ID   CDKN3_RAT               Reviewed;         212 AA.
AC   B2RZ50;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Cyclin-dependent kinase inhibitor 3 {ECO:0000250|UniProtKB:Q16667};
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|EMBL:AAI67026.1, ECO:0000312|RGD:1307781};
GN   Synonyms=Kap {ECO:0000250|UniProtKB:Q16667};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000312|EMBL:EDL88327.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000312|EMBL:EDL88327.1};
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|EMBL:AAI67026.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Brown Norway/NHsdMcwi {ECO:0000269|PubMed:15489334};
RC   TISSUE=Embryonic liver {ECO:0000312|EMBL:AAI67026.1};
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}.
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DR   EMBL; CH474040; EDL88327.1; -; Genomic_DNA.
DR   EMBL; BC167026; AAI67026.1; -; mRNA.
DR   RefSeq; XP_006251853.1; XM_006251791.3.
DR   AlphaFoldDB; B2RZ50; -.
DR   SMR; B2RZ50; -.
DR   STRING; 10116.ENSRNOP00000012985; -.
DR   PhosphoSitePlus; B2RZ50; -.
DR   PaxDb; 10116-ENSRNOP00000012985; -.
DR   Ensembl; ENSRNOT00000012985.7; ENSRNOP00000012985.5; ENSRNOG00000009785.7.
DR   Ensembl; ENSRNOT00055047015; ENSRNOP00055038635; ENSRNOG00055027193.
DR   Ensembl; ENSRNOT00060039845; ENSRNOP00060032927; ENSRNOG00060022990.
DR   Ensembl; ENSRNOT00065054894; ENSRNOP00065045159; ENSRNOG00065031861.
DR   AGR; RGD:1307781; -.
DR   CTD; 1033; -.
DR   RGD; 1307781; Cdkn3.
DR   eggNOG; KOG1720; Eukaryota.
DR   GeneTree; ENSGT00390000004717; -.
DR   HOGENOM; CLU_047330_1_0_1; -.
DR   InParanoid; B2RZ50; -.
DR   OrthoDB; 5479521at2759; -.
DR   PhylomeDB; B2RZ50; -.
DR   TreeFam; TF101040; -.
DR   PRO; PR:B2RZ50; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Proteomes; UP000234681; Chromosome 15.
DR   Bgee; ENSRNOG00000009785; Expressed in testis and 18 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:RGD.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:RGD.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
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; B2RZ50; RN.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome.
FT   CHAIN           1..212
FT                   /note="Cyclin-dependent kinase inhibitor 3"
FT                   /id="PRO_0000396639"
FT   DOMAIN          32..201
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..24
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   212 AA;  23774 MW;  345F42838AA50801 CRC64;
     MKPPISIQAS EFDSSDEEPA DDEQTPIQIS WLPLSRVNCS QFLGLCALPG CKFKDVRRNI
     QKDTEELKSS GIQDVFVFCT RGELSKYRVP NLLDLYQQYG IVTHHHPIPD GGTPDIGSCW
     EIMEELATCL KNNRKTLIHC YGGLGRSCLV AACLLLYLSD SISPQQAIDS LRDVRGSGAI
     QTIKQYNYLH EFRDKLAAYL SSRDSLSRSV SR
//