ID PPIE_DROME Reviewed; 300 AA.
AC Q9V3G3;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 182.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase E;
DE Short=PPIase E;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin 33;
DE AltName: Full=Cyclophilin E;
DE AltName: Full=Rotamase E;
GN Name=cyp33; ORFNames=CG4886;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11976948; DOI=10.1007/s00427-002-0213-8;
RA Anderson M., Fair K., Amero S., Nelson S., Harte P.J., Diaz M.O.;
RT "A new family of cyclophilins with an RNA recognition motif that interact
RT with members of the trx/MLL protein family in Drosophila and human cells.";
RL Dev. Genes Evol. 212:107-113(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Combines RNA-binding and PPIase activities (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 -!- INTERACTION:
CC Q9V3G3; P20659: trx; NbExp=2; IntAct=EBI-128445, EBI-591327;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase E
CC subfamily. {ECO:0000305}.
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DR EMBL; AF182826; AAF01031.1; -; mRNA.
DR EMBL; AE013599; AAF57839.1; -; Genomic_DNA.
DR EMBL; AY061421; AAL28969.1; -; mRNA.
DR RefSeq; NP_523773.1; NM_079049.4.
DR AlphaFoldDB; Q9V3G3; -.
DR SMR; Q9V3G3; -.
DR BioGRID; 62673; 3.
DR DIP; DIP-21959N; -.
DR IntAct; Q9V3G3; 3.
DR STRING; 7227.FBpp0086101; -.
DR PaxDb; 7227-FBpp0086101; -.
DR DNASU; 36984; -.
DR EnsemblMetazoa; FBtr0086945; FBpp0086101; FBgn0028382.
DR GeneID; 36984; -.
DR KEGG; dme:Dmel_CG4886; -.
DR UCSC; CG4886-RA; d. melanogaster.
DR AGR; FB:FBgn0028382; -.
DR CTD; 36984; -.
DR FlyBase; FBgn0028382; cyp33.
DR VEuPathDB; VectorBase:FBgn0028382; -.
DR eggNOG; KOG0111; Eukaryota.
DR GeneTree; ENSGT00940000165717; -.
DR HOGENOM; CLU_012062_27_0_1; -.
DR InParanoid; Q9V3G3; -.
DR OMA; KIVIYAC; -.
DR OrthoDB; 339082at2759; -.
DR PhylomeDB; Q9V3G3; -.
DR Reactome; R-DME-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-DME-6782135; Dual incision in TC-NER.
DR Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9V3G3; -.
DR BioGRID-ORCS; 36984; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36984; -.
DR PRO; PR:Q9V3G3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0028382; Expressed in eye disc (Drosophila) and 33 other cell types or tissues.
DR Genevisible; Q9V3G3; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0000974; C:Prp19 complex; IDA:FlyBase.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR CDD; cd01926; cyclophilin_ABH_like; 1.
DR CDD; cd12347; RRM_PPIE; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR016304; PPIE.
DR InterPro; IPR034168; PPIE_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF001475; PPI_cyclophilin_E; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Isomerase; Nucleus; Reference proteome; RNA-binding; Rotamase.
FT CHAIN 1..300
FT /note="Peptidyl-prolyl cis-trans isomerase E"
FT /id="PRO_0000064159"
FT DOMAIN 6..84
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 142..298
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 300 AA; 33276 MW; CEAC7156EE8632D6 CRC64;
MSNDKRTIYV GGLADEVTER LLNNAFIPFG DIADIQMPAD YESQRHRGFA FIEYEQSEDA
AAAIDNMNDS ELCGRTIRVN LAKPVRVKED SFKPIWADDD WLQKHAGATL QPEGEPEAEK
VETPSTGPAV IEKAEKRNPQ VFFDIRIGGN DAGRIVMLLR ADVVPKTAEN FRQLCTHEQG
YGYKGCSFHR VIPEFMCQGG DFTNNNGTGG KSIYGKKFND ENFNLKHNSF GTLSMANSGA
NTNGSQFFIC TTKTDWLDNK HVVFGHVISG AEVVRKMERC GSKSGTPSQK IVIYSCGELK
//
