PP4C_DICDI
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 03-AUG-2022, entry version 126.
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 (Slime mold).
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.DDB0185222; -.
DR PaxDb; Q9Y0B7; -.
DR PRIDE; Q9Y0B7; -.
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; HGQFWDM; -.
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 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 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
