PP1_DICDI
ID PP1_DICDI Reviewed; 321 AA.
AC O15757; Q552P2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Serine/threonine-protein phosphatase PP1;
DE EC=3.1.3.16;
DE AltName: Full=DdPP1c;
GN Name=pppB; ORFNames=DDB_G0275619;
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], FUNCTION, ACTIVITY REGULATION, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF PHE-269.
RC STRAIN=AX4;
RX PubMed=12737629; DOI=10.1042/bj20021964;
RA Andrioli L.P.M., Zaini P.A., Viviani W., da Silva A.M.;
RT "Dictyostelium discoideum protein phosphatase-1 catalytic subunit exhibits
RT distinct biochemical properties.";
RL Biochem. J. 373:703-711(2003).
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 ACTIVITY REGULATION, INTERACTION WITH DPIA, AND MUTAGENESIS OF PHE-269.
RC STRAIN=AX4;
RX PubMed=17336445; DOI=10.1016/j.biochi.2007.01.002;
RA Sousa-Canavez J.M., Beton D., Gonzalez-Kristeller D.C., da Silva A.M.;
RT "Identification and domain mapping of Dictyostelium discoideum type-1
RT protein phosphatase inhibitor-2.";
RL Biochimie 89:692-701(2007).
CC -!- FUNCTION: Protein phosphatase activity in vitro.
CC {ECO:0000269|PubMed:12737629}.
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 -!- ACTIVITY REGULATION: Inhibited by okadaic acid, tautomycin and
CC calyculin A. Inhibited by phosphatase inhibitor 2 (dpiA).
CC {ECO:0000269|PubMed:12737629, ECO:0000269|PubMed:17336445}.
CC -!- SUBUNIT: Interacts with dpiA. {ECO:0000269|PubMed:17336445}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:12737629}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. {ECO:0000305}.
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DR EMBL; AF020537; AAB71415.1; -; mRNA.
DR EMBL; AAFI02000013; EAL69560.1; -; Genomic_DNA.
DR RefSeq; XP_643639.1; XM_638547.1.
DR AlphaFoldDB; O15757; -.
DR SMR; O15757; -.
DR STRING; 44689.DDB0185058; -.
DR PaxDb; O15757; -.
DR EnsemblProtists; EAL69560; EAL69560; DDB_G0275619.
DR GeneID; 8620226; -.
DR KEGG; ddi:DDB_G0275619; -.
DR dictyBase; DDB_G0275619; pppB.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; O15757; -.
DR OMA; TVQMSEN; -.
DR PhylomeDB; O15757; -.
DR BRENDA; 3.1.3.16; 1939.
DR Reactome; R-DDI-5673000; RAF activation.
DR PRO; PR:O15757; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:InterPro.
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 Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR037981; PPP1CC.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668:SF204; PTHR11668:SF204; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 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 Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..321
FT /note="Serine/threonine-protein phosphatase PP1"
FT /id="PRO_0000328376"
FT REGION 298..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 121
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MUTAGEN 269
FT /note="F->C: Five-fold increase in phosphatase activity,
FT decreased binding efficiency to dpiA and reduced
FT sensitivity to dpiA inhibition."
FT /evidence="ECO:0000269|PubMed:12737629,
FT ECO:0000269|PubMed:17336445"
SQ SEQUENCE 321 AA; 36939 MW; 571EECA8BE113BA4 CRC64;
MEIDLDSIIT RLLEPRTTKP GKLVDLAEEE IRYLTVQATE IFINQPILLE LEAPIKICGD
IHGQYYDLLR LFEYGGFPPQ SNYLFLGDYV DRGKQSLETI CLLLAYKIKY PENFFILRGN
HECASINRIY GFYDECKRRY NSKLWKAFTD CFNCLPVAAI IDEKIFCMHG GLSPDLKNMD
QIRRITRPTV VPDFGLLCDL LWADPDKNIQ GWEDNDRGVS YTFGADVVES FLKKHDLDLV
CRAHQVVEDG YEFFAKRQLV TLFSAPNYFG EFDNAGAMMG VDETLMCSFQ ILKPADKKKL
TNDSNGRPLT PPRNKQQKPK K
