ID   ESP1_ARATH              Reviewed;        2180 AA.
AC   Q5IBC5; F4JMQ3; O82745;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Separase;
DE            EC=3.4.22.49;
DE   AltName: Full=Protein EXTRA SPINDLE POLES;
DE            Short=AtESP;
DE   AltName: Full=Protein RADIALLY SWOLLEN 4;
GN   Name=ESP1; Synonyms=AESP, ESP, RSW4; OrderedLocusNames=At4g22970;
GN   ORFNames=F7H19.150;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=16582011; DOI=10.1105/tpc.105.036913;
RA   Liu Z., Makaroff C.A.;
RT   "Arabidopsis separase AESP is essential for embryo development and the
RT   release of cohesin during meiosis.";
RL   Plant Cell 18:1213-1225(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   FUNCTION.
RX   PubMed=19592426; DOI=10.1104/pp.109.140699;
RA   Yang X., Boateng K.A., Strittmatter L., Burgess R., Makaroff C.A.;
RT   "Arabidopsis separase functions beyond the removal of sister chromatid
RT   cohesion during meiosis.";
RL   Plant Physiol. 151:323-333(2009).
RN   [5]
RP   FUNCTION.
RX   PubMed=20150278; DOI=10.1242/dev.041939;
RA   Wu S., Scheible W.R., Schindelasch D., Van Den Daele H., De Veylder L.,
RA   Baskin T.I.;
RT   "A conditional mutation in Arabidopsis thaliana separase induces chromosome
RT   non-disjunction, aberrant morphogenesis and cyclin B1;1 stability.";
RL   Development 137:953-961(2010).
RN   [6]
RP   FUNCTION.
RX   PubMed=21559383; DOI=10.1371/journal.pone.0019459;
RA   Yang X., Boateng K.A., Yuan L., Wu S., Baskin T.I., Makaroff C.A.;
RT   "The radially swollen 4 separase mutation of Arabidopsis thaliana blocks
RT   chromosome disjunction and disrupts the radial microtubule system in
RT   meiocytes.";
RL   PLoS ONE 6:E19459-E19459(2011).
CC   -!- FUNCTION: Cleaves SYN1, releasing sister chromatid cohesion. Required
CC       for the release of cohesin at anaphase I and anaphase II, whereas the
CC       release of cohesin during diplotene and diakinesis occurs in a
CC       separase-independent process. Essential for embryo and endosperm
CC       development. May play a role in centromeric heterochromatin
CC       structure/formation during early meiosis, non-homologous centromere
CC       association and radial microtubule system (RMS) formation. May regulate
CC       the mitosis-specific cyclin CYCB1-1. {ECO:0000269|PubMed:16582011,
CC       ECO:0000269|PubMed:19592426, ECO:0000269|PubMed:20150278,
CC       ECO:0000269|PubMed:21559383}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5IBC5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5IBC5-2; Sequence=VSP_047934;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and buds.
CC       {ECO:0000269|PubMed:16582011}.
CC   -!- DISRUPTION PHENOTYPE: Embryo lethality. Embryos arrested at the
CC       globular stage, no cellularization of endosperm nuclei and enlargment
CC       of many nuclei and nucleoli resulting in a titan-like phenotype.
CC       {ECO:0000269|PubMed:16582011}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA19812.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79252.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY823256; AAW32909.1; -; mRNA.
DR   EMBL; AL031018; CAA19812.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161558; CAB79252.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84686.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84687.1; -; Genomic_DNA.
DR   PIR; T05128; T05128.
DR   RefSeq; NP_001190804.1; NM_001203875.2. [Q5IBC5-2]
DR   RefSeq; NP_194028.2; NM_118426.4. [Q5IBC5-1]
DR   AlphaFoldDB; Q5IBC5; -.
DR   SMR; Q5IBC5; -.
DR   BioGRID; 13685; 1.
DR   STRING; 3702.AT4G22970.1; -.
DR   MEROPS; C50.005; -.
