PP4C1_CAEBR
ID PP4C1_CAEBR Reviewed; 333 AA.
AC A8XE00;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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; ORFNames=CBG11776;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Protein phosphatase which plays an essential role in meiosis
CC and in early embryonic mitosis. During spermatocyte meiosis and the
CC first embryonic mitosis, regulates centrosome maturation, and thus
CC spindle formation, by recruiting some of the components of the
CC pericentriolar material (PCM). During oocyte meiosis I, regulates
CC meiotic chromosome dynamics including synapsis-independent chromosome
CC pairing, restriction of synapsis to homologous chromosomes, programmed
CC DNA double-strand break initiation and crossover formation resulting in
CC chiasma formation. During oocyte meiosis II and probably together with
CC regulatory subunit ppfr-1, may regulate microtubule severing by
CC dephosphorylating and activating mei-1, a component of the katanin
CC microtubule severing complex. {ECO:0000250|UniProtKB:Q9XW79}.
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. The regulatory subunits are likely to be ppfr-1, ppfr-2,
CC ppfr-4 and smk-1. Interacts with mei-1. {ECO:0000250|UniProtKB:P60510,
CC ECO:0000250|UniProtKB:Q9XW79}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9XW79}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9XW79}. Note=Localizes at centrosomes from
CC prophase to telophase but not during interphase. Also localizes to the
CC cytoplasm throughout the cell cycle. {ECO:0000250|UniProtKB:Q9XW79}.
CC -!- PTM: Methylation at the C-terminal Leu-333 is critical for interactions
CC with regulatory subunits. {ECO:0000250|UniProtKB:P60510}.
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; HE601289; CAP30806.3; -; Genomic_DNA.
DR RefSeq; XP_002641024.1; XM_002640978.1.
DR AlphaFoldDB; A8XE00; -.
DR SMR; A8XE00; -.
DR STRING; 6238.CBG11776; -.
DR EnsemblMetazoa; CBG11776.1; CBG11776.1; WBGene00032850.
DR GeneID; 8583018; -.
DR KEGG; cbr:CBG_11776; -.
DR CTD; 8583018; -.
DR WormBase; CBG11776; CBP02888; WBGene00032850; Cbr-pph-4.1.
DR eggNOG; KOG0372; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; A8XE00; -.
DR OMA; HGQFWDM; -.
DR OrthoDB; 808922at2759; -.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0005813; C:centrosome; IEA:EnsemblMetazoa.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051026; P:chiasma assembly; IEA:EnsemblMetazoa.
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; IEA:EnsemblMetazoa.
DR GO; GO:1905261; P:regulation of meiotic DNA double-strand break formation involved in reciprocal meiotic recombination; IEA:EnsemblMetazoa.
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 3: Inferred from homology;
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_0000353209"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..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"
SQ SEQUENCE 333 AA; 37469 MW; 90F18DEC1D925BDC CRC64;
MALAVADTQN ETFARSESPT SGPSDQLSTH DLDRHIEKLM RCELIAEQDV KTLCAKAREI
LAEEGNVQVI DSPVTICGDI HGQFYDLMEL FRVGGPVPNT NYLFLGDFVD RGFYSVETFL
LLLALKARYP DRMMLIRGNH ESRQITQVYG FYDECMRKYG NASVWKHCTE VFDYLALAAV
IDGKVFCVHG GLSPSISTMD QIRVIDRKQE VPHDGPMCDL LWSDPEEGNV GWGLSPRGAG
YLFGADASKT FCEANSVDLI CRAHQLVMEG YKWHFNEKVL TVWSAPNYCY RCGNVAAILE
LDENLNREFT IFEAAPQENR GAPAKKPHAD YFL
