ID   CDC14_CANAL             Reviewed;         542 AA.
AC   Q59NH8; A0A1D8PPE7;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Tyrosine-protein phosphatase CDC14;
DE            EC=3.1.3.48;
GN   Name=CDC14; OrderedLocusNames=CAALFM_C600670WA;
GN   ORFNames=CaO19.11669, CaO19.4192;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   FUNCTION.
RX   PubMed=11427967; DOI=10.1002/yea.729;
RA   Jimenez J., Cid V.J., Nombela C., Sanchez M.;
RT   "A single-copy suppressor of the Saccharomyces cerevisae late-mitotic
RT   mutants cdc15 and dbf2 is encoded by the Candida albicans CDC14 gene.";
RL   Yeast 18:849-858(2001).
RN   [5]
RP   INDUCTION, PHOSPHORYLATION, DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=16507592; DOI=10.1242/jcs.02820;
RA   Clemente-Blanco A., Gonzalez-Novo A., Machin F., Caballero-Lima D.,
RA   Aragon L., Sanchez M., de Aldana C.R., Jimenez J., Correa-Bordes J.;
RT   "The Cdc14p phosphatase affects late cell-cycle events and morphogenesis in
RT   Candida albicans.";
RL   J. Cell Sci. 119:1130-1143(2006).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18234840; DOI=10.1091/mbc.e07-09-0876;
RA   Gonzalez-Novo A., Correa-Bordes J., Labrador L., Sanchez M.,
RA   Vazquez de Aldana C.R., Jimenez J.;
RT   "Sep7 is essential to modify septin ring dynamics and inhibit cell
RT   separation during Candida albicans hyphal growth.";
RL   Mol. Biol. Cell 19:1509-1518(2008).
RN   [7]
RP   INDUCTION.
RX   PubMed=19477921; DOI=10.1091/mbc.e09-03-0210;
RA   Cote P., Hogues H., Whiteway M.;
RT   "Transcriptional analysis of the Candida albicans cell cycle.";
RL   Mol. Biol. Cell 20:3363-3373(2009).
CC   -!- FUNCTION: Protein phosphatase which antagonizes mitotic cyclin-
CC       dependent kinase CDC28, 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 (By similarity). Plays a role
CC       in the expression of hydrolase genes such as CHT3 and ENG1 involved in
CC       septum degradation after cytokinesis. Also required for ACE2
CC       localization to the daughter nucleus. Required for invasive and hyphal
CC       growth. {ECO:0000250, ECO:0000269|PubMed:11427967,
CC       ECO:0000269|PubMed:16507592, ECO:0000269|PubMed:18234840}.
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   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Bud neck.
CC       Cytoplasm, cytoskeleton, spindle pole. Cell septum. Note=Does not
CC       accumulate in the nucleolus in interphase cells. At the G1-S
CC       transition, starts to accumulate both in the nucleolus and the and the
CC       DAPI-staining region of the nucleus. At the S-G2 transition, starts to
CC       concentrate as faint foci on the nuclear periphery. In early mitosis,
CC       the CDC14 nuclear signal diminishes concentrates to the spindle pole
CC       body (SPB). During cytokinesis, the localization at the SPBs gets
CC       fainter and the protein is preferentially found at the septum region.
CC       In yeast forms, in which cell separation takes place after cytokinesis,
CC       CDC14 is present at the bud neck; in hyphal forms, in which cell
CC       separation is inhibited, no CDC14 signal is detected.
CC   -!- INDUCTION: Both during budding and hyphal growth, no detectable levels
CC       are observed in G1 cells but, as cells passe through S-phase, begins to
CC       accumulate with a peak being reached during mitosis.
CC       {ECO:0000269|PubMed:16507592, ECO:0000269|PubMed:19477921}.
CC   -!- PTM: Mainly phosphorylated as the cells are passing through mitosis in
CC       yeast form cells. Phosphorylation is delayed in hyphal-induced cells,
CC       indicating that the timing of cell-cycle progression occurs with
CC       different kinetics in hyphae and in yeast cells.
CC       {ECO:0000269|PubMed:16507592}.
CC   -!- DISRUPTION PHENOTYPE: Leads to defective cell separation and impairs
CC       hyphal growth. {ECO:0000269|PubMed:16507592}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class CDC14 subfamily. {ECO:0000305}.
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DR   EMBL; CP017628; AOW30013.1; -; Genomic_DNA.
DR   RefSeq; XP_019330990.1; XM_019475445.1.
DR   AlphaFoldDB; Q59NH8; -.
DR   SMR; Q59NH8; -.
DR   BioGRID; 1230209; 127.
DR   STRING; 237561.Q59NH8; -.
DR   EnsemblFungi; C6_00670W_A-T; C6_00670W_A-T-p1; C6_00670W_A.
DR   GeneID; 3647132; -.
