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   03-AUG-2022, entry version 177.
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};
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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   PRIDE; P25007; -.
DR   DNASU; 32595; -.
DR   EnsemblMetazoa; FBtr0074238; FBpp0074017; FBgn0004432.
DR   GeneID; 32595; -.
DR   KEGG; dme:Dmel_CG9916; -.
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; 1403619at2759; -.
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   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 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; 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