PTPA_BOVIN
ID PTPA_BOVIN Reviewed; 324 AA.
AC Q2KJ44;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Serine/threonine-protein phosphatase 2A activator;
DE EC=5.2.1.8;
DE AltName: Full=PP2A, subunit B', PR53 isoform;
DE AltName: Full=Phosphotyrosyl phosphatase activator;
DE Short=PTPA;
DE AltName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit 4;
DE AltName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B';
GN Name=PTPA; Synonyms=PPP2R4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Acts as a regulatory subunit for serine/threonine-
CC protein phosphatase 2A (PP2A) modulating its activity or substrate
CC specificity, probably by inducing a conformational change in the
CC catalytic subunit, a proposed direct target of the PPIase. Can
CC reactivate inactive phosphatase PP2A-phosphatase methylesterase
CC complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity).
CC Reversibly stimulates the variable phosphotyrosyl phosphatase activity
CC of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in
CC vitro). The phosphotyrosyl phosphatase activity is dependent of an
CC ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in
CC apoptosis; the function appears to be independent from PP2A (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- SUBUNIT: Associates with the serine/threonine-protein phosphatase 2A
CC PP2A(D) heterodimeric core enzyme, composed of a 36 kDa catalytic
CC subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or
CC subunit A). Interacts with PPP2CB. {ECO:0000250|UniProtKB:P58389,
CC ECO:0000250|UniProtKB:Q15257}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PTPA-type PPIase family. {ECO:0000305}.
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DR EMBL; BC105529; AAI05530.1; -; mRNA.
DR RefSeq; NP_001039638.1; NM_001046173.1.
DR AlphaFoldDB; Q2KJ44; -.
DR SMR; Q2KJ44; -.
DR STRING; 9913.ENSBTAP00000032642; -.
DR PaxDb; Q2KJ44; -.
DR PeptideAtlas; Q2KJ44; -.
DR PRIDE; Q2KJ44; -.
DR Ensembl; ENSBTAT00000032713; ENSBTAP00000032642; ENSBTAG00000001933.
DR GeneID; 514460; -.
DR KEGG; bta:514460; -.
DR CTD; 5524; -.
DR VEuPathDB; HostDB:ENSBTAG00000001933; -.
DR VGNC; VGNC:33526; PTPA.
DR eggNOG; KOG2867; Eukaryota.
DR GeneTree; ENSGT00390000011500; -.
DR HOGENOM; CLU_030733_3_0_1; -.
DR InParanoid; Q2KJ44; -.
DR OMA; YMFLGCI; -.
DR OrthoDB; 1165705at2759; -.
DR TreeFam; TF105555; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000001933; Expressed in spermatid and 105 other tissues.
DR ExpressionAtlas; Q2KJ44; baseline.
DR GO; GO:1904949; C:ATPase complex; IEA:Ensembl.
DR GO; GO:0034704; C:calcium channel complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
DR GO; GO:0008160; F:protein tyrosine phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
DR CDD; cd04087; PTPA; 1.
DR Gene3D; 1.20.120.1150; -; 1.
DR InterPro; IPR004327; Phstyr_phstse_ac.
DR InterPro; IPR043170; PTPA_C_lid.
DR InterPro; IPR037218; PTPA_sf.
DR PANTHER; PTHR10012; PTHR10012; 1.
DR Pfam; PF03095; PTPA; 1.
DR PIRSF; PIRSF016325; Phstyr_phstse_ac; 1.
DR SUPFAM; SSF140984; SSF140984; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Isomerase; Nucleotide-binding;
KW Nucleus; Reference proteome; Rotamase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15257"
FT CHAIN 2..324
FT /note="Serine/threonine-protein phosphatase 2A activator"
FT /id="PRO_0000328834"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 148..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 205..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 307..308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15257"
SQ SEQUENCE 324 AA; 36882 MW; 5FCFB21DE2DBA1CB CRC64;
MAEGERQTPS DSSEDAPPTT QNFIIPKKEI HTVPDMGKWK RSQAYADYIG FILTLNEGVK
GKKLSFEYKV SEAIEKLVAL LNTLDRWIDE TPPVDQPSRF GNKAYRTWYA KLDQEAENLV
ATVVPTNLAA AVPEVAVYLK ESVGNSTRID YGTGHEAAFA AFLCCLCKIG VLRVDDQIAI
VFKVFNRYLE VMRKLQKTYR MEPAGSQGVW GLDDFQFLPF IWGSSQLIDH PYLEPRHFVD
EKAVNENHKD YMFLECILFI TEMKTGPFAE HSNQLWNISA VPSWSKVNQG LIRMYKAECL
EKFPVIQHFK FGSLLPIHPV MSSC
