CC14C_SYMSY
ID CC14C_SYMSY Reviewed; 483 AA.
AC A6N3Q4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Dual specificity protein phosphatase CDC14C {ECO:0000250|UniProtKB:A4D256};
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=CDC14 cell division cycle 14 homolog C;
GN Name=CDC14C {ECO:0000250|UniProtKB:A4D256};
GN Synonyms=CDC14Bretro {ECO:0000303|PubMed:18547142};
OS Symphalangus syndactylus (Siamang) (Hylobates syndactylus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Symphalangus.
OX NCBI_TaxID=9590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=18547142; DOI=10.1371/journal.pbio.0060140;
RA Rosso L., Marques A.C., Weier M., Lambert N., Lambot M.A.,
RA Vanderhaeghen P., Kaessmann H.;
RT "Birth and rapid subcellular adaptation of a hominoid-specific CDC14
RT protein.";
RL PLoS Biol. 6:E140-E140(2008).
CC -!- FUNCTION: Dual-specificity phosphatase. Preferentially dephosphorylates
CC proteins modified by proline-directed kinases (By similarity).
CC {ECO:0000250}.
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 -!- 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Nucleus, nucleolus. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18547142}. Note=Nucleolar during interphase (By
CC similarity). Microtubular association (PubMed:18547142). {ECO:0000250,
CC ECO:0000269|PubMed:18547142}.
CC -!- DOMAIN: Composed of two structurally equivalent A and B domains that
CC adopt a dual specificity protein phosphatase (DSP) fold.
CC -!- MISCELLANEOUS: May act as an autosomal functional substitute.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000305}.
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DR EMBL; EF606887; ABR10606.1; -; Genomic_DNA.
DR AlphaFoldDB; A6N3Q4; -.
DR SMR; A6N3Q4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
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; 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 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 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; Hydrolase; Membrane; Nucleus; Protein phosphatase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..483
FT /note="Dual specificity protein phosphatase CDC14C"
FT /id="PRO_0000315823"
FT TRANSMEM 444..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 213..373
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..197
FT /note="A"
FT /evidence="ECO:0000250"
FT REGION 198..211
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 212..378
FT /note="B"
FT /evidence="ECO:0000250"
FT REGION 407..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..53
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 10..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 313
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 483 AA; 54961 MW; 8895A87FEBA3E5F1 CRC64;
MKRKSEGRSS WAAATCSPCC SLTSPSVKKI RSPTQQDPRH RDPQDDVYLD ITDRLRLAIL
YSRPKSASNV HYFSIDNELE YENFSEDFGP LNLAMVYRYC CKINKKLKSI TMLRKKIVHF
TGSDQRKQAN AAFLVGCYMV IYLGRTPEEA YRTLIFGDTS YIPFRDAAYG SCNFYITLLD
CFHAVKKAMQ YGFLNFNSFN LDEYEHYEKA ENGDLNWIIP DRFIAFCGPH SRARLESGYH
QHSPETYIQY FKNRNVTTII RLNKKMYDAK CFTDAGFDHH DLFFADGSSP TDAIVKGFLD
ICENAEGAIA VHCKAGLGRT GTLIACYIMK HYRMTAAETI AWVRICRPGL VIGPQQQFLV
MKQTSLWLEG DYFCQKLKGQ ENGQHRAAFP KLHSGVDDIS INGVENQDQQ EPEPYSDDDE
INGGTQGDRL RALKSRRQSK TNAILLTCPL AVLTSALCSV VIWWIVCDYI LPILLFCLDG
FGT
