CYPE_DICDI
ID CYPE_DICDI Reviewed; 156 AA.
AC Q9NI62; Q55D92;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase cypE {ECO:0000303|PubMed:11690648};
DE Short=PPIase cypE;
DE EC=5.2.1.8 {ECO:0000269|PubMed:11690648};
DE AltName: Full=Cyclophilin cypE {ECO:0000303|PubMed:11690648};
DE AltName: Full=Rotamase cypE;
GN Name=cypE; ORFNames=DDB_G0269216;
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], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH SNWA.
RC STRAIN=AX3;
RX PubMed=11690648; DOI=10.1016/s0167-4781(01)00301-3;
RA Skruzny M., Ambrozkova M., Fukova I., Martinkova K., Blahuskova A.,
RA Hamplova L., Puta F., Folk P.;
RT "Cyclophilins of a novel subfamily interact with SNW/SKIP coregulator in
RT Dictyostelium discoideum and Schizosaccharomyces pombe.";
RL Biochim. Biophys. Acta 1521:146-151(2001).
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: Catalyzes the cis-trans isomerization of proline imidic
CC peptide bonds in oligopeptides (PubMed:11690648). Plays a role in
CC protein folding, transport and assembly (PubMed:11690648).
CC {ECO:0000269|PubMed:11690648, ECO:0000303|PubMed:11690648}.
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:0000269|PubMed:11690648};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16239;
CC Evidence={ECO:0000269|PubMed:11690648};
CC -!- SUBUNIT: Interacts with snwA. {ECO:0000269|PubMed:11690648}.
CC -!- INTERACTION:
CC Q9NI62; P54705: snwA; NbExp=5; IntAct=EBI-1810601, EBI-1810591;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11690648}. Nucleus
CC {ECO:0000269|PubMed:11690648}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF215865; AAF28343.2; -; mRNA.
DR EMBL; AAFI02000005; EAL71958.1; -; Genomic_DNA.
DR RefSeq; XP_646239.1; XM_641147.1.
DR AlphaFoldDB; Q9NI62; -.
DR SMR; Q9NI62; -.
DR IntAct; Q9NI62; 1.
DR STRING; 44689.DDB0191208; -.
DR PaxDb; Q9NI62; -.
DR EnsemblProtists; EAL71958; EAL71958; DDB_G0269216.
DR GeneID; 8617195; -.
DR KEGG; ddi:DDB_G0269216; -.
DR dictyBase; DDB_G0269216; cypE.
DR eggNOG; KOG0881; Eukaryota.
DR HOGENOM; CLU_012062_16_3_1; -.
DR InParanoid; Q9NI62; -.
DR OMA; ELYNDHA; -.
DR PhylomeDB; Q9NI62; -.
DR Reactome; R-DDI-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q9NI62; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:dictyBase.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
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 InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PTHR45625; 1.
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; Isomerase; Nucleus; Reference proteome; Rotamase.
FT CHAIN 1..156
FT /note="Peptidyl-prolyl cis-trans isomerase cypE"
FT /id="PRO_0000064170"
FT DOMAIN 2..155
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 156 AA; 17415 MW; D0E02E03DBA06DA3 CRC64;
MTEQTVTLQT TVGDITLELY YNHAPKACKN FYELSKRGYY DNTIFHRLIK DFMIQGGDPL
GNGRGGESIY GKKFEDEITK ELKHTGAGIL SMANSGVNSN GSQFFITFGP TPWLDGKHTI
FGRVKSGMKV VQKMNAMQTN NDKPIDEIRI IKATAN
