SECU_YEAST
ID SECU_YEAST Reviewed; 373 AA.
AC P40316; D6VS98;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Securin;
GN Name=PDS1; OrderedLocusNames=YDR113C; ORFNames=YD9727.08C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204626 / S288c / A364A;
RX PubMed=8601617; DOI=10.1083/jcb.133.1.99;
RA Yamamoto A., Guacci V., Koshland D.;
RT "Pds1p, an inhibitor of anaphase in budding yeast, plays a critical role in
RT the APC and checkpoint pathway(s).";
RL J. Cell Biol. 133:99-110(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP UBIQUITINATION, AND MUTAGENESIS OF 85-ARG--LEU-88.
RX PubMed=8985178; DOI=10.1101/gad.10.24.3081;
RA Cohen-Fix O., Peters J.M., Kirschner M.W., Koshland D.;
RT "Anaphase initiation in Saccharomyces cerevisiae is controlled by the APC-
RT dependent degradation of the anaphase inhibitor Pds1p.";
RL Genes Dev. 10:3081-3093(1996).
RN [6]
RP FUNCTION, AND INTERACTION WITH ESP1.
RX PubMed=9635435; DOI=10.1016/s0092-8674(00)81211-8;
RA Ciosk R., Zachariae W., Michaelis C., Shevchenko A., Mann M., Nasmyth K.;
RT "An ESP1/PDS1 complex regulates loss of sister chromatid cohesion at the
RT metaphase to anaphase transition in yeast.";
RL Cell 93:1067-1076(1998).
RN [7]
RP INTERACTION WITH CDC20.
RX PubMed=11553328; DOI=10.1016/s0960-9822(01)00399-2;
RA Hilioti Z., Chung Y.-S., Mochizuki Y., Hardy C.F.J., Cohen-Fix O.;
RT "The anaphase inhibitor Pds1 binds to the APC/C-associated protein Cdc20 in
RT a destruction box-dependent manner.";
RL Curr. Biol. 11:1347-1352(2001).
RN [8]
RP PHOSPHORYLATION AT SER-277 AND SER-292 BY CDC28, AND MUTAGENESIS OF
RP SER-277; SER-292 AND THR-304.
RX PubMed=12050115; DOI=10.1101/gad.971402;
RA Agarwal R., Cohen-Fix O.;
RT "Phosphorylation of the mitotic regulator Pds1/securin by Cdc28 is required
RT for efficient nuclear localization of Esp1/separase.";
RL Genes Dev. 16:1371-1382(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; SER-186; SER-212 AND
RP SER-213, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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/ESP1 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 ESP1.
CC {ECO:0000269|PubMed:9635435}.
CC -!- SUBUNIT: Interacts with the caspase-like ESP1, and prevents its
CC protease activity probably by covering its active site. Interacts with
CC CDC20. {ECO:0000269|PubMed:11553328, ECO:0000269|PubMed:9635435}.
CC -!- INTERACTION:
CC P40316; Q03018: ESP1; NbExp=2; IntAct=EBI-16908, EBI-6657;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- DOMAIN: The N-terminal destruction box (D-box) acts as a recognition
CC signal for degradation via the ubiquitin-proteasome pathway.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDC28. The phosphorylation may be important for
CC ESP1 localization to the nucleus. {ECO:0000269|PubMed:12050115}.
CC -!- PTM: Ubiquitinated by the anaphase promoting complex (APC) at the onset
CC of anaphase, conducting to its degradation.
CC {ECO:0000269|PubMed:8985178}.
CC -!- SIMILARITY: Belongs to the securin family. {ECO:0000305}.
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DR EMBL; U12185; AAB00106.1; -; Genomic_DNA.
DR EMBL; Z48758; CAA88666.1; -; Genomic_DNA.
DR EMBL; AY558573; AAS56899.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11958.1; -; Genomic_DNA.
DR PIR; S47911; S47911.
DR RefSeq; NP_010398.3; NM_001180421.3.
DR PDB; 5U1S; X-ray; 3.00 A; B=258-373.
