PTPA1_CANGA
ID PTPA1_CANGA Reviewed; 424 AA.
AC Q6FRQ9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=CAGL0H06655g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380954; CAG60018.1; -; Genomic_DNA.
DR RefSeq; XP_447085.1; XM_447085.1.
DR AlphaFoldDB; Q6FRQ9; -.
DR SMR; Q6FRQ9; -.
DR STRING; 5478.XP_447085.1; -.
DR EnsemblFungi; CAG60018; CAG60018; CAGL0H06655g.
DR GeneID; 2888483; -.
DR KEGG; cgr:CAGL0H06655g; -.
DR CGD; CAL0130004; CAGL0H06655g.
DR VEuPathDB; FungiDB:CAGL0H06655g; -.
DR eggNOG; KOG2867; Eukaryota.
DR HOGENOM; CLU_030733_2_1_1; -.
DR InParanoid; Q6FRQ9; -.
DR OMA; IKMYEAE; -.
DR Proteomes; UP000002428; Chromosome H.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:EnsemblFungi.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0019211; F:phosphatase activator activity; IEA:InterPro.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
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..424
FT /note="Serine/threonine-protein phosphatase 2A activator 1"
FT /id="PRO_0000226096"
FT REGION 348..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 47927 MW; BCA37E1869F175A7 CRC64;
MFSEPVKRIY DSQGAYYFQS SEAIRRLEGA IVKYTDLVES RDVADLELSG VVGGVVKVLD
RLDQLVSETP PIPGPRRYGN MACRDWHEKI EREIPGLLED LISSHFPSEL QCVVELRYYL
ANSFGSATRL DFGTGHELSF LATVAALDML GASFDGDQVL YIFDRYYSLV HRLILSYTLE
PAGSHGVWGL DDHFHLAYIL GSSQWCNRKK LAMEPNDLSD PVLVEQYSRT NIFCKTLNFV
FTVKSGAFRE HSPMLFDISR SVRTWAKVRK GLWKMYKDEV LNKFPVIQHF WFGTGFYPWV
DYKNGKPLPN YENSPDIDET NDLKTQAQAN MDGTRVVESR FLSPGNETFV RRPQLPQDSG
VGTMRSSTPE SRLMNVTTRS TRSTAGPGQG RMGPPTSMGI VQTRMPSSTT SQAHASRLMN
TPRQ
