ID   CC14C_HUMAN             Reviewed;         447 AA.
AC   A4D256; Q2VIP7; Q6NUS3; Q8NCT2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 3.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Dual specificity protein phosphatase CDC14C {ECO:0000305};
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:0000312|HGNC:HGNC:22427};
GN   Synonyms=CDC14B2 {ECO:0000303|PubMed:16201836}, CDC14Bretro;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-429.
RX   PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA   Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT   "Emergence of young human genes after a burst of retroposition in
RT   primates.";
RL   PLoS Biol. 3:E357-E357(2005).
RN   [5]
RP   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: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:18547142}; Single-pass membrane protein
CC       {ECO:0000255}. Note=Retains its endoplasmic reticulum localization
CC       during mitosis. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB92421.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=EAL23906.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC006024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236955; EAL23906.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC028690; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC068452; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; DQ120635; ABB92421.1; ALT_INIT; Genomic_DNA.
DR   CCDS; CCDS94101.1; -.
DR   AlphaFoldDB; A4D256; -.
DR   SMR; A4D256; -.
DR   IntAct; A4D256; 1.
DR   MINT; A4D256; -.
DR   STRING; 9606.ENSP00000497679; -.
DR   DEPOD; CDC14C; -.
DR   GlyGen; A4D256; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; A4D256; -.
DR   PhosphoSitePlus; A4D256; -.
DR   BioMuta; HGNC:22427; -.
DR   MassIVE; A4D256; -.
DR   PeptideAtlas; A4D256; -.
DR   ProteomicsDB; 639; -.
DR   Antibodypedia; 82404; 2 antibodies from 2 providers.
DR   Ensembl; ENST00000650262.2; ENSP00000497792.1; ENSG00000218305.5.
DR   MANE-Select; ENST00000650262.2; ENSP00000497792.1; NM_152627.3; NP_689840.2.
DR   AGR; HGNC:22427; -.
DR   GeneCards; CDC14C; -.
DR   HGNC; HGNC:22427; CDC14C.
DR   HPA; ENSG00000218305; Group enriched (retina, testis).
DR   neXtProt; NX_A4D256; -.
DR   VEuPathDB; HostDB:ENSG00000218305; -.
DR   GeneTree; ENSGT00940000155950; -.
DR   InParanoid; A4D256; -.
DR   OMA; FHAVKKK; -.
DR   OrthoDB; 9871at2759; -.
DR   PhylomeDB; A4D256; -.
DR   PathwayCommons; A4D256; -.
DR   ChiTaRS; CDC14C; human.
DR   Pharos; A4D256; Tdark.
DR   PRO; PR:A4D256; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; A4D256; Protein.
DR   Bgee; ENSG00000218305; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 15 other cell types or tissues.
DR   ExpressionAtlas; A4D256; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0060271; P:cilium assembly; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
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: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; 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:SF117; DUAL SPECIFICITY PROTEIN PHOSPHATASE CDC14C; 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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Hydrolase; Membrane; Protein phosphatase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..447
FT                   /note="Dual specificity protein phosphatase CDC14C"
FT                   /id="PRO_0000315822"
FT   TRANSMEM        426..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          184..344
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          14..168
FT                   /note="A"
FT                   /evidence="ECO:0000250"
FT   REGION          169..182
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          183..349
FT                   /note="B"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        284
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   VARIANT         131
FT                   /note="P -> S (in dbSNP:rs1615556)"
FT                   /id="VAR_038327"
FT   VARIANT         189
FT                   /note="I -> L (in dbSNP:rs421206)"
FT                   /id="VAR_038328"
FT   CONFLICT        12
FT                   /note="R -> W (in Ref. 2; EAL23906)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20
FT                   /note="V -> L (in Ref. 3; BC028690 and 2; EAL23906)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        347
FT                   /note="R -> K (in Ref. 2; EAL23906)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        387
FT                   /note="S -> G (in Ref. 3; BC068452, 4; ABB92421 and 2;
FT                   EAL23906)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   447 AA;  51614 MW;  962ACC30F1C6D3EF CRC64;
     MRSSTLQDPR RRDPQDDVYV DITDRLRFAI LYSRPKSASN VHYFSIDNEL EYENFSEDFG
     PLNLAMVYRY CCKINKKLKS ITMLRKKIVH FTGSDQRKQA NAAFLVGCYM VIYLGRTPEA
     AYRILIFGDT PYIPFRDAAY GSCNFYITLL DCFHAVKKAM QYGFLNFNSF NLDEYEHYEK
     AENGDLNWII PDRFIAFCGP HSRARLESGY HQHSPETYIQ YFKNHNVTTI IRLNKRMYDA
     KRFTDAGFDH HDLFFADGST PTDAIVKRFL DICENAEGAI AVHCKAGLGR TGTLIACYIM
     KHYRMTAAET IAWVRICRPG LVIGPQQQFL VMKQTSLWLE GDYFRQRLKG QENGQHRAAF
     SKLLSGVDDI SINGVENQDQ QEPKPYSDDD EINGVTQGDR SRALKRRRQS KTNDILLPSP
     LAVLTFTLCS VVIWWIVCDY ILPILLF
//