ID PPIA_DROME Reviewed; 227 AA. AC P25007; Q9VXH8; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2004, sequence version 2. DT 22-FEB-2023, entry version 179. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase; DE Short=PPIase; DE EC=5.2.1.8; DE AltName: Full=Cyclophilin; DE AltName: Full=Cyclosporin A-binding protein; DE AltName: Full=Rotamase; GN Name=Cyp1; Synonyms=Cyp-1; ORFNames=CG9916; 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 [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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-227. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A., RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-227. RX PubMed=1707759; DOI=10.1016/0092-8674(91)90156-s; RA Stamnes M.A., Shieh B.-H., Chuman L., Harris G.L., Zuker C.S.; RT "The cyclophilin homolog ninaA is a tissue-specific integral membrane RT protein required for the proper synthesis of a subset of Drosophila RT rhodopsins."; RL Cell 65:219-227(1991). RN [5] RP PROTEIN SEQUENCE OF 69-82. RC STRAIN=Vallecas; TISSUE=Wing imaginal disk; RX PubMed=8500545; DOI=10.1006/excr.1993.1141; RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J., RA Garcia-Bellido A.; RT "Identification of Drosophila wing imaginal disc proteins by two- RT dimensional gel analysis and microsequencing."; RL Exp. Cell Res. 206:220-226(1993). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC TISSUE=Embryo; RX PubMed=18327897; DOI=10.1021/pr700696a; RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; RT "Phosphoproteome analysis of Drosophila melanogaster embryos."; RL J. Proteome Res. 7:1675-1682(2008). CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the CC cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides. 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: Cytoplasm. CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB03701.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAQ22415.1; Type=Erroneous initiation; Evidence={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; AE014298; AAF48589.2; -; Genomic_DNA. DR EMBL; BT009946; AAQ22415.1; ALT_INIT; mRNA. DR EMBL; M62398; AAB03701.1; ALT_INIT; mRNA. DR PIR; B38388; B38388. DR RefSeq; NP_523366.2; NM_078642.4. DR AlphaFoldDB; P25007; -. DR SMR; P25007; -. DR BioGRID; 58935; 30. DR DIP; DIP-18774N; -. DR IntAct; P25007; 4. DR STRING; 7227.FBpp0074017; -. DR iPTMnet; P25007; -. DR PaxDb; P25007; -. DR DNASU; 32595; -. DR EnsemblMetazoa; FBtr0074238; FBpp0074017; FBgn0004432. DR GeneID; 32595; -. DR KEGG; dme:Dmel_CG9916; -. DR AGR; FB:FBgn0004432; -. DR CTD; 32595; -. DR FlyBase; FBgn0004432; Cyp1. DR VEuPathDB; VectorBase:FBgn0004432; -. DR eggNOG; KOG0865; Eukaryota. DR GeneTree; ENSGT00940000174900; -. DR HOGENOM; CLU_012062_4_3_1; -. DR InParanoid; P25007; -. DR OMA; CKGTVVN; -. DR OrthoDB; 339082at2759; -. DR PhylomeDB; P25007; -. DR BioGRID-ORCS; 32595; 0 hits in 3 CRISPR screens. DR GenomeRNAi; 32595; -. DR PRO; PR:P25007; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0004432; Expressed in eye disc (Drosophila) and 37 other tissues. DR ExpressionAtlas; P25007; baseline and differential. DR Genevisible; P25007; DM. DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase. DR GO; GO:0005829; C:cytosol; ISS:FlyBase. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IMP:FlyBase. DR GO; GO:0005634; C:nucleus; HDA:FlyBase. DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:FlyBase. DR GO; GO:0006457; P:protein folding; IBA:GO_Central. DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central. DR GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase. DR CDD; cd01926; cyclophilin_ABH_like; 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 PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1. DR PANTHER; PTHR11071:SF537; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1. DR Pfam; PF00160; Pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR SUPFAM; SSF50891; Cyclophilin-like; 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; Phosphoprotein; KW Reference proteome; Rotamase. FT CHAIN 1..227 FT /note="Peptidyl-prolyl cis-trans isomerase" FT /id="PRO_0000064123" FT DOMAIN 70..226 FT /note="PPIase cyclophilin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156" FT MOD_RES 158 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" SQ SEQUENCE 227 AA; 24666 MW; B6D832E1409C1F4D CRC64; MVSFCATLIR QFRHRSAAAF QIAESAILAN KSITLASSAC SVNRGQLQFG IQIVREYSKA SKMSTLPRVF FDMTADNEPL GRIVMELRSD VVPKTAENFR ALCTGEKGFG YKGSIFHRVI PNFMCQGGDF TNHNGTGGKS IYGNKFPDEN FELKHTGSGI LSMANAGANT NGSQFFICTV KTAWLDNKHV VFGEVVEGLD VVKKIESYGS QSGKTSKKII VANSGSL //