FLP1_SCHPO
ID FLP1_SCHPO Reviewed; 537 AA.
AC Q9P7H1;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Tyrosine-protein phosphatase CDC14 homolog;
DE EC=3.1.3.48;
DE AltName: Full=CDC fourteen-like phosphatase 1;
GN Name=clp1; Synonyms=flp1; ORFNames=SPAC1782.09c;
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 [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 [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11448769; DOI=10.1016/s0960-9822(01)00268-8;
RA Trautmann S., Wolfe B.A., Jorgensen P., Tyers M., Gould K.L., McCollum D.;
RT "Fission yeast Clp1p phosphatase regulates G2/M transition and coordination
RT of cytokinesis with cell cycle progression.";
RL Curr. Biol. 11:931-940(2001).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=11683392; DOI=10.1242/jcs.114.14.2649;
RA Cueille N., Salimova E., Esteban V., Blanco M., Moreno S., Bueno A.,
RA Simanis V.;
RT "Flp1, a fission yeast orthologue of the s. cerevisiae CDC14 gene, is not
RT required for cyclin degradation or rum1p stabilisation at the end of
RT mitosis.";
RL J. Cell Sci. 114:2649-2664(2001).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARK1.
RX PubMed=15525536; DOI=10.1016/j.devcel.2004.10.006;
RA Trautmann S., Rajagopalan S., McCollum D.;
RT "The S. pombe Cdc14-like phosphatase Clp1p regulates chromosome
RT biorientation and interacts with Aurora kinase.";
RL Dev. Cell 7:755-762(2004).
RN [5]
RP FUNCTION IN DEPHOSPHORYLATION OF CDC25, AND INTERACTION WITH CDC25.
RX PubMed=15128870; DOI=10.1242/jcs.01107;
RA Esteban V., Blanco M., Cueille N., Simanis V., Moreno S., Bueno A.;
RT "A role for the Cdc14-family phosphatase Flp1p at the end of the cell cycle
RT in controlling the rapid degradation of the mitotic inducer Cdc25p in
RT fission yeast.";
RL J. Cell Sci. 117:2461-2468(2004).
RN [6]
RP FUNCTION.
RX PubMed=15265986; DOI=10.1242/jcs.01244;
RA Mishra M., Karagiannis J., Trautmann S., Wang H., McCollum D.,
RA Balasubramanian M.K.;
RT "The Clp1p/Flp1p phosphatase ensures completion of cytokinesis in response
RT to minor perturbation of the cell division machinery in Schizosaccharomyces
RT pombe.";
RL J. Cell Sci. 117:3897-3910(2004).
RN [7]
RP INTERACTION WITH RAD24, AND SUBCELLULAR LOCATION.
RX PubMed=16085489; DOI=10.1016/j.cub.2005.06.070;
RA Mishra M., Karagiannis J., Sevugan M., Singh P., Balasubramanian M.K.;
RT "The 14-3-3 protein rad24p modulates function of the cdc14p family
RT phosphatase clp1p/flp1p in fission yeast.";
RL Curr. Biol. 15:1376-1383(2005).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16085490; DOI=10.1016/j.cub.2005.06.039;
RA Trautmann S., McCollum D.;
RT "Distinct nuclear and cytoplasmic functions of the S. pombe Cdc14-like
RT phosphatase Clp1p/Flp1p and a role for nuclear shuttling in its
RT regulation.";
RL Curr. Biol. 15:1384-1389(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-453; SER-468; SER-470 AND
RP SER-513, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [10]
RP FUNCTION IN DEPHOSPHORYLATION OF ASE1, AND MUTAGENESIS OF CYS-286.
RX PubMed=17562791; DOI=10.1083/jcb.200702145;
RA Khmelinskii A., Lawrence C., Roostalu J., Schiebel E.;
RT "Cdc14-regulated midzone assembly controls anaphase B.";
RL J. Cell Biol. 177:981-993(2007).
RN [11]
RP INTERACTION WITH MID1, SUBCELLULAR LOCATION, AND FUNCTION IN
RP DEPHOSPHORYLATION OF CDC15.
RX PubMed=18378776; DOI=10.1083/jcb.200709060;
RA Clifford D.M., Wolfe B.A., Roberts-Galbraith R.H., McDonald W.H.,
RA Yates J.R. III, Gould K.L.;
RT "The Clp1/Cdc14 phosphatase contributes to the robustness of cytokinesis by
RT association with anillin-related Mid1.";
RL J. Cell Biol. 181:79-88(2008).
