ID F7FIB7_MACMU Unreviewed; 212 AA.
AC F7FIB7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 11-DEC-2019, entry version 66.
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|EMBL:AFH30750.1,
GN ECO:0000313|Ensembl:ENSMMUP00000016171, ECO:0000313|VGNC:VGNC:70991};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000016171, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Ensembl:ENSMMUP00000016171, ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000016171,
RC ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000016171}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000016171};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [3] {ECO:0000313|EMBL:AFH30750.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thymus {ECO:0000313|EMBL:AFH30750.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
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 EMBL; JU473946; AFH30750.1; -; mRNA.
DR RefSeq; NP_001247846.1; NM_001260917.1.
DR STRING; 9544.ENSMMUP00000016171; -.
DR Ensembl; ENSMMUT00000017267; ENSMMUP00000016171; ENSMMUG00000012323.
DR GeneID; 694877; -.
DR KEGG; mcc:694877; -.
DR CTD; 1033; -.
DR VGNC; VGNC:70991; CDKN3.
DR eggNOG; KOG1720; Eukaryota.
DR eggNOG; COG2453; LUCA.
DR GeneTree; ENSGT00390000004717; -.
DR KO; K14167; -.
DR OMA; ALPGCKY; -.
DR OrthoDB; 1539111at2759; -.
DR TreeFam; TF101040; -.
DR Proteomes; UP000006718; Chromosome 7.
DR Bgee; ENSMMUG00000012323; Expressed in 15 organ(s), highest expression level in testis.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0004722; F:protein serine/threonine phosphatase activity; IEA:Ensembl.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0007050; P:cell cycle arrest; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell cycle {ECO:0000256|PIRNR:PIRNR037322};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR037322};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037322};
KW Kinase {ECO:0000313|EMBL:AFH30750.1};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR037322};
KW Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW Transferase {ECO:0000313|EMBL:AFH30750.1}.
FT DOMAIN 135..187
FT /note="TYR_PHOSPHATASE_2"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..21
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; 23808 MW; 6B4A6FA90310B863 CRC64;
MKPPSSIQTS EFDSSDEEPI EDEQTPIQIS WLSLSRVNCS QFLGLCALPG CKFKDVRRNV
QKDTEELKSC GIQDIFVFCT RGELSKYRVP NLLDLYQQCG IITHHHPIAD GGTPDIASCC
EIMEELTICL KNYRKTLIHC YGGLGRSCLV AACLLLYLSD TISPEQAIDS LRDLRGSGAI
QTIKQYNYLH EFRDKLAAHL SSRDSQSRSV SR
//
