ID   CDKN3_MOUSE             Reviewed;         211 AA.
AC   Q810P3; Q9CWS3;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Cyclin-dependent kinase inhibitor 3 {ECO:0000250|UniProtKB:Q16667, ECO:0000312|EMBL:AAH49694.1};
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
DE   AltName: Full=CDK2-associated dual-specificity phosphatase {ECO:0000250|UniProtKB:Q16667};
DE   AltName: Full=Kinase-associated phosphatase {ECO:0000250|UniProtKB:Q16667};
GN   Name=Cdkn3 {ECO:0000312|MGI:MGI:1919641};
GN   Synonyms=Kap {ECO:0000250|UniProtKB:Q16667};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000312|EMBL:BAE27067.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB26929.1}, and DBA/2J
RC   {ECO:0000312|EMBL:BAE27067.1};
RC   TISSUE=Embryonic stem cell {ECO:0000312|EMBL:BAB26929.1}, and
RC   Embryonic testis {ECO:0000312|EMBL:BAC28238.1};
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2] {ECO:0000312|EMBL:AAH49694.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis {ECO:0000312|EMBL:AAH49694.1};
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).
CC   -!- FUNCTION: May play a role in cell cycle regulation. Dual specificity
CC       phosphatase active toward substrates containing either phosphotyrosine
CC       or phosphoserine residues. Dephosphorylates CDK2 at 'Thr-160' in a
CC       cyclin-dependent manner (By similarity).
CC       {ECO:0000250|UniProtKB:Q16667}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q16667};
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   -!- SUBUNIT: Interacts with cyclin-dependent kinases such as CDK1, CDK2 and
CC       CDK3. Does not interact with CDK4. Interacts (via C-terminus) with
CC       phosphorylated CDK2 (via C-terminal helix). Interacts with MS4A3 (via
CC       C-terminus); the interaction enhances CDKN3 enzymatic activity (By
CC       similarity). {ECO:0000250|UniProtKB:Q16667}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q16667}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB26929.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC       Sequence=BAC28238.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR   EMBL; AK010426; BAB26929.1; ALT_SEQ; mRNA.
DR   EMBL; AK033341; BAC28238.1; ALT_SEQ; mRNA.
DR   EMBL; AK146312; BAE27067.1; -; mRNA.
DR   EMBL; BC049694; AAH49694.1; -; mRNA.
DR   CCDS; CCDS49466.1; -.
DR   RefSeq; NP_082498.1; NM_028222.1.
DR   AlphaFoldDB; Q810P3; -.
DR   SMR; Q810P3; -.
DR   STRING; 10090.ENSMUSP00000070575; -.
DR   PhosphoSitePlus; Q810P3; -.
DR   PaxDb; 10090-ENSMUSP00000070575; -.
DR   ProteomicsDB; 281519; -.
DR   Antibodypedia; 3940; 582 antibodies from 31 providers.
DR   DNASU; 72391; -.
DR   Ensembl; ENSMUST00000067426.6; ENSMUSP00000070575.5; ENSMUSG00000037628.11.
DR   GeneID; 72391; -.
DR   KEGG; mmu:72391; -.
DR   UCSC; uc007the.2; mouse.
DR   AGR; MGI:1919641; -.
DR   CTD; 1033; -.
DR   MGI; MGI:1919641; Cdkn3.
DR   VEuPathDB; HostDB:ENSMUSG00000037628; -.
DR   eggNOG; KOG1720; Eukaryota.
DR   GeneTree; ENSGT00390000004717; -.
DR   HOGENOM; CLU_047330_1_0_1; -.
DR   InParanoid; Q810P3; -.
DR   OMA; CRYKDIR; -.
DR   OrthoDB; 5479521at2759; -.
DR   PhylomeDB; Q810P3; -.
DR   TreeFam; TF101040; -.
DR   BioGRID-ORCS; 72391; 0 hits in 81 CRISPR screens.
DR   ChiTaRS; Cdkn3; mouse.
DR   PRO; PR:Q810P3; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q810P3; Protein.
DR   Bgee; ENSMUSG00000037628; Expressed in seminiferous tubule of testis and 162 other cell types or tissues.
DR   ExpressionAtlas; Q810P3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISO:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006974; P:DNA damage response; ISO:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR   CDD; cd14505; CDKN3-like; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR008425; CDK_inhib_3.
DR   InterPro; IPR022778; CDKN3.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR23339:SF98; CYCLIN-DEPENDENT KINASE INHIBITOR 3-RELATED; 1.
DR   PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF05706; CDKN3; 1.
DR   PIRSF; PIRSF037322; CDKN3; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
DR   Genevisible; Q810P3; MM.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome.
FT   CHAIN           1..211
FT                   /note="Cyclin-dependent kinase inhibitor 3"
FT                   /id="PRO_0000396637"
FT   DOMAIN          32..200
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          1..34
FT                   /note="Interaction with CDK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16667"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        140
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   211 AA;  23793 MW;  A119D81C61A7F20F CRC64;
     MKPPISIQAS EFDSSDEEPV DEEQTPIQIS WLPLSRVNCS QFLGLCALPG CKFKDVRRNI
     QKDTEELKSY GIQDVFVFCT RGELSKYRVP NLLDLYQQYG IVTHHHPIPD GGTPDIGSCW
     EIMEELATCL KNNRKTLIHC YGGLGRSCLA ACLLLYLSDS ISPQQAIDSL RDVRGSGAIQ
     TIKQYNYLHE FRDKLAAYLS SRDSLSRSVS R
//