PP4C1_CAEEL
ID PP4C1_CAEEL Reviewed; 333 AA.
AC Q9XW79; Q966Q4;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit 1;
DE Short=PP4C-1;
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:P60510};
GN Name=pph-4.1 {ECO:0000303|PubMed:11896188, ECO:0000312|WormBase:Y75B8A.30};
GN ORFNames=Y75B8A.30 {ECO:0000312|WormBase:Y75B8A.30};
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], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
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).
RN [3]
RP FUNCTION, INTERACTION WITH MEI-1, AND DISRUPTION PHENOTYPE.
RX PubMed=19087961; DOI=10.1534/genetics.108.096016;
RA Han X., Gomes J.E., Birmingham C.L., Pintard L., Sugimoto A., Mains P.E.;
RT "The role of protein phosphatase 4 in regulating microtubule severing in
RT the Caenorhabditis elegans embryo.";
RL Genetics 181:933-943(2009).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-107 AND ARG-262.
RX PubMed=25340746; DOI=10.1371/journal.pgen.1004638;
RA Sato-Carlton A., Li X., Crawley O., Testori S., Martinez-Perez E.,
RA Sugimoto A., Carlton P.M.;
RT "Protein phosphatase 4 promotes chromosome pairing and synapsis, and
RT contributes to maintaining crossover competence with increasing age.";
RL PLoS Genet. 10:E1004638-E1004638(2014).
CC -!- FUNCTION: Protein phosphatase which plays an essential role in meiosis
CC and in early embryonic mitosis (PubMed:11896188, PubMed:25340746).
CC During spermatocyte meiosis and the first embryonic mitosis, regulates
CC centrosome maturation, and thus spindle formation, by recruiting some
CC of the components of the pericentriolar material (PCM)
CC (PubMed:11896188). During oocyte meiosis I, regulates meiotic
CC chromosome dynamics including synapsis-independent chromosome pairing,
CC restriction of synapsis to homologous chromosomes, programmed DNA
CC double-strand break initiation and crossover formation resulting in
CC chiasma formation (PubMed:11896188, PubMed:25340746). During oocyte
CC meiosis II and probably together with regulatory subunit ppfr-1, may
CC regulate microtubule severing by dephosphorylating and activating mei-
CC 1, a component of the katanin microtubule severing complex
CC (PubMed:19087961). {ECO:0000269|PubMed:11896188,
CC ECO:0000269|PubMed:19087961, ECO:0000269|PubMed:25340746}.
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:P67775};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:P67775};
CC -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in
CC different assemblies of the catalytic and one or more regulatory
CC subunits (By similarity). The regulatory subunits are likely to be
CC ppfr-1, ppfr-2, ppfr-4 and smk-1 (PubMed:19087961). Interacts with mei-
CC 1 (PubMed:19087961). {ECO:0000250|UniProtKB:P60510,
CC ECO:0000269|PubMed:19087961, ECO:0000305|PubMed:19087961}.
CC -!- INTERACTION:
CC Q9XW79; Q9N4E9: ppfr-4; NbExp=3; IntAct=EBI-331742, EBI-331766;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11896188}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:11896188}. Note=Localizes at centrosomes from
CC prophase to telophase but not during interphase. Also localizes to the
CC cytoplasm throughout the cell cycle. {ECO:0000269|PubMed:11896188}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos (at protein level).
CC {ECO:0000269|PubMed:11896188}.
CC -!- PTM: Methylation at the C-terminal Leu-333 is critical for interactions
CC with regulatory subunits. {ECO:0000250|UniProtKB:P60510}.