DR   KEGG; cal:CAALFM_C600670WA; -.
DR   CGD; CAL0000180943; CDC14.
DR   VEuPathDB; FungiDB:C6_00670W_A; -.
DR   HOGENOM; CLU_017787_1_2_1; -.
DR   InParanoid; Q59NH8; -.
DR   OMA; ACMLCCY; -.
DR   OrthoDB; 9871at2759; -.
DR   PRO; PR:Q59NH8; -.
DR   Proteomes; UP000000559; Chromosome 6.
DR   GO; GO:0030428; C:cell septum; IDA:CGD.
DR   GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000776; C:kinetochore; IEA:EnsemblFungi.
DR   GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IEA:EnsemblFungi.
DR   GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR   GO; GO:1990023; C:mitotic spindle midzone; IEA:EnsemblFungi.
DR   GO; GO:0044732; C:mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0140602; C:nucleolar peripheral inclusion body; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IGI:CGD.
DR   GO; GO:0005654; C:nucleoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IDA:CGD.
DR   GO; GO:0000936; C:primary cell septum; IMP:CGD.
DR   GO; GO:0030869; C:RENT complex; IEA:EnsemblFungi.
DR   GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR   GO; GO:0005816; C:spindle pole body; IDA:CGD.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:CGD.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IMP:CGD.
DR   GO; GO:0071470; P:cellular response to osmotic stress; IEA:EnsemblFungi.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006974; P:DNA damage response; IEA:EnsemblFungi.
DR   GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR   GO; GO:0036267; P:invasive filamentous growth; IMP:CGD.
DR   GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:CGD.
DR   GO; GO:0051229; P:meiotic spindle disassembly; IEA:EnsemblFungi.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:1902406; P:mitotic actomyosin contractile ring maturation; IEA:EnsemblFungi.
DR   GO; GO:0000278; P:mitotic cell cycle; IGI:CGD.
DR   GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; IEA:EnsemblFungi.
DR   GO; GO:2000786; P:positive regulation of autophagosome assembly; IEA:EnsemblFungi.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; IBA:GO_Central.
DR   GO; GO:0031536; P:positive regulation of exit from mitosis; IEA:EnsemblFungi.
DR   GO; GO:1903501; P:positive regulation of mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR   GO; GO:0140429; P:positive regulation of mitotic sister chromatid biorientation; IEA:EnsemblFungi.
DR   GO; GO:1902846; P:positive regulation of mitotic spindle elongation; IEA:EnsemblFungi.
DR   GO; GO:0031031; P:positive regulation of septation initiation signaling; IEA:EnsemblFungi.
DR   GO; GO:0034501; P:protein localization to kinetochore; IEA:EnsemblFungi.
DR   GO; GO:1902440; P:protein localization to mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:1901891; P:regulation of cell septum assembly; IMP:CGD.
DR   GO; GO:0007096; P:regulation of exit from mitosis; IMP:CGD.
DR   GO; GO:0000920; P:septum digestion after cytokinesis; IMP:CGD.
DR   CDD; cd14499; CDC14_C; 1.
DR   CDD; cd17657; CDC14_N; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
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; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 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; (Phosphotyrosine protein) phosphatases II; 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.
FT   CHAIN           1..542
FT                   /note="Tyrosine-protein phosphatase CDC14"
FT                   /id="PRO_0000425253"
FT   DOMAIN          177..334
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          516..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        275
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   542 AA;  61582 MW;  34E207CFCA770FE7 CRC64;
     MHSSSVHVPL IEFLKNRIYL GAYDHHKRDT EDLAYFTVED ALPYNAFYMD FGPLNIGHLY
     RFAVLLHKKL NEDSTQGKGL VIYSSTSPKE RANLACLLCC YMILLQNWAP HQVLQPIAQI
     TPPLQAFRDA GYSSADYEIT IQDVVYAMWR AKERGMIDLA KFDLDEYEQY ERVDQGDFNV
     ISKDFIAFAS PQQSKRGGLN EPFQKVLEYF VENNVQLVVR LNSHLYDAKE FTKRNIKHID
     MIFDDGTCPT LEYVQKFIGA AECIINKGGK IAVHCKAGLG RTGCLIGAHL IYTHGFTANE
     CIAYMRMIRP GMVVGPQQHW LYLHHDDFRS WRHTMIVDNR PDPLIGNLFP LCSYEDYKQR
     LKEAKRKERL QLQQQLTSPL ADSSVINTPI RRRKVSGALA SKIQTVVPIE SPGQPRKYFE
     DSEDIDEVEM VNNSDDENTM QDIIQSSPAR YDSVTPKTKD NSDWRVLRSI STNNVSSQQS
     IHIIKTTTTK TVNETLSSPP GTSPTNVLRV SKARSKNRIA SGNSQTSRAH SGGVRKLSGK
     KH
//