PP2AA_DICDI
ID PP2AA_DICDI Reviewed; 306 AA.
AC Q9XZE5; Q54G92;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Serine/threonine-protein phosphatase 2A catalytic subunit A;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase 2A 37 kDa catalytic subunit;
GN Name=pho2a; Synonyms=PP2A, PP2Ac; ORFNames=DDB_G0290263;
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], AND SUBCELLULAR LOCATION.
RX PubMed=10452519; DOI=10.1016/s0014-5793(99)00835-2;
RA Murphy M.B., Levi S.K., Egelhoff T.T.;
RT "Molecular characterization and immunolocalization of Dictyostelium
RT discoideum protein phosphatase 2A.";
RL FEBS Lett. 456:7-12(1999).
RN [2]
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 [3]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10491107; DOI=10.1046/j.1432-1327.1999.00670.x;
RA Murphy M.B., Egelhoff T.T.;
RT "Biochemical characterization of a Dictyostelium myosin II heavy-chain
RT phosphatase that promotes filament assembly.";
RL Eur. J. Biochem. 264:582-590(1999).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=18673380; DOI=10.1111/j.1432-0436.2008.00301.x;
RA Lee N.-S., Veeranki S., Kim B., Kim L.;
RT "The function of PP2A/B56 in non-metazoan multicellular development.";
RL Differentiation 76:1104-1110(2008).
CC -!- FUNCTION: Plays a role in activating the myosin contractile function.
CC Dephosphorylates threonine at 'Thr-1823', 'Thr-1833' and 'Thr-2029' in
CC the C-terminal tail region of myosin II heavy chain (mhcA). Drives the
CC assembly of dephosphorylated myosin II filaments to allow myosin
CC recruitment into the cytoskeleton. {ECO:0000269|PubMed:10491107}.
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: PP2A consists of a trimeric holoenzyme, composed of a 37 kDa
CC catalytic subunit (C subunit) and a 65 kDa constant regulatory subunit
CC (A subunit), that associates with a variety of regulatory subunits (B
CC subunit) such as phr2AB (B55) and psrA (B56 homolog). The trimer may
CC partially dissociates into a core 'AC' dimer equally active compared to
CC the trimer. {ECO:0000269|PubMed:10491107}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus speckle.
CC -!- PTM: Reversibly methyl esterified on Leu-306 by leucine carboxyl
CC methyltransferase 1 (LCMT) and protein phosphatase methylesterase 1
CC (PPME1). Carboxyl methylation influences the affinity of the catalytic
CC subunit for the different regulatory subunits, thereby modulating the
CC PP2A holoenzyme's substrate specificity, enzyme activity and cellular
CC localization (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC {ECO:0000305}.
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DR EMBL; AF138278; AAD29693.1; -; mRNA.
DR EMBL; AAFI02000162; EAL62258.1; -; Genomic_DNA.
DR RefSeq; XP_635791.1; XM_630699.1.
DR AlphaFoldDB; Q9XZE5; -.
DR SMR; Q9XZE5; -.
DR STRING; 44689.DDB0191299; -.
DR PaxDb; Q9XZE5; -.
DR EnsemblProtists; EAL62258; EAL62258; DDB_G0290263.
DR GeneID; 8627596; -.
DR KEGG; ddi:DDB_G0290263; -.
DR dictyBase; DDB_G0290263; pho2a.
DR eggNOG; KOG0371; Eukaryota.
DR HOGENOM; CLU_004962_0_5_1; -.
DR InParanoid; Q9XZE5; -.
DR OMA; EGYNWGQ; -.
DR PhylomeDB; Q9XZE5; -.
DR BRENDA; 3.1.3.16; 1939.
DR Reactome; R-DDI-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-DDI-198753; ERK/MAPK targets.
DR Reactome; R-DDI-202670; ERKs are inactivated.
DR Reactome; R-DDI-389513; CTLA4 inhibitory signaling.
DR Reactome; R-DDI-5673000; RAF activation.
DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DDI-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-DDI-69231; Cyclin D associated events in G1.
DR Reactome; R-DDI-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR PRO; PR:Q9XZE5; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IDA:dictyBase.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:dictyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0031034; P:myosin filament assembly; IDA: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; Methylation; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..306
FT /note="Serine/threonine-protein phosphatase 2A catalytic
FT subunit A"
FT /id="PRO_0000368206"
FT ACT_SITE 115
FT /note="Proton donor"
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 56
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 306
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000250"
SQ SEQUENCE 306 AA; 35186 MW; 1DC85DC05E292FEE CRC64;
MGEFQDVDKY ISILKECKPL SESEVRDLCE KAREILSKES NVQPVRCPVT VCGDIHGQFH
DLMELFKIGG NCPDTNYLFM GDYVDRGFYS VETVTLLVAL KVRYKDRVTI LRGNHESRQI
TQVYGFYDEC LRKYGNPNVW KLFTDLFDYL PLTALIENQV FCLHGGLSPS IDTLDHIENL
DRVQEVPHEG AMCDLLWSDP DDRLGFGYSP RGAGYTFGKD ISEQFNHNNG LTLVARAHQL
VMEGYNWCHD QNVVTIFSAP NYCYRCGNLA AIMEIDEKMK HTFLQFDPAP RRGEPHVTRR
TPDYFL