CC -!- DISRUPTION PHENOTYPE: Severe embryonic lethality associated with a high
CC incidence of male progeny (PubMed:25340746). RNAi-mediated knockdown
CC causes 20 percent embryonic lethality and 18 percent larval lethality
CC (PubMed:11896188). Abnormal meiosis and mitosis leading to defects in
CC gametogenesis and embryogenesis (PubMed:11896188, PubMed:25340746). In
CC spermatocytes, defects in the organization of astral microtubules
CC (PubMed:11896188). In oocyte meiosis I, defects in autosomal chromosome
CC pairing resulting from abnormal synapsis (PubMed:25340746). In embryos,
CC RNAi-mediated knockdown causes abnormal mitosis due to defects in
CC astral microtubules organization (PubMed:11896188). In a gain of
CC function mei-1 (ct46) or in mel-26 (ct61sb4) mutant background, RNAi-
CC mediated knockdown partially rescues embryonic lethality without
CC affecting mei-1 expression levels and localization (PubMed:19087961).
CC {ECO:0000269|PubMed:11896188, ECO:0000269|PubMed:19087961,
CC ECO:0000269|PubMed:25340746}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X)
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB63947.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AB070573; BAB63947.1; ALT_INIT; mRNA.
DR EMBL; AL033514; CAA22090.1; -; Genomic_DNA.
DR PIR; T27390; T27390.
DR RefSeq; NP_499603.1; NM_067202.5.
DR AlphaFoldDB; Q9XW79; -.
DR SMR; Q9XW79; -.
DR BioGRID; 41836; 14.
DR DIP; DIP-24807N; -.
DR IntAct; Q9XW79; 7.
DR STRING; 6239.Y75B8A.30; -.
DR EPD; Q9XW79; -.
DR PaxDb; Q9XW79; -.
DR PeptideAtlas; Q9XW79; -.
DR EnsemblMetazoa; Y75B8A.30.1; Y75B8A.30.1; WBGene00004085.
DR GeneID; 176657; -.
DR KEGG; cel:CELE_Y75B8A.30; -.
DR UCSC; Y75B8A.30; c. elegans.
DR CTD; 176657; -.
DR WormBase; Y75B8A.30; CE23041; WBGene00004085; pph-4.1.
DR eggNOG; KOG0372; Eukaryota.
DR GeneTree; ENSGT00930000151040; -.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; Q9XW79; -.
DR OMA; HGQFWDM; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; Q9XW79; -.
DR SignaLink; Q9XW79; -.
DR PRO; PR:Q9XW79; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004085; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005813; C:centrosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
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; ISS:WormBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051026; P:chiasma assembly; IMP:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISS:WormBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:WormBase.
DR GO; GO:1905261; P:regulation of meiotic DNA double-strand break formation involved in reciprocal meiotic recombination; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Hydrolase; Manganese;
KW Meiosis; Metal-binding; Methylation; Mitosis; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..333
FT /note="Serine/threonine-protein phosphatase 4 catalytic
FT subunit 1"
FT /id="PRO_0000353210"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 107
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 107
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 139
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 189
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 264
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT MOD_RES 333
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT MUTAGEN 107
FT /note="D->A: Probable loss of catalytic activity. Severe
FT loss of bivalent chromosome formation in diakinetic
FT oocytes."
FT /evidence="ECO:0000269|PubMed:25340746"
FT MUTAGEN 262
FT /note="R->L: Probable loss of catalytic activity. Severe
FT loss of bivalent chromosome formation in diakinetic
FT oocytes."
FT /evidence="ECO:0000269|PubMed:25340746"
SQ SEQUENCE 333 AA; 37359 MW; 7C7EA2177E45AA52 CRC64;
MALACTDSAN STFSRVDSPT SGPSDQLTTH DLDRHIEKLM RCELIAEQDV KTLCAKAREI
LAEEGNVQVI DSPVTICGDI HGQFYDLMEL FKVGGPVPNT NYLFLGDFVD RGFYSVETFL
LLLALKARYP DRMMLIRGNH ESRQITQVYG FYDECLRKYG NASVWKHCTE VFDYLSLAAV
IDGKVFCVHG GLSPSISTMD QIRVIDRKQE VPHDGPMCDL LWSDPEEGNV GWGLSPRGAG
YLFGADASKT FCETNGVDLI CRAHQLVMEG YKWHFNEKVL TVWSAPNYCY RCGNVAAILE
LDENLNKEFT IFEAAPQENR GAPAKKPHAD YFL
