PTPA1_YARLI
ID PTPA1_YARLI Reviewed; 432 AA.
AC Q6CFX5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=YALI0B02772g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382128; CAG82655.1; -; Genomic_DNA.
DR RefSeq; XP_500437.1; XM_500437.1.
DR AlphaFoldDB; Q6CFX5; -.
DR SMR; Q6CFX5; -.
DR STRING; 4952.CAG82655; -.
DR PRIDE; Q6CFX5; -.
DR EnsemblFungi; CAG82655; CAG82655; YALI0_B02772g.
DR GeneID; 2907316; -.
DR KEGG; yli:YALI0B02772g; -.
DR VEuPathDB; FungiDB:YALI0_B02772g; -.
DR HOGENOM; CLU_030733_2_1_1; -.
DR InParanoid; Q6CFX5; -.
DR OMA; IKMYEAE; -.
DR Proteomes; UP000001300; Chromosome B.
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..432
FT /note="Serine/threonine-protein phosphatase 2A activator 1"
FT /id="PRO_0000226105"
FT REGION 322..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 47585 MW; 64658AEE16D8A379 CRC64;
MTFSEPQKRI SSAADVDSFK RSQPYATIIS LLDKYSSTVQ EHLLPPNEDE LAASSKALVT
LCRKLSALID ETPPLEGPRR FGNVAVRDWH DKMEAQTTAL LTEAFPSINK DSIIELQYYL
HGGMGSKQRL DFGTGHELSF MAFVGGLQKL GLLETDLPAP DVLFIFETYF VLVRKLIMTY
SLEPAGSHGV WGLDDHSHLP YILGSAQKVS RSVTASTLLV PTKYDKECPP SSVMNPRIVQ
QQKTTNLYFA AIAFIYDIKS GPFYEHSPIL YDISGIATWA KIHSGMIKMY IAEVLGKFPV
VQHFYFGSEL YPWKDTEGND LPYSKVEDEE PVKPKLPLGF KSKKEPQTTP HARLPLMGPR
GMPMETVERL ARRDGQRAAR EKEEREDRAS GGASGTTGAP GATALPPTRA PGSSVPGGDA
PGMAPTKAPW AK
