ID   CDKN3_PIG               Reviewed;         212 AA.
AC   Q9MYN5;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Cyclin-dependent kinase inhibitor 3 {ECO:0000250|UniProtKB:Q16667, ECO:0000303|PubMed:12078753, ECO:0000312|EMBL:CAB98135.1};
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
DE   AltName: Full=CDK2-associated dual-specificity phosphatase {ECO:0000250|UniProtKB:Q16667, ECO:0000303|PubMed:12078753};
DE   AltName: Full=Kinase-associated phosphatase {ECO:0000250|UniProtKB:Q16667};
GN   Name=CDKN3 {ECO:0000312|EMBL:CAB98135.1};
GN   Synonyms=KAP {ECO:0000250|UniProtKB:Q16667};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1] {ECO:0000312|EMBL:CAB97522.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Thigh muscle {ECO:0000269|PubMed:12078753};
RX   PubMed=12078753; DOI=10.2527/2002.8061698x;
RA   Maak S., Jaesert S., Neumann K., von Lengerken G.;
RT   "Rapid communication: nucleotide sequence and physical mapping of the
RT   porcine cyclin-dependent kinase inhibitor 3 (CDKN3) gene.";
RL   J. Anim. Sci. 80:1698-1699(2002).
RN   [2] {ECO:0000305}
RP   VARIANTS VAL-6; CYS-39; PHE-60; CYS-76; SER-78 AND GLY-79.
RX   PubMed=12927088; DOI=10.1186/1297-9686-35-s1-s157;
RA   Maak S., Jaesert S., Neumann K., von Lengerken G.;
RT   "Characterization of the porcine CDKN3 gene as a potential candidate for
RT   congenital splay leg in piglets.";
RL   Genet. Sel. Evol. 35:S157-S165(2003).
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; AJ404882; CAB97522.1; -; mRNA.
DR   EMBL; AJ404883; CAB98135.1; -; Genomic_DNA.
DR   EMBL; AJ404884; CAB98135.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_999485.1; NM_214320.1.
DR   RefSeq; XP_013842063.1; XM_013986609.1.
DR   AlphaFoldDB; Q9MYN5; -.
DR   SMR; Q9MYN5; -.
DR   STRING; 9823.ENSSSCP00000060429; -.
DR   PaxDb; 9823-ENSSSCP00000019951; -.
DR   GeneID; 397589; -.
DR   KEGG; ssc:397589; -.
DR   CTD; 1033; -.
DR   eggNOG; KOG1720; Eukaryota.
DR   InParanoid; Q9MYN5; -.
DR   OrthoDB; 5479521at2759; -.
DR   PRO; PR:Q9MYN5; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
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:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
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.
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_0000396638"
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..23
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"
FT   VARIANT         6
FT                   /note="S -> V"
FT                   /evidence="ECO:0000269|PubMed:12927088"
FT   VARIANT         39
FT                   /note="Y -> C"
FT                   /evidence="ECO:0000269|PubMed:12927088"
FT   VARIANT         60
FT                   /note="I -> F"
FT                   /evidence="ECO:0000269|PubMed:12927088"
FT   VARIANT         76
FT                   /note="F -> C"
FT                   /evidence="ECO:0000269|PubMed:12927088"
FT   VARIANT         78
FT                   /note="F -> S"
FT                   /evidence="ECO:0000269|PubMed:12927088"
FT   VARIANT         79
FT                   /note="C -> G"
FT                   /evidence="ECO:0000269|PubMed:12927088"
SQ   SEQUENCE   212 AA;  23906 MW;  3AD675A1EA40347E CRC64;
     MKPPSSIQTS EFDSSDEEPI EDEQTPIQIS WLPLSRVNYS QFLGLCALPG CKFKDVRRNI
     QKDTEELKSC GIQDVFVFCT RGELSKYRVP NLLDLYHQYG IITHHHPIPD GGAPDIASCC
     EIMEELEICL QNNRKTLIHC YGGLGRSCLV AACLLLYLSD TVSPQQAIDS LRDLRGSGAI
     QTIKQYNYLH EFRDKLAAHL SSRESLSRSV SR
//