DR PDB; 5U1T; X-ray; 2.60 A; B=258-373.
DR PDBsum; 5U1S; -.
DR PDBsum; 5U1T; -.
DR AlphaFoldDB; P40316; -.
DR SMR; P40316; -.
DR BioGRID; 32170; 223.
DR ComplexPortal; CPX-1340; Separase-Securin complex.
DR DIP; DIP-2798N; -.
DR IntAct; P40316; 13.
DR MINT; P40316; -.
DR STRING; 4932.YDR113C; -.
DR iPTMnet; P40316; -.
DR MaxQB; P40316; -.
DR PaxDb; P40316; -.
DR PRIDE; P40316; -.
DR EnsemblFungi; YDR113C_mRNA; YDR113C; YDR113C.
DR GeneID; 851691; -.
DR KEGG; sce:YDR113C; -.
DR SGD; S000002520; PDS1.
DR VEuPathDB; FungiDB:YDR113C; -.
DR eggNOG; ENOG502S4FI; Eukaryota.
DR HOGENOM; CLU_079150_0_0_1; -.
DR InParanoid; P40316; -.
DR OMA; DCESANE; -.
DR BioCyc; YEAST:G3O-29713-MON; -.
DR PRO; PR:P40316; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P40316; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:1990520; C:separase-securin complex; IPI:ComplexPortal.
DR GO; GO:0005819; C:spindle; IDA:SGD.
DR GO; GO:0019899; F:enzyme binding; IPI:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IGI:SGD.
DR GO; GO:0007127; P:meiosis I; IMP:SGD.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD.
DR GO; GO:0001100; P:negative regulation of exit from mitosis; IMP:SGD.
DR GO; GO:1902104; P:positive regulation of metaphase/anaphase transition of meiotic cell cycle; IDA:ComplexPortal.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
DR GO; GO:0000725; P:recombinational repair; IMP:SGD.
DR DisProt; DP00256; -.
DR InterPro; IPR006940; Securin_separation_inhibitor.
DR Pfam; PF04856; Securin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..373
FT /note="Securin"
FT /id="PRO_0000206366"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 85..88
FT /note="D-box"
FT COMPBIAS 10..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:12050115,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 292
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000305|PubMed:12050115"
FT MUTAGEN 85..88
FT /note="RLPL->ALPA: Abolishes ubiquitination and subsequent
FT degradation."
FT /evidence="ECO:0000269|PubMed:8985178"
FT MUTAGEN 277
FT /note="S->A: Affects phosphorylation and the interaction
FT with ESP1."
FT /evidence="ECO:0000269|PubMed:12050115"
FT MUTAGEN 292
FT /note="S->A: Affects phosphorylation and the interaction
FT with ESP1."
FT /evidence="ECO:0000269|PubMed:12050115"
FT MUTAGEN 304
FT /note="T->A: No effect."
FT /evidence="ECO:0000269|PubMed:12050115"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 281..288
FT /evidence="ECO:0007829|PDB:5U1T"
FT HELIX 365..371
FT /evidence="ECO:0007829|PDB:5U1T"
SQ SEQUENCE 373 AA; 41838 MW; 7B31777C539433F4 CRC64;
MMPANEDKEN NIVYTGNESS GINFPQTPAH LLKRSHSNIL KPPVRLDQLK RDANSNNGNT
LKYIQGGKEV SPTKRLHTHA QQQGRLPLAA KDNNRSKSFI FPETSNQSKD ADLPQLQNTL
SIRKNDQLRK LSQISRSRSR ANHNDLLSNS RKLQKYGSVL GYNALPKMKS LVLKDLADSG
KNEESSDDDE GNEDSESKLG KKLQSALLKQ DSSDGENELN GGLGLFNEQG GLQQLIKNST
KNEQKTKNDK SDKTDDYDIE IAPQRQEPLP YVPEGYSPFQ QDDIEKLKTF NSPYKLDLED
EDDTPDKVDL LPLEQIDEEG EKDETECITR NQEEGAALPL LSKNFKEVAA VPTMELVYSE
EGLDPEELED LVT
