(data stored in ACNUC8465 zone)

SWISSPROT: PTPA2_CANGA

ID   PTPA2_CANGA             Reviewed;         358 AA.
AC   Q6FK00;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 76.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A activator 2;
DE            EC=5.2.1.8;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase PTPA-2;
DE            Short=PPIase PTPA-2;
DE            Short=Rotamase PTPA-2;
DE   AltName: Full=Phosphotyrosyl phosphatase activator 2;
GN   Name=RRD2; OrderedLocusNames=CAGL0M02255g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   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
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. Acts as a regulatory subunit for PP2A-like
CC       phosphatases modulating their activity or substrate specificity,
CC       probably by inducing a conformational change in the catalytic
CC       subunit, a direct target of the PPIase. Can reactivate inactive
CC       phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in
CC       presence of ATP and Mg(2+) by dissociating the inactive form from
CC       the complex (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PTPA-type PPIase family. {ECO:0000305}.
DR   EMBL; CR380959; CAG62420.1; -; Genomic_DNA.
DR   RefSeq; XP_449444.1; XM_449444.1.
DR   ProteinModelPortal; Q6FK00; -.
DR   SMR; Q6FK00; -.
DR   STRING; 284593.XP_449444.1; -.
DR   EnsemblFungi; CAG62420; CAG62420; CAGL0M02255g.
DR   KEGG; cgr:CAGL0M02255g; -.
DR   CGD; CAL0137449; CAGL0M02255g.
DR   EuPathDB; FungiDB:CAGL0M02255g; -.
DR   eggNOG; KOG2867; Eukaryota.
DR   eggNOG; COG5057; LUCA.
DR   HOGENOM; HOG000205736; -.
DR   InParanoid; Q6FK00; -.
DR   KO; K17605; -.
DR   OMA; NTSRFGK; -.
DR   OrthoDB; EOG092C3CMG; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:GOC.
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:0030472; P:mitotic spindle organization in nucleus; IEA:EnsemblFungi.
DR   GO; GO:0006970; P:response to osmotic stress; IEA:EnsemblFungi.
DR   CDD; cd04087; PTPA; 1.
DR   InterPro; IPR004327; Phstyr_phstse_ac.
DR   PANTHER; PTHR10012; PTHR10012; 1.
DR   Pfam; PF03095; PTPA; 1.
DR   PIRSF; PIRSF016325; Phstyr_phstse_ac; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FK00.
DR   SWISS-2DPAGE; Q6FK00.
KW   Complete proteome; Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT   CHAIN         1    358       Serine/threonine-protein phosphatase 2A
FT                                activator 2.
FT                                /FTId=PRO_0000226110.
SQ   SEQUENCE   358 AA;  41231 MW;  A3E2730004E450F4 CRC64;
     MIPSKRILTD KDVKIWEESE TREDILSFIE SLAKAVEGFE NDQVSEPVSD SVQSTIAVLT
     EIDKLIKLHP VIQDKNTSRF GKVEFRDFYD DVCEKADDLL SSHFPALTSE QIEQLSIYLQ
     ESWGNKRRID YGSGHELNFI CFLYGLTHYK IFDLQRDARN LVLVLFIEYL KIMREIETLY
     WLEPAGSHGV WGLDDYHFLP FLFGAFQLAP HKHLKPKSIH NEELVEMFAD KYLYFGCIAF
     INSVKTSTSL RWHSPMLDDI SGVKKWSKVA EGMIKMYKAE VLGKLPIMQH FYFSEFLVCP
     EGISEPRTHI HNGDEDDDQC CQDGAAHNTW GDCCGIKIPS LYAANAMEKQ SHKPIPFD
//

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