PPIA_DICDI
ID PPIA_DICDI Reviewed; 179 AA.
AC Q54SM3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase A;
DE Short=PPIase A;
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:P62937};
DE AltName: Full=Cyclophilin A;
DE AltName: Full=Rotamase A;
GN Name=ppiA; Synonyms=cyp1; ORFNames=DDB_G0282359;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PROTEIN SEQUENCE OF 2-10, SUBCELLULAR LOCATION, CLEAVAGE OF INITIATOR
RP METHIONINE, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX2;
RX PubMed=10575348; DOI=10.1016/s0300-9084(99)00225-4;
RA Tapparo A., Kieffer S., Cretin F., Satre M., Klein G.;
RT "The multigene immunophilin family of Dictyostelium discoideum.
RT Characterization of microsomal and mitochondrial cyclophilin isoforms.";
RL Biochimie 81:943-954(1999).
RN [3]
RP PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
RN [4]
RP IDENTIFICATION, AND DEVELOPMENTAL STAGE.
RX PubMed=2049879; DOI=10.1002/dvg.1020120110;
RA Barisic K., Mollner S., Noegel A.A., Gerisch G., Segall J.E.;
RT "cDNA sequence of cyclophilin from Dictyostelium discoideum.";
RL Dev. Genet. 12:50-53(1991).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=8643519; DOI=10.1073/pnas.93.10.5003;
RA Spann T.P., Brock D.A., Lindsey D.F., Wood S.A., Gomer R.H.;
RT "Mutagenesis and gene identification in Dictyostelium by shotgun
RT antisense.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5003-5007(1996).
RN [6]
RP DEVELOPMENTAL STAGE [LARGE SCALE ANALYSIS].
RX PubMed=15470253; DOI=10.1128/ec.3.5.1241-1248.2004;
RA Maruo T., Sakamoto H., Iranfar N., Fuller D., Morio T., Urushihara H.,
RA Tanaka Y., Maeda M., Loomis W.F.;
RT "Control of cell type proportioning in Dictyostelium discoideum by
RT differentiation-inducing factor as determined by in situ hybridization.";
RL Eukaryot. Cell 3:1241-1248(2004).
CC -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline
CC imidic peptide bonds in oligopeptides and may therefore assist protein
CC folding. {ECO:0000250|UniProtKB:P62937}.
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 Evidence={ECO:0000250|UniProtKB:P62937};
CC -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase.
CC {ECO:0000250|UniProtKB:P62937}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10575348}.
CC -!- DEVELOPMENTAL STAGE: Not developmentally regulated.
CC {ECO:0000269|PubMed:10575348, ECO:0000269|PubMed:15470253,
CC ECO:0000269|PubMed:2049879}.
CC -!- DISRUPTION PHENOTYPE: Grows and develops almost normally, except for
CC the production of tall fruiting bodies. {ECO:0000269|PubMed:8643519}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000047; EAL66039.1; -; Genomic_DNA.
DR RefSeq; XP_640016.1; XM_634924.1.
DR AlphaFoldDB; Q54SM3; -.
DR SMR; Q54SM3; -.
DR STRING; 44689.DDB0216173; -.
DR PaxDb; Q54SM3; -.
DR EnsemblProtists; EAL66039; EAL66039; DDB_G0282359.
DR GeneID; 8623540; -.
DR KEGG; ddi:DDB_G0282359; -.
DR dictyBase; DDB_G0282359; ppiA.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; Q54SM3; -.
DR OMA; CSIINSG; -.
DR PhylomeDB; Q54SM3; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q54SM3; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0016018; F:cyclosporin A binding; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; ISS:dictyBase.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Isomerase; Reference proteome;
KW Rotamase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10575348, ECO:0000269|Ref.3"
FT CHAIN 2..179
FT /note="Peptidyl-prolyl cis-trans isomerase A"
FT /id="PRO_0000386632"
FT DOMAIN 15..178
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 179 AA; 19008 MW; 66CE4E8535B1FD41 CRC64;
MTTVKPTSPE NPRVFFDITI GGVEAGKVVM ELYANTVPKT AENFRALCTG EKGIGKSGKP
LSYKGSSFHR VITNFMCQGG DFTMGNGTGG ESIYGNKFAD ENFKLKHFGQ GTLSMANAGA
NTNGSQFFIC VAPTDWLDGK HVVFGFVTEG MDVVKKMEAA GSQSGKTTKP VVIANCGQL
