SECU_SCHPO
ID SECU_SCHPO Reviewed; 301 AA.
AC P21135; Q9UUM0;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Securin;
DE AltName: Full=Cell untimely torn protein 2;
DE Short=Protein Cut2;
GN Name=cut2; ORFNames=SPBC14C8.01c, SPBC1815.02c;
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 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 [3]
RP FUNCTION.
RX PubMed=8632802; DOI=10.1038/381438a0;
RA Funabiki H., Yamano H., Kumada K., Nagao K., Hunt T., Yanagida M.;
RT "Cut2 proteolysis required for sister-chromatid seperation in fission
RT yeast.";
RL Nature 381:438-441(1996).
RN [4]
RP FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF 33-ARG--LEU-36 AND
RP 52-ARG--LEU-55.
RX PubMed=9312055; DOI=10.1093/emboj/16.19.5977;
RA Funabiki H., Yamano H., Nagao K., Tanaka H., Yasuda H., Hunt T.,
RA Yanagida M.;
RT "Fission yeast Cut2 required for anaphase has two destruction boxes.";
RL EMBO J. 16:5977-5987(1997).
CC -!- FUNCTION: Regulatory protein, which plays a central role in chromosome
CC stability. Probably acts by blocking the action of key proteins. During
CC the mitosis, it blocks separase/cut1 function, preventing the
CC proteolysis of the cohesin complex and the subsequent segregation of
CC the chromosomes. At the onset of anaphase, it is ubiquitinated,
CC conducting to its destruction and to the liberation of cut1.
CC {ECO:0000269|PubMed:8632802, ECO:0000269|PubMed:9312055}.
CC -!- SUBUNIT: Interacts with the caspase-like cut1, and prevents its
CC protease activity probably by covering its active site.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- DOMAIN: The N-terminal destruction boxes (D-box 1 and D-box 2) act as a
CC recognition signal for degradation via the ubiquitin-proteasome
CC pathway. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by the anaphase promoting complex (APC) at the onset
CC of anaphase, conducting to its degradation.
CC {ECO:0000269|PubMed:9312055}.
CC -!- SIMILARITY: Belongs to the securin family. {ECO:0000305}.
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DR EMBL; M57750; AAA35299.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB43487.1; -; Genomic_DNA.
DR PIR; B35694; B35694.
DR RefSeq; NP_595904.2; NM_001021811.3.
DR AlphaFoldDB; P21135; -.
DR BioGRID; 276196; 58.
DR DIP; DIP-317N; -.
DR STRING; 4896.SPBC14C8.01c.1; -.
DR iPTMnet; P21135; -.
DR MaxQB; P21135; -.
DR PaxDb; P21135; -.
DR EnsemblFungi; SPBC14C8.01c.1; SPBC14C8.01c.1:pep; SPBC14C8.01c.
DR GeneID; 2539641; -.
DR KEGG; spo:SPBC14C8.01c; -.
DR PomBase; SPBC14C8.01c; cut2.
DR VEuPathDB; FungiDB:SPBC14C8.01c; -.
DR HOGENOM; CLU_924889_0_0_1; -.
DR OMA; DLEYMPP; -.
DR Reactome; R-SPO-2467813; Separation of Sister Chromatids.
DR PRO; PR:P21135; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0072687; C:meiotic spindle; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:1990520; C:separase-securin complex; IDA:PomBase.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; TAS: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:0051276; P:chromosome organization; IEA:InterPro.
DR GO; GO:0045143; P:homologous chromosome segregation; IBA:GO_Central.
DR GO; GO:0140013; P:meiotic nuclear division; IMP:PomBase.
DR GO; GO:2000816; P:negative regulation of mitotic sister chromatid separation; IMP:PomBase.
DR InterPro; IPR006940; Securin_separation_inhibitor.
DR PANTHER; PTHR10418; PTHR10418; 1.
DR Pfam; PF04856; Securin; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome partition; Cytoplasm; Mitosis;
KW Nucleus; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..301
FT /note="Securin"
FT /id="PRO_0000206365"
FT REPEAT 250..260
FT REPEAT 270..280
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 33..36
FT /note="D-box 1"
FT MOTIF 52..55
FT /note="D-box 2"
FT COMPBIAS 35..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 33..36
FT /note="RAPL->AAPA: Abolishes ubiquitination at first D-box
FT site. Abolishes ubiquitination and subsequent degradation;
FT when associated with A-52 and A-55."
FT /evidence="ECO:0000269|PubMed:9312055"
FT MUTAGEN 52..55
FT /note="RTVL->ATVA: Abolishes ubiquitination at second D-box
FT site. Abolishes ubiquitination and subsequent degradation;
FT when associated with A-33 and A-36."
FT /evidence="ECO:0000269|PubMed:9312055"
SQ SEQUENCE 301 AA; 32854 MW; 98158315C7C07E3D CRC64;
MLPRTMFSYG KENAFPVTPI SNRNGTKGAG SKRAPLGSTK QSNAPSSVTV PRTVLGGKST
NISKFISAPS TKKMSPMDIS MDSPTILEPN SQGISRSAVQ ERSKRLSASP RRSSLTDTPL
PNELEEDIEY MPPPVHLDPI QSLGFDDVAI DCETLDPWPS MQNKATSVTI RNTPASDFHV
YKEFSDDDPI QFPLLSVDGD SPLTEKDTNL TTPATLKASD QQRKVLEKPS VSKQSSSRTR
LSTVYRTKLA SGKSIPRPLS HKLTRPRVTA SGNSRRRPLS RSIHSLSSSR IDFSSLDTGL
L
