PTPA1_USTMA
ID PTPA1_USTMA Reviewed; 487 AA.
AC Q4P4W3; A0A0D1CII7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
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; ORFNames=UMAG_04850;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) 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 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; CM003156; KIS66788.1; -; Genomic_DNA.
DR RefSeq; XP_011391699.1; XM_011393397.1.
DR AlphaFoldDB; Q4P4W3; -.
DR SMR; Q4P4W3; -.
DR STRING; 5270.UM04850P0; -.
DR EnsemblFungi; KIS66788; KIS66788; UMAG_04850.
DR GeneID; 23564903; -.
DR KEGG; uma:UMAG_04850; -.
DR VEuPathDB; FungiDB:UMAG_04850; -.
DR eggNOG; KOG2867; Eukaryota.
DR HOGENOM; CLU_030733_1_2_1; -.
DR InParanoid; Q4P4W3; -.
DR OMA; KMYDAEC; -.
DR OrthoDB; 1165705at2759; -.
DR Proteomes; UP000000561; Chromosome 17.
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:0007052; P:mitotic spindle organization; IBA:GO_Central.
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 SUPFAM; SSF140984; SSF140984; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; Nucleus; Reference proteome; Rotamase.
FT CHAIN 1..487
FT /note="Serine/threonine-protein phosphatase 2A activator 1"
FT /id="PRO_0000226104"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..487
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 53624 MW; 5C472C8674DBA00B CRC64;
MPMIPPALRR TQAAATPTTS SPAASSSTTA TLDSQSLCAL PRIRVSASTL NSIVTPVKKI
TSETDVEAWK ASAAYSIYTL FLQRVCEACV GKPTRLPTRS TDAPVTPVDK LVSLLWELDS
WTQEIEPHEK PQRFGNLAFR DWGARLEERI DSLLSDLLPS RLHAFAVELR VYLLDSFGSF
TRIDYGSGHE LAFFAWLCFL YRLGFFDASE EQEQDETLAD IQVEERIGLD IFPLYLMVVW
KLQDRYGLEP AGSHGVWGLD DFQFLPYVIG AAQLRRQSGL RPNQVIGASS HASILQTQLA
TRTDPASLIS TTLVLPASSL VGTQVEVPLP NLYLSSLLRI HVLKRGPFHE HSPLLNDIAS
SVPNWLKVYF GMLKMYAAEC LAKKVVVQHF AFGGVGWVWT HQAHSELPRL ATPSAPVAAR
RHLPLGGIQG NMTSMGVPTP RITRPPATPD SFDHPLRLPP RSTPSRPSTT PSVPPLAAST
RPAPKPE
