ID   PP4C_DICDI              Reviewed;         305 AA.
AC   Q9Y0B7; Q559Z8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit;
DE            Short=PP4C;
DE            EC=3.1.3.16;
GN   Name=ppp4c; Synonyms=pppC; ORFNames=DDB_G0272116;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=AX4;
RX   PubMed=10454741; DOI=10.1590/s0100-879x1999000700006;
RA   da-Silva A.M., Zapella P.D.A., Andrioli L.P.M., Campanha R.B.,
RA   Fiorini L.C., Etchebehere L.C., da-Costa-Maia J.C., Terenzi H.F.;
RT   "Searching for the role of protein phosphatases in eukaryotic
RT   microorganisms.";
RL   Braz. J. Med. Biol. Res. 32:835-839(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SMKA AND PPP4R2.
RX   PubMed=17353263; DOI=10.1128/mcb.02194-06;
RA   Mendoza M.C., Booth E.O., Shaulsky G., Firtel R.A.;
RT   "MEK1 and protein phosphatase 4 coordinate Dictyostelium development and
RT   chemotaxis.";
RL   Mol. Cell. Biol. 27:3817-3827(2007).
CC   -!- FUNCTION: Required for development, chemotaxis and the expression of
CC       numerous genes. {ECO:0000269|PubMed:17353263}.
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. Probably part of a PP4 complex containing ppp4c and ppp4r2.
CC       Interacts with smkA. {ECO:0000269|PubMed:17353263}.
CC   -!- INTERACTION:
CC       Q9Y0B7; Q54I18: smkA; NbExp=2; IntAct=EBI-2015876, EBI-2015890;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17353263}. Nucleus
CC       {ECO:0000269|PubMed:17353263}. Note=Translocated to the nucleus in
CC       aggregation-competent cells, probably by smkA.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF161253; AAD43137.1; -; mRNA.
DR   EMBL; AAFI02000008; EAL71210.1; -; Genomic_DNA.
DR   RefSeq; XP_645186.1; XM_640094.1.
DR   AlphaFoldDB; Q9Y0B7; -.
DR   SMR; Q9Y0B7; -.
DR   IntAct; Q9Y0B7; 1.
DR   STRING; 44689.Q9Y0B7; -.
DR   PaxDb; 44689-DDB0185222; -.
DR   EnsemblProtists; EAL71210; EAL71210; DDB_G0272116.
DR   GeneID; 8618358; -.
DR   KEGG; ddi:DDB_G0272116; -.
DR   dictyBase; DDB_G0272116; ppp4c.
DR   eggNOG; KOG0372; Eukaryota.
DR   HOGENOM; CLU_004962_8_1_1; -.
DR   InParanoid; Q9Y0B7; -.
DR   OMA; QSTMPID; -.
DR   PhylomeDB; Q9Y0B7; -.
DR   PRO; PR:Q9Y0B7; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030289; C:protein phosphatase 4 complex; IDA:dictyBase.
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; IDA:dictyBase.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0050920; P:regulation of chemotaxis; IGI:dictyBase.
DR   GO; GO:0031156; P:regulation of sorocarp development; IMP:dictyBase.
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   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Manganese; Metal-binding; Nucleus;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..305
FT                   /note="Serine/threonine-protein phosphatase 4 catalytic
FT                   subunit"
FT                   /id="PRO_0000327847"
FT   ACT_SITE        113
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
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         80
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  34862 MW;  C0903104ADA93D41 CRC64;
     MSSDLDRQIE QLKRCEIIKE SEVRALCSKA REILLEEGNV QRVDSPVTIC GDIHGQFYDL
     KELFKVGGDC PQTNYLFMGD FVDRGFYSVE TFLLLLALKV RYPDRITLIR GNHESRQITQ
     VYGFYEECVR KYGSVTVWKY CTEIFDYLSL SALVDGKIFC VHGGLSPSIN TLDQIRAIDR
     KQEVPHEGPM CDLMWSDPED IPGWNGSPRG AGFLFGEDVV QKFNHDNNLE FICRAHQLVM
     EGFKYMFNET LVTVWSAPNY CYRCGNVAAI LQLDENLKKN FAIFEAAPQE SRGAPAKKPA
     PEYFL
//