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Description:
Separin (EC 3.4.22.49) (Separase) (Cell untimely torn protein 1).
Molecular weight: 2094
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
double-strand break repair( GO:0006302 )
Important dates:
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
14-AUG-2001, sequence version 3.
07-FEB-2006, entry version 53.
Phylogenetic order:
Eukaryota Fungi Ascomycota Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein CUT1_SCHPO:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | M36179 | AAB06192.1 | - |
| EMBL | AL033406 | CAA21959.1 | - |
| PIR | A35694 | A35694. | |
| PIR | T41455 | T41455. | |
| MEROPS | C50.001 | -. | |
| GeneDB_Spombe | SPCC5E4.04 | -.1 | |
| BioCyc | SPOM-XXX-01:SPOM-XXX-01-002244-MONOMER | -.1 | |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0006302 | P:double-strand break repair | IGI. |
| GO | GO:0045143 | P:homologous chromosome segregation | IMP. |
| GO | GO:0000090 | P:mitotic anaphase | IMP. |
| GO | GO:0051306 | P:mitotic chromosome separation | IGI. |
| GO | GO:0006508 | P:proteolysis and peptidolysis | TAS. |
| InterPro | IPR005314 | Peptidase_C50. | |
| InterPro | IPR011990 | TPR-like_helical. | |
| PANTHER | PTHR12792 | Peptidase_C50.1 | 1. |
| Pfam | PF03568 | Peptidase_C50 | 1. |
Keywords:
Cell cycle; Cell division; Chromosome partition; Complete proteome; Hydrolase; Nuclear protein; Protease; Thiol protease.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972;
RX MEDLINE=90367123; PubMed=2203537; DOI=10.1016/0092-8674(90)90266-H;
RA Uzawa S., Samejima I., Hirano T., Tanaka K., Yanagida M.;
RT "The fission yeast cut1+ gene regulates spindle pole body duplication
RT and has homology to the budding yeast ESP1 gene.";
RL Cell 62:913-925(1990).
RN [2]
RP SEQUENCE REVISION, INTERACTION WITH CUT2, AND MUTANT CUT1-T693.
RC STRAIN=972;
RX MEDLINE=97133291; PubMed=8978688;
RA Funabiki H., Kumada K., Yanagida M.;
RT "Fission yeast Cut1 and Cut2 are essential for sister chromatid
RT separation, concentrate along the metaphase spindle and form large
RT complexes.";
RL EMBO J. 15:6617-6628(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972;
RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF ASP-1767; GLU-1779 AND ALA-1816.
RX MEDLINE=22278392; PubMed=12390246;
RA Nakamura T., Nagao K., Nakaseko Y., Yanagida M.;
RT "Cut1/separase C-terminus affects spindle pole body positioning in
RT interphase of fission yeast: pointed nuclear formation.";
RL Genes Cells 7:1113-1124(2002).
Feature:
CHAIN 1 1828 Separin.
/FTId=PRO_0000205903.
ACT_SITE 1730 1730
MUTAGEN 1767 1767 D->A: Affects the formation of the
pointed nucleus; when associated with V-
1779.
MUTAGEN 1779 1779 E->V: Affects the formation of the
pointed nucleus; when associated with A-
1767.
MUTAGEN 1816 1816 A->T: In cut1-T693; reduced function;
when transferred at 33 degrees Celsius.
CONFLICT 430 437 LFVENALP -> PLSKMLDR (in Ref. 1 and 2).
CONFLICT 1125 1125 T -> S (in Ref. 1 and 2).
CONFLICT 1131 1131 N -> Y (in Ref. 1 and 2).
Comments:
-!- FUNCTION: Caspase-like protease, which plays a central role in the
chromosome segregation by cleaving the rad21 subunit of the
cohesin complex at the onset of anaphase. During most of the cell
cycle, it is inactivated by securin/cut2 protein. It is also
required for pointed nuclear formation.
-!- 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 an hydroxy-amino-acid
residue, the phosphorylation of which enhances cleavage.
-!- ENZYME REGULATION: It is inactivated via its interaction with
cut2, which probably covers its active site. Cut2 degradation at
anaphase, liberates it and triggers rad21 cleavage.
-!- SUBUNIT: Interacts with cut2. Interacts with rad21.
-!- SUBCELLULAR LOCATION: Nuclear and cytoplasmic.
-!- SIMILARITY: Belongs to the peptidase C50 family.
