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Database: UniProt
Entry: M3Y281_MUSPF
LinkDB: M3Y281_MUSPF
Original site: M3Y281_MUSPF 
ID   M3Y281_MUSPF            Unreviewed;       212 AA.
AC   M3Y281;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   16-OCT-2019, entry version 34.
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:ENSMPUP00000005432};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000005432, ECO:0000313|Proteomes:UP000000715};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000005432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ID#1420 {ECO:0000313|Ensembl:ENSMPUP00000005432};
RA   Di Palma F., Alfoldi J., Johnson J., Jaffe D., Berlin A., Gnerre S.,
RA   Grabherr M., Hall G., Lara M., MacCallum I., Mauceli E.,
RA   Przyblyski D., Ribeiro F., Russell P., Sharpe T., Turner-Maier J.,
RA   Walker B.J., Young S., Birren B., Lindblad-Toh K.;
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMPUP00000005432}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2013) 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   EMBL; AEYP01003638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01003639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004738868.1; XM_004738811.2.
DR   STRING; 9668.ENSMPUP00000005432; -.
DR   Ensembl; ENSMPUT00000005523; ENSMPUP00000005432; ENSMPUG00000005473.
DR   GeneID; 101670553; -.
DR   CTD; 1033; -.
DR   eggNOG; KOG1720; Eukaryota.
DR   eggNOG; COG2453; LUCA.
DR   GeneTree; ENSGT00390000004717; -.
DR   InParanoid; M3Y281; -.
DR   OMA; ALPGCKY; -.
DR   Proteomes; UP000000715; Unassembled WGS sequence.
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:UP000000715};
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:UP000000715}.
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;  23884 MW;  580880417FB49129 CRC64;
     MKPPSSLQTS EFDSSDEEPI EDEQTPIQIS WLPLSQVNCS QFLGLCALPG CKFKNVRRNI
     QKDTEELKSY GIQDIFVFCT RGELSKYRVP NLLDLYHQYG FITHHHPIPD GGTPDIASCC
     EIMEELAICL KNNRKTLIHC YGGLGRSCLV AACLLLYLSD TVSPEQAIDS LRDLRGSGAI
     QTIKQYNYLH EFRDKLAAHL SSRDSLSRSV SR
//
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