PTPA1_ASHGO
ID PTPA1_ASHGO Reviewed; 365 AA.
AC Q753L9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Serine/threonine-protein phosphatase 2A activator 1;
DE EC=5.2.1.8;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase PTPA-1;
DE Short=PPIase PTPA-1;
DE Short=Rotamase PTPA-1;
DE AltName: Full=Phosphotyrosyl phosphatase activator 1;
GN Name=RRD1; OrderedLocusNames=AFR293C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 PP2A-like phosphatases
CC modulating their activity or substrate specificity, probably by
CC inducing a conformational change in the catalytic subunit, a direct
CC target of the PPIase. Can reactivate inactive phosphatase PP2A-
CC phosphatase methylesterase complexes (PP2Ai) in presence of ATP and
CC Mg(2+) by dissociating the inactive form from the complex (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 -!- 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; AE016819; AAS53664.1; -; Genomic_DNA.
DR RefSeq; NP_985840.1; NM_211195.1.
DR AlphaFoldDB; Q753L9; -.
DR SMR; Q753L9; -.
DR STRING; 33169.AAS53664; -.
DR EnsemblFungi; AAS53664; AAS53664; AGOS_AFR293C.
DR GeneID; 4622103; -.
DR KEGG; ago:AGOS_AFR293C; -.
DR eggNOG; KOG2867; Eukaryota.
DR HOGENOM; CLU_030733_2_1_1; -.
DR InParanoid; Q753L9; -.
DR OMA; LACRDWH; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0008160; F:protein tyrosine phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:EnsemblFungi.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IEA:EnsemblFungi.
DR GO; GO:0006970; P:response to osmotic stress; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Cytoplasm; Isomerase; Nucleus; Reference proteome; Rotamase.
FT CHAIN 1..365
FT /note="Serine/threonine-protein phosphatase 2A activator 1"
FT /id="PRO_0000226092"
FT REGION 321..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 365 AA; 41327 MW; 8F0C34F4B24ED469 CRC64;
MEFSVEGTQF SPPVKRIFDT AGTHDFQKSL TMYRLQSHLE RYLKLVQGQK IPKSSQNRAV
VRFVCILERL DALMDETPPR TGSARRFGDL ACRDWHDRMQ GELDGLLETL LPEAARRSAA
ELRYYLGSAF GSRERLDYGT GHELAFLAVV VALDMLGLWT EDKFTGEDML YVWARYYALV
HRLILTYNLE PAGSHGVWGL DDHLHLAYIL GASQWAQDRN VPMQPSDILD PKAVARYSET
NLYCNSIAFL LRVKTGHFAQ HSPMLHDIAQ TVPTWSKVTT GLIKMYRVEV LNKFPVVQHF
WFGTGFFPWV DMAHGMSLPN YEAPSETSEK PAAGTAHTTT TTMPPPRMTA NCGYGPLGRL
VTPRR