DR   PaxDb; Q5IBC5; -.
DR   PRIDE; Q5IBC5; -.
DR   EnsemblPlants; AT4G22970.1; AT4G22970.1; AT4G22970. [Q5IBC5-1]
DR   EnsemblPlants; AT4G22970.2; AT4G22970.2; AT4G22970. [Q5IBC5-2]
DR   GeneID; 828396; -.
DR   Gramene; AT4G22970.1; AT4G22970.1; AT4G22970. [Q5IBC5-1]
DR   Gramene; AT4G22970.2; AT4G22970.2; AT4G22970. [Q5IBC5-2]
DR   KEGG; ath:AT4G22970; -.
DR   Araport; AT4G22970; -.
DR   TAIR; locus:2127238; AT4G22970.
DR   eggNOG; KOG1849; Eukaryota.
DR   InParanoid; Q5IBC5; -.
DR   OMA; IVANLWE; -.
DR   PhylomeDB; Q5IBC5; -.
DR   BRENDA; 3.4.22.49; 399.
DR   PRO; PR:Q5IBC5; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q5IBC5; baseline and differential.
DR   Genevisible; Q5IBC5; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IDA:TAIR.
DR   GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008233; F:peptidase activity; IMP:TAIR.
DR   GO; GO:0051304; P:chromosome separation; IMP:TAIR.
DR   GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0009960; P:endosperm development; IMP:TAIR.
DR   GO; GO:0006887; P:exocytosis; IMP:TAIR.
DR   GO; GO:0051307; P:meiotic chromosome separation; IMP:TAIR.
DR   GO; GO:0045876; P:positive regulation of sister chromatid cohesion; IMP:TAIR.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:TAIR.
DR   GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR   GO; GO:0016192; P:vesicle-mediated transport; IMP:TAIR.
DR   InterPro; IPR005314; Peptidase_C50.
DR   InterPro; IPR030397; SEPARIN_core_dom.
DR   PANTHER; PTHR12792; PTHR12792; 1.
DR   PROSITE; PS51700; SEPARIN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell cycle; Cell division; Chromosome partition;
KW   Hydrolase; Meiosis; Mitosis; Reference proteome.
FT   CHAIN           1..2180
FT                   /note="Separase"
FT                   /id="PRO_0000423514"
FT   DOMAIN          1937..2031
FT                   /note="Peptidase C50"
FT   REGION          1252..1283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2101..2125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1670..1672
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047934"
SQ   SEQUENCE   2180 AA;  244847 MW;  BF8E09DA382A9725 CRC64;
     MASSGDDLRL LSLIDVGDNV FSSFSDYLKP FSTLSTSRKK QDRATTIRAL AKQFLPFLNK
     SISLLPKRLS VANSDKEARE SALDLFRAYE LCLDCLELVS AQLACKPHTV QSQRLRMIHC
     LDVWGLYENV YTEAFKVLEK LRGSDSKSRK SRLLPEVQDG DAEMALVVVD AVAAIFRAVA
