ID A0A1S3A0F0_ERIEU Unreviewed; 212 AA.
AC A0A1S3A0F0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_007527428.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007527428.1};
RN [1] {ECO:0000313|RefSeq:XP_007527428.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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|ARBA:ARBA00009580, ECO:0000256|PIRNR:PIRNR037322}.
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DR RefSeq; XP_007527428.1; XM_007527366.2.
DR AlphaFoldDB; A0A1S3A0F0; -.
DR STRING; 9365.ENSEEUP00000013740; -.
DR GeneID; 103117333; -.
DR CTD; 1033; -.
DR eggNOG; KOG1720; Eukaryota.
DR InParanoid; A0A1S3A0F0; -.
DR OrthoDB; 5479521at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Cell cycle {ECO:0000256|PIRNR:PIRNR037322};
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:UP000079721}.
FT DOMAIN 32..201
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 114..187
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037322-1"
SQ SEQUENCE 212 AA; 23926 MW; 2F9ACF55C72CFF1D CRC64;
MKPPSSLQTS EFDSSDEEPI EDEQTPIQIS WLPLSQVNCS QFLGLSALPG CKFKDVRRNI
QKDTEELKSY GIQDIFVFCT RGELSKYRVP NLLDLYQQYG IITHHHPIPD GGTPDIARCC
KMMEELAICL KNNRKTLIHC YGGLGRSCLV AACLLLYLSD TVSPQQAIDS LRDLRGSGAI
QTIKQYNYLH EFRDELAAHL SSRESLSRSV SR
//