RN [12]
RP INTERACTION WITH BIR1; NBL1 AND PIC1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19570910; DOI=10.1091/mbc.e09-04-0289;
RA Bohnert K.A., Chen J.S., Clifford D.M., Vander Kooi C.W., Gould K.L.;
RT "A link between aurora kinase and Clp1/Cdc14 regulation uncovered by the
RT identification of a fission yeast borealin-like protein.";
RL Mol. Biol. Cell 20:3646-3659(2009).
RN [13]
RP FUNCTION IN DEPHOSPHORYLATION OF NSK1.
RX PubMed=22065639; DOI=10.1083/jcb.201105074;
RA Chen J.S., Lu L.X., Ohi M.D., Creamer K.M., English C., Partridge J.F.,
RA Ohi R., Gould K.L.;
RT "Cdk1 phosphorylation of the kinetochore protein Nsk1 prevents error-prone
RT chromosome segregation.";
RL J. Cell Biol. 195:583-593(2011).
RN [14]
RP FUNCTION.
RX PubMed=22624651; DOI=10.1186/gb-2012-13-5-r36;
RA Navarro F.J., Nurse P.;
RT "A systematic screen reveals new elements acting at the G2/M cell cycle
RT control.";
RL Genome Biol. 13:R36.1-R36.10(2012).
RN [15]
RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=22918952; DOI=10.1091/mbc.e12-06-0475;
RA Broadus M.R., Gould K.L.;
RT "Multiple protein kinases influence the redistribution of fission yeast
RT Clp1/Cdc14 phosphatase upon genotoxic stress.";
RL Mol. Biol. Cell 23:4118-4128(2012).
CC -!- FUNCTION: Protein phosphatase which antagonizes mitotic cyclin-
CC dependent kinase cdc2, the inactivation of which is essential for exit
CC from mitosis. To access its substrates, is released from nucleolar
CC sequestration during mitosis. Plays an essential in coordinating the
CC nuclear division cycle with cytokinesis through the cytokinesis
CC checkpoint. Involved in chromosome segregation, where it is required
CC for meiosis I spindle dissambly as well as for establishing two
CC consecutive chromosome segregation phases. Allows damaged actomyosin
CC rings to be maintained to facilitate completion of cell division in
CC response to minor perturbation of the cell division machinery.
CC Dephosphorylates the mitotic inducer cdc25 for its rapid degradation.
CC Down-regulation of cdc25 activity ensures a prompt inactivation of
CC mitotic cdc2 complexes to trigger cell division. Dephosphorylates also
CC cdc2-phosphorylated nsk1, allowing nsk1-binding to kinetochores and
CC spindle. Dephosphorylates ase1, which is essential for spindle midzone
CC assembly and for continuous extension of the anaphase spindle. Tethered
CC to the contractile ring by mid1, where it dephosphorylates cdc15.
CC {ECO:0000269|PubMed:11448769, ECO:0000269|PubMed:11683392,
CC ECO:0000269|PubMed:15128870, ECO:0000269|PubMed:15265986,
CC ECO:0000269|PubMed:15525536, ECO:0000269|PubMed:16085490,
CC ECO:0000269|PubMed:17562791, ECO:0000269|PubMed:18378776,
CC ECO:0000269|PubMed:19570910, ECO:0000269|PubMed:22065639,
CC ECO:0000269|PubMed:22624651}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBUNIT: Interacts with ark1 at the kinetochores. Interacts with bir1,
CC cdc25, mid1, nbl1, pic1, and rad24. {ECO:0000269|PubMed:15128870,
CC ECO:0000269|PubMed:15525536, ECO:0000269|PubMed:16085489,
CC ECO:0000269|PubMed:18378776, ECO:0000269|PubMed:19570910}.
CC -!- INTERACTION:
CC Q9P7H1; P42656: rad24; NbExp=3; IntAct=EBI-704737, EBI-704791;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm, cytoskeleton,
CC microtubule organizing center, spindle pole body. Cell septum.
CC Note=Localizes to kinetochores in prometaphase. Cytoplasmic retention
CC is mediated through the binding of rad24. Tethered to the contractile
CC ring by mid1.
CC -!- PTM: Phosphorylated by cds1, chk1, pmk1, and cdc2 upon Hydroxylurea and
CC H(2)O(2) stress treatment. Phosphorylation regulates the nucleolar-to-
CC nucleoplasmic transition. Is able to autodephosphorylate.
CC {ECO:0000269|PubMed:11683392, ECO:0000269|PubMed:18257517,
CC ECO:0000269|PubMed:22918952}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB76271.1; -; Genomic_DNA.
DR PIR; T50099; T50099.
