PPID_DICDI
ID PPID_DICDI Reviewed; 174 AA.
AC Q9UA41; Q54VE9;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase D, mitochondrial;
DE Short=PPIase D;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin D;
DE AltName: Full=Rotamase D;
GN Name=cypD; Synonyms=cyp3; ORFNames=DDB_G0280401;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 8-14, SUBCELLULAR LOCATION,
RP 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 [2]
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).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By 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 -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10575348}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in vegetative cells, and a
CC steady decrease during the differentiation cycle.
CC {ECO:0000269|PubMed:10575348}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D
CC subfamily. {ECO:0000305}.
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DR EMBL; AF121347; AAD50375.1; -; mRNA.
DR EMBL; AAFI02000036; EAL67179.1; -; Genomic_DNA.
DR RefSeq; XP_641160.1; XM_636068.1.
DR AlphaFoldDB; Q9UA41; -.
DR SMR; Q9UA41; -.
DR STRING; 44689.DDB0215377; -.
DR PaxDb; Q9UA41; -.
DR EnsemblProtists; EAL67179; EAL67179; DDB_G0280401.
DR GeneID; 8622540; -.
DR KEGG; ddi:DDB_G0280401; -.
DR dictyBase; DDB_G0280401; cypD.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; Q9UA41; -.
DR OMA; AWIKATC; -.
DR PhylomeDB; Q9UA41; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q9UA41; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:dictyBase.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
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 Direct protein sequencing; Isomerase; Mitochondrion; Reference proteome;
KW Rotamase.
FT CHAIN 1..174
FT /note="Peptidyl-prolyl cis-trans isomerase D,
FT mitochondrial"
FT /id="PRO_0000365605"
FT DOMAIN 10..173
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 174 AA; 19016 MW; EA1984BAF901ED96 CRC64;
MTGIIRNKVF FQIKQGNTPL GRVVFELYND IVPKTAENFR ALCTGEKGIG KSGKPLHYKG
SSFHRVIKNF MVQGGDFTHG TGIGGESIYG RTFNDENFLV KHKIGCLSMA NAGKNTNGSQ
FFITTAETPH LNGGHTVFGE VVEGFDIVKK VENAETDRSD RPKAACVIED CGQL
