CC14A_DANRE
ID CC14A_DANRE Reviewed; 611 AA.
AC A0A0R4IVA4;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Dual specificity protein phosphatase CDC14AB;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=CDC14 cell division cycle 14 homolog AB;
GN Name=cdc14ab;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=27259055; DOI=10.1016/j.ajhg.2016.04.015;
RA Delmaghani S., Aghaie A., Bouyacoub Y., El Hachmi H., Bonnet C., Riahi Z.,
RA Chardenoux S., Perfettini I., Hardelin J.P., Houmeida A., Herbomel P.,
RA Petit C.;
RT "Mutations in CDC14A, encoding a protein phosphatase involved in hair cell
RT ciliogenesis, cause autosomal-recessive severe to profound deafness.";
RL Am. J. Hum. Genet. 98:1266-1270(2016).
CC -!- FUNCTION: Dual-specificity phosphatase. Required for centrosome
CC separation and productive cytokinesis during cell division.
CC Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the
CC APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation
CC of mitotic cyclins and subsequent exit from mitosis.
CC {ECO:0000250|UniProtKB:Q9UNH5}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000250|UniProtKB:Q9UNH5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000250|UniProtKB:Q9UNH5};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNH5}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q9UNH5}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q9UNH5}. Cell projection, kinocilium
CC {ECO:0000250|UniProtKB:Q6GQT0}. Note=Centrosomal during interphase,
CC released into the cytoplasm at the onset of mitosis. Subsequently
CC localizes to the mitotic spindle pole and at the central spindle (By
CC similarity). Present along both the transient kinocilia of developing
CC cochlear hair cells and the persistent kinocilia of vestibular hair
CC cells (By similarity). {ECO:0000250|UniProtKB:Q6GQT0,
CC ECO:0000250|UniProtKB:Q9UNH5}.
CC -!- DOMAIN: Composed of two structurally equivalent A and B domains that
CC adopt a dual specificity protein phosphatase (DSP) fold.
CC {ECO:0000250|UniProtKB:Q9UNH5}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes a
CC shortening of the hair cell kinocilia in a larvae at 3 dpf. There are
CC no other gross morphological defects in the inner ear.
CC {ECO:0000269|PubMed:27259055}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000305}.
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DR EMBL; BX908733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR751228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005161772.1; XM_005161715.3.
DR AlphaFoldDB; A0A0R4IVA4; -.
DR SMR; A0A0R4IVA4; -.
DR STRING; 7955.ENSDARP00000096458; -.
DR GeneID; 565969; -.
DR CTD; 565969; -.
DR ZFIN; ZDB-GENE-070705-309; cdc14ab.
DR eggNOG; KOG1720; Eukaryota.
DR OrthoDB; 1357618at2759; -.
DR Reactome; R-DRE-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-DRE-5687128; MAPK6/MAPK4 signaling.
DR PRO; PR:A0A0R4IVA4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1902636; C:kinociliary basal body; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0007096; P:regulation of exit from mitosis; IBA:GO_Central.
DR CDD; cd14499; CDC14_C; 1.
DR CDD; cd17657; CDC14_N; 1.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR044506; CDC14_C.
DR InterPro; IPR029260; DSPn.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR026068; Dual_Pase_CDC14A.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR23339:SF77; PTHR23339:SF77; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF14671; DSPn; 1.
DR SMART; SM00195; DSPc; 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 3: Inferred from homology;
KW Cell cycle; Cell division; Cell projection; Cytoplasm; Cytoskeleton;
KW Hydrolase; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..611
FT /note="Dual specificity protein phosphatase CDC14AB"
FT /id="PRO_0000438706"
FT DOMAIN 194..352
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 23..178
FT /note="A"
FT REGION 179..192
FT /note="Linker"
FT REGION 193..359
FT /note="B"
FT REGION 408..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 294
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 611 AA; 68117 MW; E1EE5AEBCFD09B7F CRC64;
MTLDNLKHSA ILSTLFKMAD DNDLLGASEF IKDRLYFATL RSKPKSTANT HYFSTDEEFV
YENFYADFGP LNLAMLYRYC CKLNKKLKSF TLTRKRIVHY TSFDQRKRAN AAVLIGAYAV
IYLKKTPEEA YRALISGSNA SYLPFRDASF GNCTYNLTVL DCLQGIRKAL QHGFLNFETF
DVNEYEHYER VENGDLNWIT PGKLLAFSGP HPKSKVENGY PLHAPEAYFP YFRKHNVTTI
VRLNKKIYDA KRFTDAGFDH YDLFFVDGST PSDIITRRFL HICESTSGAV AVHCKAGLGR
TGTLIGCYLM KHYRFTSAEA IAWIRICRPG SIIGPQQHYL EEKQASLWAH GDSLRSKQRQ
YQDRSVPQLI SSMDNLSIST SIFKSHSLDR MEENDYAEND LGMTQGDKLR ALKGRRQPRS
ATTGAIRVED VKVHTRSPSQ PLSRMKPPAS SQGSISPLKS SKVPASSSSS SSSSSVSASA
KRIGRSSSSS TNLKSTRLAS SLGNLYEPNT ESISSGKPPS PSSFTPHPVR TTYNYHYEVN
NNNNQYSTTS SPSKSLGYNL NHSGPSGASA NARLSAGEQG HQRNPPAGLS GLSTRHLSRS
IPSLQSEYVQ Y
