase, the kinetochore protein Slk19, and Spo12 function in a network that controls Cdc14 localization during early anaphase."
Stegmeier F., Visintin R., Amon A.
Cell 108:207-220(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A COMPONENT OF THE FEAR NETWORK.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07289 Genomic DNA. Translation: AAB03897.1.
Z72883 Genomic DNA. Translation: CAA97101.1.
BK006941 Genomic DNA. Translation: DAA08191.1.
PIRS64403.
RefSeqNP_011612.3. NM_001181227.3.

3D structure databases

ProteinModelPortalQ03018.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33341. 35 interactions.
DIPDIP-2933N.
IntActQ03018. 7 interactions.
MINTMINT-614508.
STRING4932.YGR098C.

Protein family/group databases

MEROPSC50.001.

Proteomic databases

MaxQBQ03018.
PaxDbQ03018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR098C; YGR098C; YGR098C.
GeneID852990.
KEGGsce:YGR098C.

Organism-specific databases

CYGDYGR098c.
SGDS000003330. ESP1.

Phylogenomic databases

eggNOGCOG5155.
GeneTreeENSGT00390000004990.
HOGENOMHOG000065988.
KOK02365.
OMAFDILLFH.
OrthoDBEOG7V76G0.

Enzyme and pathway databases

BioCycYEAST:G3O-30808-MONOMER.

Gene expression databases

GenevestigatorQ03018.

Family and domain databases

InterProIPR005314. Peptidase_C50.
[Graphical view]
PANTHERPTHR12792. PTHR12792. 1 hit.
PfamPF03568. Peptidase_C50. 1 hit.
[Graphical view]
PROSITEPS51700. SEPARIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972815.
PROQ03018.

Entry information

Entry nameESP1_YEAST
AccessionPrimary (citable) accession number: Q03018
Secondary accession number(s): D6VUN0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries