CUT1_SCHPO
ID CUT1_SCHPO Reviewed; 1828 AA.
AC P18296; O94304;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Separin;
DE EC=3.4.22.49;
DE AltName: Full=Cell untimely torn protein 1;
DE AltName: Full=Separase;
GN Name=cut1; ORFNames=SPCC5E4.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX 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 and
RT has homology to the budding yeast ESP1 gene.";
RL Cell 62:913-925(1990).
RN [2]
RP SEQUENCE REVISION, INTERACTION WITH CUT2, AND MUTAGENESIS OF ALA-1816.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8978688; DOI=10.1002/j.1460-2075.1996.tb01052.x;
RA Funabiki H., Kumada K., Yanagida M.;
RT "Fission yeast Cut1 and Cut2 are essential for sister chromatid separation,
RT concentrate along the metaphase spindle and form large complexes.";
RL EMBO J. 15:6617-6628(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX 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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA 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 PubMed=12390246; DOI=10.1046/j.1365-2443.2002.00586.x;
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).
CC -!- FUNCTION: Caspase-like protease, which plays a central role in the
CC chromosome segregation by cleaving the rad21 subunit of the cohesin
CC complex at the onset of anaphase. During most of the cell cycle, it is
CC inactivated by securin/cut2 protein. It is also required for pointed
CC nuclear formation. {ECO:0000269|PubMed:12390246}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=All bonds known to be hydrolyzed by this endopeptidase have
CC arginine in P1 and an acidic residue in P4. P6 is often occupied by
CC an acidic residue or by a hydroxy-amino-acid residue, the
CC phosphorylation of which enhances cleavage.; EC=3.4.22.49;
CC -!- ACTIVITY REGULATION: It is inactivated via its interaction with cut2,
CC which probably covers its active site. Cut2 degradation at anaphase,
CC liberates it and triggers rad21 cleavage.
CC -!- SUBUNIT: Interacts with cut2. Interacts with rad21.
CC {ECO:0000269|PubMed:8978688}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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DR EMBL; M36179; AAB06192.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA21959.1; -; Genomic_DNA.
DR PIR; A35694; A35694.
DR PIR; T41455; T41455.
DR RefSeq; NP_587903.1; NM_001022895.2.
DR AlphaFoldDB; P18296; -.
DR SMR; P18296; -.
DR BioGRID; 276005; 54.
DR DIP; DIP-84N; -.
DR ELM; P18296; -.
DR STRING; 4896.SPCC5E4.04.1; -.
DR iPTMnet; P18296; -.
DR MaxQB; P18296; -.
DR PaxDb; P18296; -.
DR EnsemblFungi; SPCC5E4.04.1; SPCC5E4.04.1:pep; SPCC5E4.04.
DR GeneID; 2539442; -.
DR KEGG; spo:SPCC5E4.04; -.
DR PomBase; SPCC5E4.04; cut1.
DR VEuPathDB; FungiDB:SPCC5E4.04; -.
DR eggNOG; KOG1849; Eukaryota.
DR HOGENOM; CLU_237201_0_0_1; -.
DR InParanoid; P18296; -.
DR OMA; IYEHMGQ; -.
DR PhylomeDB; P18296; -.
DR BRENDA; 3.4.22.49; 5613.
DR Reactome; R-SPO-2467813; Separation of Sister Chromatids.
DR PRO; PR:P18296; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990520; C:separase-securin complex; IDA:PomBase.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IMP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:PomBase.
DR GO; GO:0051307; P:meiotic chromosome separation; IMP:PomBase.
DR GO; GO:0140013; P:meiotic nuclear division; IMP:PomBase.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IMP:PomBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR005314; Peptidase_C50.
DR InterPro; IPR030397; SEPARIN_core_dom.
DR PANTHER; PTHR12792; PTHR12792; 1.
DR PROSITE; PS51700; SEPARIN; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome partition; Cytoplasm; Hydrolase;
KW Nucleus; Protease; Reference proteome; Thiol protease.
FT CHAIN 1..1828
FT /note="Separin"
FT /id="PRO_0000205903"
FT DOMAIN 1647..1741
FT /note="Peptidase C50"
FT ACT_SITE 1730
FT MUTAGEN 1767
FT /note="D->A: Affects the formation of the pointed nucleus;
FT when associated with V-1779."
FT /evidence="ECO:0000269|PubMed:12390246"
FT MUTAGEN 1779
FT /note="E->V: Affects the formation of the pointed nucleus;
FT when associated with A-1767."
FT /evidence="ECO:0000269|PubMed:12390246"
FT MUTAGEN 1816
FT /note="A->T: In cut1-T693; reduced function; when
FT transferred at 33 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:12390246,
FT ECO:0000269|PubMed:8978688"
FT CONFLICT 430..437
FT /note="LFVENALP -> PLSKMLDR (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1125
FT /note="T -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1131
FT /note="N -> Y (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1828 AA; 209434 MW; B6216CA28DA7CAE1 CRC64;
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