     MSQQLDDKRY RKVLLLLEEV GGWLRVLDAK VYEKLHRAMV TSMGKCAVSL VREAERFNGD
     LVISFCDLTV KEHYKSALSK DRVYKFAREV LSVLFGFKDR KMSVTIDISM SVLRSLSCQF
     EDESNENLME FFDLVDYCAH KFRAAGDMYC AKVSKKLNEM AAIFVEAIPQ LNLVLRLYST
     GLSITVCNSK LGEIKLEDST DDWKIQAMFD DDARWQSLVS LLGMVDSYSG DEGNQTGSSS
     IGGHRNYNNK THDSCKDRNK ITCWPQYVDA LKFLCQPLAD FIYSVKRKIV LETEMSCASA
     HLITIHDAFL QFCDGCLFLQ RCTSDKGDRE IANNKAFLNA AMGAFIVSLR TQLKLEISAH
     LVEDVIGSPW IQSQELKYLI ATLYNIGIVL YRNKELNKAC EALKLCSKVS WRCVELHCHM
     FVNQSSSSDN DLSEDAIMDF VGEACNRCAF YLDILQKCSR RKIRQNIVHI LENWLSAEHL
     IRRLPGPEAI VKQWVKIERE CHTDLDAAGS CTTLYSLLSS SQKKSKRGIG KILEQELLAY
     DRVLPLRSNL GQQTRIKIAD ILLKDVYVTE DMHIERARIL IWKARMTRTS GTEHITECIC
     FLSEAISILG ELHHGPNEEG SPSSHMLPIA YCLRAFCTQE ADPNSKKVFQ DISTSLNLWL
     RILSLDDSGD SLPTENIIPL LYNMIDLMSV KGCTELHHHI YQLIFRLFKW KNVKLEVCLA
     MLWECRRLSH ALCPSPISDA FIQTLSENCA DKSTCIDFWM DCLKDSKAKL IGFQQNFHDL
     HNKDEGPFQS DITIDDIKDA ASELISSASL SGNSSFAAAY LYYDLCERLI SFGKLSEALS
     YAKEAYRIRT LIFQDKFKYT AEKHIEKHNE DGKISEIRTF SIKNFQVYRL LATDFWPCGN
     FLWDINRCYL SPWSVLQCYL ESTLQVGILN ELIGNGLEAE TILSWGKAFS CSQSLFPFVV
     AFSSALGNLY HKKQCLDLAE KELQNAKEIL IANQRDFSCV KCKLKLEVTL DKQLGDISRK
     QIDRVSQTDG FLHAESLFSA ALGKFCCSAW KSCIRSHGEE IAEEIVIDRN GGEGLGHNSS
     KTKLSIKEPP GNRGSRRGGR ANKTCLSKDQ DLISEPTSRL TRSMRHSLRE QCQNRSNVPE
     VVSKKPNLCD RSVGSRGERV LLDTSNALPG FCICYKEKRQ QCLSEEVTES GSLNNLVSLK
     WELCHRKLAS SILVSLGKCL GDSGRIHLAH EALLHSISVL FKSTWSSHNQ PSVSQLLEFI
     GKEVTRDVFA VDRAIILYNL CWLNLRNYHC RKSRSICCDL FHIPFTKLVS WLMLAFVLSG
     EVPILFQKVS RLLASLYLLS SSNSEFTFES DGNELSASHW VSFFHQASLG THLSYHFISN
     LSQKHKSQCL SDKECTEATC SSCMVPEDLD LPRLAPDRTQ DLVQFAKEFF INLPSSTIIC
     ISLLGGALNQ LLQELMHIRS PVCAWVLISR LNPESQPVAT LLPVDSIVED MSDDSANLSS
     TEATQVKSLK GPWLCPWGTT VVDEVAPAFK SILEESHSSS STTEEDTIES RGLWWKKRKK
     LNHRLGIFLR NLEASWLGPW RCLLLGEWSN YKLPDSAQKK LVNDLKSKCK MEVNEMLLKV
     ILGGGTDNFK GEACVAQLSL RNGCYVGRGG YLYEEDSCKT PTAASNISES RHELALKLIH
     DAASKLGQQD GHENREPIIL VLDPEVQMLP WENIPILRKQ EVYRMPSVGC ISAVLKKRSL
     QGEPAKSHVA SFPLIDPLDS FYLLNPGGDL TDTQVTFESW FRDQNFEGKA GSEPSAIELT
     EALETHDLFL YFGHGSGAQY IPRREIEKLD NCSATFLMGC SSGSLWLKGC YIPQGVPLSY
     LLGGSPAIVA TLWDVTDRDI DRFGKALLEA WLQERSDSSS EGGCSQCESL ANDLAAMTLK
     GTKRSRKPSS RNKPAQSDVD GSGKIECNHK HRRKIGSFIA AARDACNLQY LIGAAPVCYG
     VPTGITRKKG IDALLPSSSR