PP4C2_CAEEL
ID PP4C2_CAEEL Reviewed; 321 AA.
AC Q9XTT8; Q966Q3;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit 2;
DE Short=PP4C-2;
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:P60510};
GN Name=pph-4.2 {ECO:0000303|PubMed:11896188, ECO:0000312|WormBase:Y49E10.3a};
GN ORFNames=Y49E10.3 {ECO:0000312|WormBase:Y49E10.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Bristol N2;
RX PubMed=11896188; DOI=10.1242/jcs.115.7.1403;
RA Sumiyoshi E., Sugimoto A., Yamamoto M.;
RT "Protein phosphatase 4 is required for centrosome maturation in mitosis and
RT sperm meiosis in C. elegans.";
RL J. Cell Sci. 115:1403-1410(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Protein phosphatase which seems to be involved in larval
CC development but not essential for embryogenesis.
CC {ECO:0000269|PubMed:11896188}.
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 Evidence={ECO:0000250|UniProtKB:P60510};
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 Evidence={ECO:0000250|UniProtKB:P60510};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P60510};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:P60510};
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|UniProtKB:P60510}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X)
CC subfamily. {ECO:0000305}.
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DR EMBL; AB070574; BAB63948.1; -; mRNA.
DR EMBL; Z98866; CAB11559.1; -; Genomic_DNA.
DR PIR; T27049; T27049.
DR RefSeq; NP_001022898.1; NM_001027727.3.
DR AlphaFoldDB; Q9XTT8; -.
DR SMR; Q9XTT8; -.
DR STRING; 6239.Y49E10.3a; -.
DR EPD; Q9XTT8; -.
DR PaxDb; Q9XTT8; -.
DR PeptideAtlas; Q9XTT8; -.
DR PRIDE; Q9XTT8; -.
DR EnsemblMetazoa; Y49E10.3a.1; Y49E10.3a.1; WBGene00004086.
DR GeneID; 176663; -.
DR KEGG; cel:CELE_Y49E10.3; -.
DR UCSC; Y49E10.3b; c. elegans.
DR CTD; 176663; -.
DR WormBase; Y49E10.3a; CE22221; WBGene00004086; pph-4.2.
DR eggNOG; KOG0372; Eukaryota.
DR GeneTree; ENSGT00930000151040; -.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; Q9XTT8; -.
DR OMA; TVDQMRI; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; Q9XTT8; -.
DR PRO; PR:Q9XTT8; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004086; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; Q9XTT8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..321
FT /note="Serine/threonine-protein phosphatase 4 catalytic
FT subunit 2"
FT /id="PRO_0000353211"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 66
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 249
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT CONFLICT 303
FT /note="A -> G (in Ref. 1; BAB63948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 36306 MW; FB599CACFF3B1D05 CRC64;
MLEEDAAGPD QLGPNDLDRQ IEIAMRCELI CETQVKSICA KVREILIEEA NVQVIDTPVT
ICGDIHGQFH DLMELFRVGG SPPNTNYLFL GDYVDRGYNS VETFILLMLL KCRYPDRITL
IRGNHESRQI TQVYGFYDEC VRKYGSGQVW KHCTEIFDYL SLAAVIDGKL FCVHGGLSPS
IATLDQIRVL DRKIEVPHEG PMCDLLWSDP EEGCSGWGIS PRGAGYLFGG DAAELFCENN
DFLRICRAHQ LVMEGYKLHF RKRVVTVWSA PNYCYRCGNV AAIMEVTEEN IDSDPVFEVF
EAATVENRGE PKKQPIAQYF L
