CDC14_CANAL
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 03-AUG-2022, entry version 108.
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 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; EWKYTMR; -.
DR OrthoDB; 1357618at2759; -.
DR PRO; PR:Q59NH8; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
DR GO; GO:0140602; C:nucleolar ring; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:EnsemblFungi.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
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; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:EnsemblFungi.
DR GO; GO:0035853; P:chromosome passenger complex localization to spindle midzone; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; 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:1903490; P:positive regulation of mitotic cytokinesis; 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:0006470; P:protein dephosphorylation; IEA:InterPro.
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:0007096; P:regulation of exit from mitosis; IBA:GO_Central.
DR GO; GO:1904789; P:regulation of mitotic actomyosin contractile ring maintenance; IEA:EnsemblFungi.
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.
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
