ID PP4C_XENLA Reviewed; 307 AA. AC Q6IP91; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 90. DE RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit; DE Short=PP4C; DE Short=Pp4; DE EC=3.1.3.16; GN Name=ppp4c; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (JUN-2004) 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=H2O + O-phospho-L-seryl-[protein] = 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=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 -!- 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}. Nucleus {ECO:0000250}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {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; BC072026; AAH72026.1; -; mRNA. DR RefSeq; NP_001085238.1; NM_001091769.1. DR RefSeq; XP_018095722.1; XM_018240233.1. DR RefSeq; XP_018095723.1; XM_018240234.1. DR AlphaFoldDB; Q6IP91; -. DR SMR; Q6IP91; -. DR BioGRID; 101700; 1. DR IntAct; Q6IP91; 1. DR MaxQB; Q6IP91; -. DR DNASU; 432334; -. DR GeneID; 108703929; -. DR GeneID; 432334; -. DR KEGG; xla:108703929; -. DR KEGG; xla:432334; -. DR AGR; Xenbase:XB-GENE-17330529; -. DR AGR; Xenbase:XB-GENE-6078278; -. DR CTD; 108703929; -. DR CTD; 432334; -. DR Xenbase; XB-GENE-6078278; ppp4c.S. DR OrthoDB; 19833at2759; -. DR Proteomes; UP000186698; Chromosome 9_10L. DR Proteomes; UP000186698; Chromosome 9_10S. DR Bgee; 108703929; Expressed in blastula and 19 other cell types or tissues. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR CDD; cd07415; MPP_PP2A_PP4_PP6; 1. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. 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 PANTHER; PTHR45619:SF8; SERINE_THREONINE-PROTEIN PHOSPHATASE 4 CATALYTIC SUBUNIT; 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 Nucleus; Protein phosphatase; Reference proteome. FT CHAIN 1..307 FT /note="Serine/threonine-protein phosphatase 4 catalytic FT subunit" FT /id="PRO_0000291880" 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; 35123 MW; D2E0F60B5AB7C30E CRC64; MTEISDLDRQ IEQLRRCELI KESEVKALCA KAREILVEES NVQRVDSPVT VCGDIHGQFY DLKELFRVGG DVPETNYLFM GDFVDRGFYS VETFLLLLAL KVRYPDRITL IRGNHESRQI TQVYGFYDEC LRKYGSVTVW RYCTEIFDYL SLSAIIDGKI FCVHGGLSPS IQTLDQIRTI DRKQEVPHDG PMCDLLWSDP EDTTGWGVSP RGAGYLFGSD VVAQFNAANN IDMICRAHQL VMEGYKWHFN ETVLTVWSAP NYCYRCGNVA AILELDEHLQ KEFIIFEAAP QETRGIPSKK PVADYFL //