DR RefSeq; NP_594716.1; NM_001020143.2.
DR AlphaFoldDB; Q9P7H1; -.
DR SMR; Q9P7H1; -.
DR BioGRID; 278823; 255.
DR IntAct; Q9P7H1; 4.
DR STRING; 4896.SPAC1782.09c.1; -.
DR iPTMnet; Q9P7H1; -.
DR MaxQB; Q9P7H1; -.
DR PaxDb; Q9P7H1; -.
DR PRIDE; Q9P7H1; -.
DR EnsemblFungi; SPAC1782.09c.1; SPAC1782.09c.1:pep; SPAC1782.09c.
DR GeneID; 2542358; -.
DR KEGG; spo:SPAC1782.09c; -.
DR PomBase; SPAC1782.09c; clp1.
DR VEuPathDB; FungiDB:SPAC1782.09c; -.
DR eggNOG; KOG1720; Eukaryota.
DR HOGENOM; CLU_017787_1_2_1; -.
DR InParanoid; Q9P7H1; -.
DR OMA; RIMRPGM; -.
DR PhylomeDB; Q9P7H1; -.
DR Reactome; R-SPO-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR PRO; PR:Q9P7H1; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IDA: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:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:PomBase.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:PomBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:PomBase.
DR GO; GO:0035853; P:chromosome passenger complex localization to spindle midzone; IMP:PomBase.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; IMP:PomBase.
DR GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; IMP:PomBase.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IMP:PomBase.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0031536; P:positive regulation of exit from mitosis; IMP:PomBase.
DR GO; GO:1903490; P:positive regulation of mitotic cytokinesis; IMP:PomBase.
DR GO; GO:0140429; P:positive regulation of mitotic sister chromatid biorientation; IMP:PomBase.
DR GO; GO:1902846; P:positive regulation of mitotic spindle elongation; IMP:PomBase.
DR GO; GO:0031031; P:positive regulation of septation initiation signaling; IGI:PomBase.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:PomBase.
DR GO; GO:1902440; P:protein localization to mitotic spindle pole body; IMP:PomBase.
DR GO; GO:0007096; P:regulation of exit from mitosis; IBA:GO_Central.
DR GO; GO:1904789; P:regulation of mitotic actomyosin contractile ring maintenance; IGI:PomBase.
DR GO; GO:0072479; P:response to mitotic cell cycle spindle assembly checkpoint signaling; IMP:PomBase.
DR CDD; cd14499; CDC14_C; 1.
DR CDD; cd17657; CDC14_N; 1.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR026070; CDC14.
DR InterPro; IPR044506; CDC14_C.
DR InterPro; IPR029260; DSPn.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR23339:SF27; PTHR23339:SF27; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF14671; DSPn; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Hydrolase; Meiosis;
KW Mitosis; Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome;
KW Septation.
FT CHAIN 1..537
FT /note="Tyrosine-protein phosphatase CDC14 homolog"
FT /id="PRO_0000094874"
FT DOMAIN 182..345
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 359..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOD_RES 453
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 286
FT /note="C->A: Inactivates phosphatase activity."
FT /evidence="ECO:0000269|PubMed:17562791"
SQ SEQUENCE 537 AA; 60253 MW; F5E50A8C0924C7EA CRC64;
MDYQDDGLGE MIEFLEDKLY YTSLSQPPKA ELYPHMHFFT IDDELIYNPF YHDFGPLNVS
HLIRFAVIVH GIMGKHRQAK KSKAIVLYSS TDTRLRANAA CLLACYMVLV QNWPPHLALA
PLAQAEPPFL GFRDAGYAVS DYYITIQDCV YGLWRARESS ILNIRNIDVH DYETYERVEN
GDFNWISPKF IAFASPIQAG WNHASTRPKK LPQPFAIVLD YFVANKVKLI VRLNGPLYDK
KTFENVGIRH KEMYFEDGTV PELSLVKEFI DLTEEVEEDG VIAVHCKAGL GRTGCLIGAY
LIYKHCFTAN EVIAYMRIMR PGMVVGPQQH WLHINQVHFR AYFYEKAMGR AIQQATAAEP
LATPPRHPLN ATNGTSQSNI STPLPEPTPG QPRKVSGHNP PSARRLPSAS SVKFNEKLKN
ASKQSIQNEN KASYSSYEDS EIQNDDETRT VGTPTETISV VRLRRSSSQS NIEPNGVRSP
TSSPTGSPIR RTSGNRWSSG SSHSKKSAQR SVSMSSLNNT SNGRVAKPKP SKSRLIS
