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Database: UniProt
Entry: A0A1U7U218_TARSY
LinkDB: A0A1U7U218_TARSY
Original site: A0A1U7U218_TARSY 
ID   A0A1U7U218_TARSY        Unreviewed;       198 AA.
AC   A0A1U7U218;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   11-DEC-2019, entry version 9.
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|RefSeq:XP_008066289.1};
OS   Tarsius syrichta (Philippine tarsier).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Tarsiiformes; Tarsiidae;
OC   Carlito.
OX   NCBI_TaxID=1868482 {ECO:0000313|Proteomes:UP000189704, ECO:0000313|RefSeq:XP_008066289.1};
RN   [1] {ECO:0000313|RefSeq:XP_008066289.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (DEC-2018) to UniProtKB.
CC   -!- FUNCTION: May play a role in cell cycle regulation. Dual specificity
CC       phosphatase active toward substrates containing either phosphotyrosine
CC       or phosphoserine residues. {ECO:0000256|PIRNR:PIRNR037322}.
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         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_008066289.1; XM_008068098.1.
DR   GeneID; 103270571; -.
DR   CTD; 1033; -.
DR   OrthoDB; 1539111at2759; -.
DR   Proteomes; UP000189704; Genome assembly.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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   Cytoplasm {ECO:0000256|PIRNR:PIRNR037322};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037322};
KW   Kinase {ECO:0000313|RefSeq:XP_008066289.1};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR037322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189704};
KW   Transferase {ECO:0000313|RefSeq:XP_008066289.1}.
FT   DOMAIN          106..173
FT                   /note="TYR_PHOSPHATASE_2"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   ACT_SITE        126
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037322-1"
SQ   SEQUENCE   198 AA;  22562 MW;  11EE52D230939857 CRC64;
     MKILLKMNRL QSRYHGCLCH ERIVLSSWAY VPFQAGCKFK DVRRNVQKDT EELKSHGIQD
     IFVFCTRGEL SKYRVPNLLD LYQQCGMTTH HHPIPDGDTP DIASCCEIME ELAICLKNNR
     KTLIHCYGGL GRSCLVAACL LLYLSDTVSP QEAIDSLRDL RGSGAIQTIK QYNYLHEFRD
     KLAAHLSSRD SLSRSVSR
//
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