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Database: UniProt
Entry: Q32PC4_BOVIN
LinkDB: Q32PC4_BOVIN
Original site: Q32PC4_BOVIN 
ID   Q32PC4_BOVIN            Unreviewed;       167 AA.
AC   Q32PC4;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   13-NOV-2019, entry version 115.
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:AAI08174.1,
GN   ECO:0000313|Ensembl:ENSBTAP00000041263, ECO:0000313|VGNC:VGNC:27148};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI08174.1};
RN   [1] {ECO:0000313|EMBL:AAI08174.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Crossbred x Angus {ECO:0000313|EMBL:AAI08174.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:AAI08174.1};
RA   Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA   Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA   Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA   Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA   Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D.,
RA   Siddiqui A., Holt R., Jones S.J., Marra M.A.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000041263}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000041263};
RG   Ensembl;
RL   Submitted (MAR-2016) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSBTAP00000041263, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000041263,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L.,
RA   Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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; BC108173; AAI08174.1; -; mRNA.
DR   RefSeq; NP_001035672.1; NM_001040582.2.
DR   STRING; 9913.ENSBTAP00000041263; -.
DR   Ensembl; ENSBTAT00000043712; ENSBTAP00000041263; ENSBTAG00000019496.
DR   GeneID; 615282; -.
DR   KEGG; bta:615282; -.
DR   CTD; 1033; -.
DR   VGNC; VGNC:27148; CDKN3.
DR   eggNOG; KOG1720; Eukaryota.
DR   eggNOG; COG2453; LUCA.
DR   GeneTree; ENSGT00390000004717; -.
DR   HOGENOM; HOG000060336; -.
DR   KO; K14167; -.
DR   OMA; ALPGCKY; -.
DR   OrthoDB; 1539111at2759; -.
DR   TreeFam; TF101040; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000019496; Expressed in 9 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:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
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; IPR000340; Dual-sp_phosphatase_cat-dom.
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   Pfam; PF00782; DSPc; 1.
DR   PIRSF; PIRSF037322; CDKN3; 2.
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   Complete proteome {ECO:0000313|Proteomes:UP000009136};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR037322};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037322};
KW   Kinase {ECO:0000313|EMBL:AAI08174.1};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR037322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Transferase {ECO:0000313|EMBL:AAI08174.1}.
FT   DOMAIN       75    142       TYR_PHOSPHATASE_2. {ECO:0000259|PROSITE:
FT                                PS50056}.
FT   REGION        1     20       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   ACT_SITE     95     95       Phosphocysteine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR037322-1}.
SQ   SEQUENCE   167 AA;  18659 MW;  D01469F6FFC89A4D CRC64;
     MKPPSSMQTS EFDSSDEEPI EDEQTPIQIS WLPLSRVNCS QFLGLCALPG CKFKDVRRNI
     QKDTDGGTPD ITSCCEIMEE LEICLKNNRK TLIHCYGGLG RSCLVAACLL LYLSDTVSPQ
     QAIDSLRDLR GSGAIQTIKQ YNYLHEFRDK LAAHLSSRNS LSRSVSR
//
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