PP2AB_PIG
ID PP2AB_PIG Reviewed; 293 AA.
AC P11493;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform;
DE Short=PP2A-beta;
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:P62714};
DE Flags: Fragment;
GN Name=PPP2CB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=2827745; DOI=10.1021/bi00397a003;
RA Stone S.R., Hofsteenge J., Hemmings B.A.;
RT "Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit
RT of protein phosphatase 2A.";
RL Biochemistry 26:7215-7220(1987).
CC -!- FUNCTION: Catalytic subunit of protein phosphatase 2A (PP2A), a
CC serine/threonine phosphatase involved in the regulation of a wide
CC variety of enzymes, signal transduction pathways, and cellular events.
CC PP2A can modulate the activity of phosphorylase B kinase, casein kinase
CC 2, mitogen-stimulated S6 kinase, and MAP-2 kinase.
CC {ECO:0000250|UniProtKB:P62714}.
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 Evidence={ECO:0000250|UniProtKB:P62714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000250|UniProtKB:P62714};
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 Evidence={ECO:0000250|UniProtKB:P62714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005;
CC Evidence={ECO:0000250|UniProtKB:P62714};
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 common heterodimeric core enzyme, composed
CC of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant
CC regulatory subunit (PR65 or subunit A), that associates with a variety
CC of regulatory subunits. Proteins that associate with the core dimer
CC include three families of regulatory subunits B (the R2/B/PR55/B55,
CC R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable
CC regulatory subunit, viral proteins, and cell signaling molecules. Binds
CC PPME1. May indirectly interact with SGO1, most probably through
CC regulatory B56 subunits. Found in a complex with at least ARL2, PPP2CB,
CC PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD. Interacts with
CC CTTNBP2NL. Interacts with PTPA. {ECO:0000250|UniProtKB:P62714,
CC ECO:0000250|UniProtKB:Q0P594}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Chromosome,
CC centromere {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250}. Note=In prometaphase cells, but not in anaphase cells,
CC localizes at centromeres. During mitosis, also found at spindle poles
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Reversibly methyl esterified on Leu-293 by leucine carboxyl
CC methyltransferase 1 (Lcmt1) 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 -!- PTM: Phosphorylation of either threonine (by autophosphorylation-
CC activated protein kinase) or tyrosine results in inactivation of the
CC phosphatase. Auto-dephosphorylation has been suggested as a mechanism
CC for reactivation (By similarity). {ECO:0000250}.
CC -!- PTM: May be monoubiquitinated by NOSIP. {ECO:0000250|UniProtKB:P62715}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; M20193; AAA30982.1; -; mRNA.
DR PIR; B27430; B27430.
DR AlphaFoldDB; P11493; -.
DR SMR; P11493; -.
DR STRING; 9823.ENSSSCP00000016788; -.
DR PaxDb; P11493; -.
DR PeptideAtlas; P11493; -.
DR PRIDE; P11493; -.
DR eggNOG; KOG0371; Eukaryota.
DR InParanoid; P11493; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
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 GO; GO:0000278; P:mitotic cell cycle; 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; 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 Centromere; Chromosome; Cytoplasm; Cytoskeleton; Hydrolase; Manganese;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Ubl conjugation.
FT CHAIN <1..293
FT /note="Serine/threonine-protein phosphatase 2A catalytic
FT subunit beta isoform"
FT /id="PRO_0000058847"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 291
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62715"
FT MOD_RES 293
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P62714"
FT NON_TER 1
SQ SEQUENCE 293 AA; 33610 MW; EEFE8E6F0FEF8710 CRC64;
LNECKQLNEN QVRTLCEKAK EILTKESNVQ EVRCPVTVCG DVHGQFHDLM ELFRIGGKSP
DTNYLFMGDY VDRGYYSVET VTLLVALKVR YPERITILRG NHESRQITQV YGFYDECLRK
YGNANVWKYF TDLFDYLPLT ALVDGQIFCL HGGLSPSIDT LDHIRALDRL QEVPHEGPMC
DLLWSDPDDR GGWGISPRGA GYTFGQDISE TFNHANGLTL VSRAHQLVME GYNWCHDRNV
VTIFSAPNYC YRCGNQAAIM ELDDTLKYSF LQFDPAPRRG EPHVTRRTPD YFL
