ID   PP2A_ACEPE              Reviewed;         307 AA.
AC   P48577;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Serine/threonine-protein phosphatase PP2A-1 catalytic subunit;
DE            EC=3.1.3.16;
OS   Acetabularia peniculus (Green alga) (Polyphysa peniculus).
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; TCBD clade;
OC   Dasycladales; Polyphysaceae; Acetabularia.
OX   NCBI_TaxID=35862;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7664759;
RA   Menzel D., Vugrek O., Frank S., Elsner-Menzel C.;
RT   "Protein phosphatase 2A, a potential regulator of actin dynamics and actin-
RT   based organelle motility in the green alga Acetabularia.";
RL   Eur. J. Cell Biol. 67:179-187(1995).
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   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z26654; CAA81395.1; -; mRNA.
DR   AlphaFoldDB; P48577; -.
DR   SMR; P48577; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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:SF12; SERINE_THREONINE-PROTEIN PHOSPHATASE PP2A; 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   2: Evidence at transcript level;
KW   Hydrolase; Manganese; Metal-binding; Protein phosphatase.
FT   CHAIN           1..307
FT                   /note="Serine/threonine-protein phosphatase PP2A-1
FT                   catalytic subunit"
FT                   /id="PRO_0000058851"
FT   REGION          286..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   307 AA;  35246 MW;  AA021D16540EDA98 CRC64;
     MVVYKQLDEW IEHLMQCKPL PEENVKELVA KAREVFSNEK NVQPVKMPVT VCGDIHGQFH
     DMVELFKIGG TCPDTNYLFM GDYVDRGYNS VETVTLLVSL KVRYPERITI LRGNHESRQI
     TQVYGFYDEC LRKYGNANVW QLFTDLFDFL PLTGLIENEV FCLHGGLSPA LDTLDQIREL
     DRIQEVPHEG PMCDLLWSDP DERLGWGISP RGAGYTFGQD ISEQFNVRNS LKLVARAHQL
     VMEGYNWSHE KNVVTIFSAP NYCYRCGNMA AIMEVAEGMD KGFQQFEPAP RRGAEGEVNR
     RTPDYFL
//