PP2A_ACEPE
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 03-AUG-2022, entry version 80.
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 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 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
