CDKN3_PIG
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 03-AUG-2022, entry version 91.
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.ENSSSCP00000019951; -.
DR PaxDb; Q9MYN5; -.
DR GeneID; 397589; -.
DR KEGG; ssc:397589; -.
DR CTD; 1033; -.
DR eggNOG; KOG1720; Eukaryota.
DR InParanoid; Q9MYN5; -.
DR OrthoDB; 1539111at2759; -.
DR PRO; PR:Q9MYN5; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; 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:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 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 Pfam; PF05706; CDKN3; 1.
DR PIRSF; PIRSF037322; CDKN3; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 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
