(data stored in ACNUC7421 zone)

SWISSPROT: PTPA2_ASHGO

ID   PTPA2_ASHGO             Reviewed;         359 AA.
AC   Q75BY1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 94.
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=ACR139C;
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}.
CC   -!- SIMILARITY: Belongs to the PTPA-type PPIase family. {ECO:0000305}.
DR   EMBL; AE016816; AAS51365.1; -; Genomic_DNA.
DR   RefSeq; NP_983541.1; NM_208894.1.
DR   SMR; Q75BY1; -.
DR   STRING; 33169.AAS51365; -.
DR   EnsemblFungi; AAS51365; AAS51365; AGOS_ACR139C.
DR   GeneID; 4619673; -.
DR   KEGG; ago:AGOS_ACR139C; -.
DR   HOGENOM; HOG000205736; -.
DR   InParanoid; Q75BY1; -.
DR   KO; K17605; -.
DR   OMA; MQHFYFG; -.
DR   Proteomes; UP000000591; Chromosome III.
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   GO; GO:0006970; P:response to osmotic stress; IEA:EnsemblFungi.
DR   CDD; cd04087; PTPA; 1.
DR   InterPro; IPR004327; Phstyr_phstse_ac.
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;
DR   PRODOM; Q75BY1.
DR   SWISS-2DPAGE; Q75BY1.
KW   Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..359
FT                   /note="Serine/threonine-protein phosphatase 2A activator 2"
FT                   /id="PRO_0000226106"
SQ   SEQUENCE   359 AA;  40520 MW;  699749A85FC42B44 CRC64;
     MSDGAELKMA AQKRLLTGSD LDKWKASKTF EELLRFVSSL AQSVRGRENS EHAEPVSPAI
     EALEALLEEM QGIAAHHPVL QDAATSRFGK VEFRDFHKEV QARAEALVLQ VDPSLTDEQA
     QELAVYLGNA WGDCKRIDYG SGHELNFVCF LYGLWKYGVL SEHDFTNAVL RVFVKYMDVM
     RVLETKYWLE PAGSHGVWGL DDYHFLPFLF GAFQLATHKH LKPKSIHNPE VVELFENRYL
     YFGCIAFINR VKTTASLRWH SPMLDDISGV RSWTKVSEGM VKMYKAEVLG KLPIMQHFFF
     SRFLPVPDGV SPPRTSEEEL ADCSEHAHST WGDCCGIPIP SAVAASEATR KHSKPLPFD
//

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