PTPA1_CANAL
ID PTPA1_CANAL Reviewed; 424 AA.
AC Q5ADP9; A0A1D8PKN2; Q8J1X1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
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; Synonyms=YPA1; OrderedLocusNames=CAALFM_C307080WA;
GN ORFNames=CaO19.14084, CaO19.6792;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SC5314 / CAI4 / ATCC MYA-682;
RA Knowles D.G., Jimenez J., Sanchez M.;
RT "Involvement of the Candida albicans YPA1 homolog in the mitosis exit
RT network.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PTPA-type PPIase family. {ECO:0000305}.
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DR EMBL; AJ507322; CAD45366.1; -; Genomic_DNA.
DR EMBL; CP017625; AOW28711.1; -; Genomic_DNA.
DR RefSeq; XP_719888.1; XM_714795.1.
DR AlphaFoldDB; Q5ADP9; -.
DR SMR; Q5ADP9; -.
DR BioGRID; 1221539; 2.
DR STRING; 237561.Q5ADP9; -.
DR GeneID; 3638445; -.
DR KEGG; cal:CAALFM_C307080WA; -.
DR CGD; CAL0000191133; RRD1.
DR VEuPathDB; FungiDB:C3_07080W_A; -.
DR eggNOG; KOG2867; Eukaryota.
DR HOGENOM; CLU_030733_2_1_1; -.
DR InParanoid; Q5ADP9; -.
DR OMA; LACRDWH; -.
DR OrthoDB; 1165705at2759; -.
DR PRO; PR:Q5ADP9; -.
DR Proteomes; UP000000559; Chromosome 3.
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 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_0000226095"
FT REGION 362..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 48232 MW; 77D8183BB6BE6EC9 CRC64;
MNWKTPSKKI YDSADLKNFE KSIAFEKLQK TLQQIILSVE NHKIPPGILN VDIVTRPGRI
GSIPLPSLIE PTTTTTTREN KIGPSNGNVE ILIELFQYLN KLIDETPPLK GPTRFGNFAC
RDWHDKIDII PILKKFKFPQ ELSSSNNSSS KSNIDGFLLE SSYYLLNSFG SKIRLDYGTG
HELSFLAFIG SLIEFKILNH PTTTEEINGK EILIIFANYY DLVRRLILVY NLEPAGSHGV
WGLDDHFHLI YILGASQFIN DKLAPIVQRS LSSQVINSCK LTNFYINAIA FIFRLKTGPF
NEHSPIIFDI HNKVFSWTKV RQGLIKMYMV EVFNKFPVLQ HFWCGEVLYP WKDHQGNDLP
VNEKEETELD KPPETTLNST TTTTTTTKVS SSTSKIPFTP APWANTTTTH AVPRNTRNTR
NPRS
