ID PP4CB_DANRE Reviewed; 307 AA. AC A9JRC7; DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 04-NOV-2026, entry version 103. DE RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit B; DE Short=PP4C-B; DE EC=3.1.3.16; GN Name=ppp4cb; ORFNames=zgc:172126; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Protein phosphatase that regulates many processes such as CC microtubule organization at centrosomes. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-threonyl-[protein] + H2O = 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 -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in CC different assemblies of the catalytic and one or more regulatory CC subunits. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X) CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC155609; AAI55610.1; -; mRNA. DR RefSeq; NP_001104638.1; NM_001111168.1. DR RefSeq; XP_073773810.1; XM_073917709.1. DR AlphaFoldDB; A9JRC7; -. DR SMR; A9JRC7; -. DR FunCoup; A9JRC7; 2083. DR STRING; 7955.ENSDARP00000103385; -. DR PaxDb; 7955-ENSDARP00000103385; -. DR PeptideAtlas; A9JRC7; -. DR Ensembl; ENSDART00000114857; ENSDARP00000103385; ENSDARG00000076439. DR GeneID; 562705; -. DR KEGG; dre:562705; -. DR AGR; ZFIN:ZDB-GENE-080219-32; -. DR CTD; 562705; -. DR ZFIN; ZDB-GENE-080219-32; ppp4cb. DR eggNOG; KOG0372; Eukaryota. DR GeneTree; ENSGT00930000151040; -. DR HOGENOM; CLU_004962_8_1_1; -. DR InParanoid; A9JRC7; -. DR OMA; AAGPFCQ; -. DR OrthoDB; 1930084at2759; -. DR PhylomeDB; A9JRC7; -. DR Reactome; R-DRE-5693607; Processing of DNA double-strand break ends. DR PRO; PR:A9JRC7; -. DR Proteomes; UP000000437; Chromosome 12. DR Bgee; ENSDARG00000076439; Expressed in mature ovarian follicle and 23 other cell types or tissues. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central. DR GO; GO:0048264; P:determination of ventral identity; IMP:ZFIN. DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central. DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:ZFIN. DR CDD; cd07415; MPP_PP2A_PP4_PP6; 1. DR FunFam; 3.60.21.10:FF:000010; Serine/threonine-protein phosphatase; 1. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR047129; PPA2-like. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR SMART; SM00156; PP2Ac; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Cytoskeleton; Hydrolase; Manganese; Metal-binding; Methylation; KW Protein phosphatase; Reference proteome. FT CHAIN 1..307 FT /note="Serine/threonine-protein phosphatase 4 catalytic FT subunit B" FT /id="PRO_0000353207" FT ACT_SITE 115 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 54 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 56 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 82 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 82 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 114 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 164 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 238 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT MOD_RES 307 FT /note="Leucine methyl ester" FT /evidence="ECO:0000250" SQ SEQUENCE 307 AA; 35097 MW; F3162A40BE347E16 CRC64; MGDMSDLDRQ IDQLRRCELI KENEVKALCA KAREILVEES NVQRVDSPVT VCGDIHGQFY DLKELFRVGG DVPETNYLFM GDFVDRGFYS VETFLLLLAL KVRYPDRITL IRGNHESRQI TQVYGFYDEC LRKYGSVTVW RYCTEIFDYL SLSAIIDGKI FCVHGGLSPS IQTLDQIRTI DRKQEVPHDG PMCDLLWSDP EDTTGWGVSP RGAGYLFGSD VVAQFNAAND IDMICRAHQL VMEGYKWHFN ETVLTVWSAP NYCYRCGNVA AILELDEHLQ KEFIIFEAAP QETRGIPSKK PVADYFL //