PTPA_MOUSE
ID PTPA_MOUSE Reviewed; 323 AA.
AC P58389;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA David J., Yang X., Hashimoto K., Ramotar D.;
RT "Characterization of the mouse homolog of the human phosphotyrosyl
RT phosphatase activator, PTPA.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He, and FVB/N; TISSUE=Mammary gland, and Osteoblast;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND INTERACTION WITH PPP2CB.
RX PubMed=12952889; DOI=10.1101/gad.259903;
RA Fellner T., Lackner D.H., Hombauer H., Piribauer P., Mudrak I.,
RA Zaragoza K., Juno C., Ogris E.;
RT "A novel and essential mechanism determining specificity and activity of
RT protein phosphatase 2A (PP2A) in vivo.";
RL Genes Dev. 17:2138-2150(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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+). Reversibly
CC stimulates the variable phosphotyrosyl phosphatase activity of PP2A
CC core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The
CC phosphotyrosyl phosphatase activity is dependent of an ATPase activity
CC of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function
CC appears to be independent from PP2A (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12952889}.
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 PP2A heterodimeric core enzyme PP2A(D),
CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
CC constant regulatory subunit (PR65 or subunit A) (By similarity).
CC Interacts with PPP2CB (PubMed:12952889). {ECO:0000250|UniProtKB:Q15257,
CC ECO:0000269|PubMed:12952889}.
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; AY035997; AAK62028.1; -; mRNA.
DR EMBL; BC006626; AAH06626.1; -; mRNA.
DR EMBL; BC052852; AAH52852.1; -; mRNA.
DR CCDS; CCDS15883.1; -.
DR RefSeq; NP_620087.3; NM_138748.5.
DR AlphaFoldDB; P58389; -.
DR SMR; P58389; -.
DR BioGRID; 225960; 13.
DR IntAct; P58389; 2.
DR STRING; 10090.ENSMUSP00000046837; -.
DR BindingDB; P58389; -.
DR PhosphoSitePlus; P58389; -.
DR EPD; P58389; -.
DR jPOST; P58389; -.
DR PaxDb; P58389; -.
DR PeptideAtlas; P58389; -.
DR PRIDE; P58389; -.
DR ProteomicsDB; 291631; -.
DR Antibodypedia; 1074; 377 antibodies from 40 providers.
DR DNASU; 110854; -.
DR Ensembl; ENSMUST00000042055; ENSMUSP00000046837; ENSMUSG00000039515.
DR GeneID; 110854; -.
DR KEGG; mmu:110854; -.
DR UCSC; uc008jcn.2; mouse.
DR CTD; 5524; -.
DR MGI; MGI:1346006; Ptpa.
DR VEuPathDB; HostDB:ENSMUSG00000039515; -.
DR eggNOG; KOG2867; Eukaryota.
DR GeneTree; ENSGT00390000011500; -.
DR HOGENOM; CLU_030733_3_0_1; -.
DR InParanoid; P58389; -.
DR OMA; YMFLGCI; -.
DR OrthoDB; 1165705at2759; -.
DR PhylomeDB; P58389; -.
DR TreeFam; TF105555; -.
DR BioGRID-ORCS; 110854; 23 hits in 76 CRISPR screens.
DR ChiTaRS; Ptpa; mouse.
DR PRO; PR:P58389; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P58389; protein.
DR Bgee; ENSMUSG00000039515; Expressed in aortic valve and 258 other tissues.
DR ExpressionAtlas; P58389; baseline and differential.
DR Genevisible; P58389; MM.
DR GO; GO:1904949; C:ATPase complex; ISS:HGNC-UCL.
DR GO; GO:0034704; C:calcium channel complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; ISS:HGNC-UCL.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC-UCL.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISS:HGNC-UCL.
DR GO; GO:0019888; F:protein phosphatase regulator activity; ISS:HGNC-UCL.
DR GO; GO:0008160; F:protein tyrosine phosphatase activator activity; ISS:HGNC-UCL.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISS:HGNC-UCL.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; ISS:HGNC-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISS:HGNC-UCL.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:HGNC-UCL.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; ISS:HGNC-UCL.
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 1: Evidence at protein 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..323
FT /note="Serine/threonine-protein phosphatase 2A activator"
FT /id="PRO_0000071525"
FT REGION 1..22
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"
FT CONFLICT 10
FT /note="Missing (in Ref. 1; AAK62028)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="Q -> L (in Ref. 1; AAK62028)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 36710 MW; 1C7FA6C357A35F24 CRC64;
MAEGERQPPP DSSEETPPTT QNFIIPKKEI HTVPDMGKWK RSQAYADYIG FILTLNEGVK
GKKLTFDYKV SEAIEKLVAL LDTLDRWIDE TPPVDQPSRF GNKAYRTWYA KLDQEAENLV
ATVVPTHLAA AVPEVAVYLK EAVGNSTRID YGTGHEAAFA AFLCCLCKIG VLRVDDQVAI
VFKVFDRYLE VMRKLQKTYR MEPAGSQGVW GLDDFQFLPF IWGSSQLIDH PHLEPRHFVD
EKAVSENHKD YMFLQCILFI TEMKTGPFAE HSNQLWNISA VPSWSKVNQG LIRMYKAECL
EKFPVIQHFK FGSLLPIHPV TSG
