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Database: UniProt
Entry: F6X5L7_CALJA
LinkDB: F6X5L7_CALJA
Original site: F6X5L7_CALJA 
ID   F6X5L7_CALJA            Unreviewed;       212 AA.
AC   F6X5L7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   16-OCT-2019, entry version 41.
DE   RecName: Full=Cyclin-dependent kinase inhibitor 3 {ECO:0000256|PIRNR:PIRNR037322};
DE            EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR037322};
DE            EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR037322};
GN   Name=CDKN3 {ECO:0000313|Ensembl:ENSCJAP00000013588};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000013588, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000013588, ECO:0000313|Proteomes:UP000008225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000013588}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
CC   -!- FUNCTION: May play a role in cell cycle regulation. Dual
CC       specificity phosphatase active toward substrates containing either
CC       phosphotyrosine or phosphoserine residues.
CC       {ECO:0000256|PIRNR:PIRNR037322}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
CC         [protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
CC         COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
CC         EC=3.1.3.16; Evidence={ECO:0000256|PIRNR:PIRNR037322};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000256|PIRNR:PIRNR037322}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000256|PIRNR:PIRNR037322}.
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DR   RefSeq; XP_002753964.1; XM_002753918.4.
DR   STRING; 9483.ENSCJAP00000013588; -.
DR   Ensembl; ENSCJAT00000014312; ENSCJAP00000013588; ENSCJAG00000007280.
DR   GeneID; 100398984; -.
DR   KEGG; cjc:100398984; -.
DR   CTD; 1033; -.
DR   eggNOG; KOG1720; Eukaryota.
DR   eggNOG; COG2453; LUCA.
DR   GeneTree; ENSGT00390000004717; -.
DR   InParanoid; F6X5L7; -.
DR   KO; K14167; -.
DR   OMA; ALPGCKY; -.
DR   OrthoDB; 1539111at2759; -.
DR   TreeFam; TF101040; -.
DR   Proteomes; UP000008225; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Ensembl.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007050; P:cell cycle arrest; IEA:Ensembl.
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_PHOSPHATASE_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.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|PIRNR:PIRNR037322};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008225};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR037322};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037322};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR037322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225}.
FT   DOMAIN      120    187       TYR_PHOSPHATASE_2. {ECO:0000259|PROSITE:
FT                                PS50056}.
FT   REGION        1     20       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   ACT_SITE    140    140       Phosphocysteine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR037322-1}.
SQ   SEQUENCE   212 AA;  23765 MW;  E2CD4603C7C89C5F CRC64;
     MKPPSSIQAS EFDSSDEEPI EDEQTPIQIS WLPLSRVNCS QFLGLCALPG CKFKNVRRNV
     EKDTEELKSC GIQDIFVFCT RGELSKYRVP NLLDLYQQCG IITHHHPIAD GGTPDIACCC
     EIMEELAICL KNNRKTLIHC YGGLGRSCLV AACLLLYLSD TVSPEQAIDS LRDLRGSGAI
     QTIKQYNYLH EFRDKLAAYL SSRDSRSRSV SR
//
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