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Sequence length: 1828
MSTRSIVTSK VSWTPEKFIS ALSYPEHCSI TLVKRLKASV KLKDLKQNIS RDAPSWTFEH
LFVAFKCAVS NLAKQWAELS TTDKEKTRRM FCTPSRLNTA HRPEVFYLLE CCTYILEQMQ
VVTKNTSHLY DCIRSGVSIC NRLLDMEIFE PAISLLMKTH KNLIILLTYR DHDAIPTATL
LNPTLDVSEI QLESCLFVPM VPASYFLNIG TIVVTFQLNV LRCLSLSQIN GLSLNTINNL
QSEDGPFQWI ERSFPSQVQL ANSRREILAR LLTRFSMIQN NALQSFKLLI LSIALWLNIL
SSQRADDKEF DVNQLETRIL QLFSKVVQLC KSEDIEGSIL NKDMTQLHHL LENLSKESRL
HILLQLSQLY YKYNDFQLSA AYVIRGYSLS FEDISFKLKF LLFSFRLSIH DNSICFPFNL
IQELSSLQQL FVENALPYSE ALHLLDSIER SFRLFNDSTV FDDTVFALNI SEILSWILSS
VVRDILVEDE LLNLQLKIRK FLMFTFHIIR SFSELTKFQS SLEGCLNLAA YYEDAEFPQK
LSNHLYNLCV KSSNVNYARE CISLSIKIAV SHKLTNDETY LLKILKNFQL RYHDSLQLQE
KCDVLHTTFN QLDLYVGTTS VGKSSVLDNI LKRIFNSLTS INDSNIEKLL ESISYSLLKL
FFKCANEGSR YNASAALSFK LSLMLHEKEE VLLLKTNVSC VLANHGYNDI KFEEMVLCVI
KGDQNLLEHN SNNNAKLALN ESLLCSWENL LCYRRAEDDS RILTIIESWT IFISRFSSVI
SRCSFTDFEI NSILNFFFCF LHTVEPSGKL TFELAFLEIF YELFNCLLHL QFSKYLVIIG
TLLSDKYMTL GFSGKAHLFY TKCYSYLRQC KSSPFINFWN VSYGKYLILT GNTDKGILQL
KKYSLSSEED FNSNGLSRTV SLNLLLYERI QLSDALFQLG YTTVSLGFIM QNLKVIKGLF
SKSSKEHFNG GKYITWRLFA VSAHSNVCAA RIYEHMGQAR EAEFFYRQAC SISEKMPFSC
FSATFQLRLC SLLTRAGKLE KGEKILFDLT EAMKSTDTYH KLLWNYGAAE VCATKSELDG
AICHYSECVK LLEIIKSEYY LFFNRNREKS LTKGIKRLSL SSQPTFVTES NTTEFDDWSI
LQNTAANLLR LISMFELKRG NLEIAKALMT DSTKCSIASF FNIVSANILK SKLIVCEADS
TLFGDPVLRT LPDSVISLPG ISHKFQKNQS KTKALGENTG FRKGSKRLDY LRERLKINLQ
NVRLSCEIIF SNAYERSSVC VCREVNELIS YSTIMQSALT TIGETTDVDS SSASFFLEIP
KALGFHRRRE AQKFRNQHKE LHFSSLEQIL NSRLSIPDVR TFQDNFIDSL PSIWNVVSIT
INNSGEDLFI SKIRKGHSPL IFRLPLQRHN SRDADEEILV FTKAQTELFR IISKSNQMAQ
NGKHYTRRED KETWWKERRH LDQCLQQLLE NIEISWLGGF KGIFNPHKID TSLFAKFSSQ
FQNIIAKNFN MDKKTPVPTL SPEILELFIT LGKPGYEGYE QLLEDLIYFI LDIFQFRGLH
FAYDEIDTDQ LSMDLQDALN AYFNNYVSEE NRSHTVLVLD KSVHQFPWES LPCLNRQSVS
RVPSLSILRD ILSQSFVVNG EYVEVRKEAG SYILNPSLDL KHTQEMFEHK LVEGGWKGLI
ASQPSNRDFI KMLSGNDFFL YFGHGGGEQY TTSYDLATLK RCAVTILMGC SSGALYECGS
FEPWGTPLDY LSAGCPTLVA NLWDVTDKDI DRFSLKMLES WGLFENKAPF VNSTSICTAV
SESRSCCHLR YLNGAAPVIY GIPAYIIP