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Database: UniProt
Entry: F6UZN6_MONDO
LinkDB: F6UZN6_MONDO
Original site: F6UZN6_MONDO 
ID   F6UZN6_MONDO            Unreviewed;       212 AA.
AC   F6UZN6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   16-OCT-2019, entry version 42.
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:ENSMODP00000014508};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000014508, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000014508, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L.,
RA   Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J.,
RA   Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A.,
RA   Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L.,
RA   Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M.,
RA   Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E.,
RA   Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M.,
RA   Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E.,
RA   Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A.,
RA   Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J.,
RA   Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J.,
RA   Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S.,
RA   Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A.,
RA   Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C.,
RA   Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P.,
RA   Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C.,
RA   Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K.,
RA   Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D.,
RA   Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G.,
RA   Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E.,
RA   Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C.,
RA   Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E.,
RA   Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K.,
RA   Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A.,
RA   Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R.,
RA   Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A.,
RA   Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N.,
RA   Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S.,
RA   Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F.,
RA   Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P.,
RA   Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D.,
RA   Sparrow T., Spaulding J., Stalker J., Stange-Thomann N.,
RA   Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T.,
RA   Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A.,
RA   Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C.,
RA   Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in
RT   non-coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000014508}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2011) 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   RefSeq; XP_007473193.1; XM_007473131.2.
DR   STRING; 13616.ENSMODP00000014508; -.
DR   Ensembl; ENSMODT00000014776; ENSMODP00000014508; ENSMODG00000011594.
DR   GeneID; 100029059; -.
DR   KEGG; mdo:100029059; -.
DR   CTD; 1033; -.
DR   eggNOG; KOG1720; Eukaryota.
DR   eggNOG; COG2453; LUCA.
DR   GeneTree; ENSGT00390000004717; -.
DR   InParanoid; F6UZN6; -.
DR   KO; K14167; -.
DR   OrthoDB; 1539111at2759; -.
DR   TreeFam; TF101040; -.
DR   Proteomes; UP000002280; Chromosome 1.
DR   Bgee; ENSMODG00000011594; Expressed in 7 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: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   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|PIRNR:PIRNR037322};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002280};
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:UP000002280}.
FT   DOMAIN      131    187       TYR_PHOSPHATASE_2. {ECO:0000259|PROSITE:
FT                                PS50056}.
FT   ACT_SITE    140    140       Phosphocysteine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR037322-1}.
SQ   SEQUENCE   212 AA;  24043 MW;  E80B129BC05E97CC CRC64;
     MKVPSTMQTS EFDSSDEETV ENEQTPFQVS WLPLSLVNCS QFLGLCSLPG CKFKDVRRNL
     QKDMEELKNY GIQDIFVFCT RGELSKYRVP NLLDFYQQHG IIIHHHPIPD GDTPDIDRCC
     GILQELAICL ENNRKTLIHC YGGLGRSCLV AACLLLYLSD TVSPQQAIDS LRDLRGSGAI
     QTIKQYNYLH DFRDKLAAHL STRDSISRSV SR
//
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