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Database: UniProt
Entry: A0A2I3MFA9_PAPAN
LinkDB: A0A2I3MFA9_PAPAN
Original site: A0A2I3MFA9_PAPAN 
ID   A0A2I3MFA9_PAPAN        Unreviewed;       172 AA.
AC   A0A2I3MFA9;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   13-FEB-2019, entry version 6.
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:ENSPANP00000034433};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000034433, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000034433, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A.,
RA   Aqrawi P.A., Arias F.A., Attaway T.A., Awwad R.A., Babu C.B.,
RA   Bandaranaike D.B., Battles P.B., Bell A.B., Beltran B.B.,
RA   Berhane-Mersha D.B., Bess C.B., Bickham C.B., Bolden T.B.,
RA   Carter K.C., Chau D.C., Chavez A.C., Clerc-Blankenburg K.C.,
RA   Coyle M.C., Dao M.D., Davila M.L.D., Davy-Carroll L.D., Denson S.D.,
RA   Dinh H.D., Fernandez S.F., Fernando P.F., Forbes L.F., Francis C.F.,
RA   Francisco L.F., Fu Q.F., Garcia-Iii R.G., Garrett T.G., Gross S.G.,
RA   Gubbala S.G., Hirani K.H., Hogues M.H., Hollins B.H., Jackson L.J.,
RA   Javaid M.J., Jhangiani S.J., Johnson A.J., Johnson B.J., Jones J.J.,
RA   Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K., Kovar C.K.,
RA   Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P.,
RA   Perez Y.P., Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q.,
RA   Rouhana J.R., Ruiz M.R., Ruiz S.-J.R., Saada N.S., Santibanez J.S.,
RA   Scheel M.S., Schneider B.S., Simmons D.S., Sisson I.S., Tang L.-Y.T.,
RA   Thornton R.T., Tisius J.T., Toledanes G.T., Trejos Z.T., Usmani K.U.,
RA   Varghese R.V., Vattathil S.V., Vee V.V., Walker D.W.,
RA   Weissenberger G.W., White C.W., Williams A.W., Woodworth J.W.,
RA   Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N., Nazareth L.N.,
RA   Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000034433}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2018) 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; AHZZ02032196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHZZ02032197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSPANT00000048335; ENSPANP00000034433; ENSPANG00000015151.
DR   GeneTree; ENSGT00390000004717; -.
DR   Proteomes; UP000028761; Chromosome 7.
DR   ExpressionAtlas; A0A2I3MFA9; baseline.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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   Complete proteome {ECO:0000313|Proteomes:UP000028761};
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:UP000028761}.
FT   DOMAIN       95    147       TYR_PHOSPHATASE_2. {ECO:0000259|PROSITE:
FT                                PS50056}.
FT   ACT_SITE    100    100       Phosphocysteine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR037322-1}.
SQ   SEQUENCE   172 AA;  19371 MW;  5CEF6729BF6409FB CRC64;
     MKPPSSIQTS CKFKDVRRNV QKDTEELKSC GIQDIFVFCT RGELSKYRVP NLLDLYQQCG
     IITHHHPIAD GGTPDIASCC EIMEELTICL KNYRKTLIHC YGGLGRSCLV AACLLLYLSD
     TISPEQAIDS LRDLRGSGAI QTIKQYNYLH EFRDKLAAHL SSRDSQSRSV SR
//
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