CYPR_DROME
ID CYPR_DROME Reviewed; 237 AA.
AC P15425; Q9VPV0;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=ninaA; ORFNames=CG3966;
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 [GENOMIC DNA].
RC TISSUE=Head;
RX PubMed=2493138; DOI=10.1038/338067a0;
RA Shieh B.-H., Stamnes M.A., Seavello S., Harris G.L., Zuker C.S.;
RT "The ninaA gene required for visual transduction in Drosophila encodes a
RT homologue of cyclosporin A-binding protein.";
RL Nature 338:67-70(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2664782; DOI=10.1073/pnas.86.14.5390;
RA Schneuwly S., Shortridge R.D., Larrivee D.C., Ono T., Ozaki M., Pak W.L.;
RT "Drosophila ninaA gene encodes an eye-specific cyclophilin (cyclosporine A
RT binding protein).";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5390-5394(1989).
RN [3]
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 [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND TRANSMEMBRANE REGION.
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 [6]
RP MUTAGENESIS.
RX PubMed=1644830; DOI=10.1016/s0021-9258(18)42025-x;
RA Ondek B., Hardy R.W., Baker E.K., Stamnes M.A., Shieh B.-H., Zuker C.S.;
RT "Genetic dissection of cyclophilin function. Saturation mutagenesis of the
RT Drosophila cyclophilin homolog ninaA.";
RL J. Biol. Chem. 267:16460-16466(1992).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Acts on the folding of rhodopsin RH1 and RH2 (but not
CC RH3) and is required for visual transduction.
CC {ECO:0000269|PubMed:1707759}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:1707759}; Single-
CC pass membrane protein {ECO:0000269|PubMed:1707759}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in photoreceptor cells.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; X14769; CAA32877.1; -; Genomic_DNA.
DR EMBL; M22851; AAA28717.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51437.1; -; Genomic_DNA.
DR PIR; A33906; CYFFBE.
DR RefSeq; NP_476656.1; NM_057308.4.
DR AlphaFoldDB; P15425; -.
DR SMR; P15425; -.
DR BioGRID; 59525; 11.
DR DIP; DIP-18923N; -.
DR IntAct; P15425; 2.
DR MINT; P15425; -.
DR STRING; 7227.FBpp0077688; -.
DR GlyGen; P15425; 1 site.
DR iPTMnet; P15425; -.
DR PaxDb; P15425; -.
DR DNASU; 33271; -.
DR EnsemblMetazoa; FBtr0078023; FBpp0077688; FBgn0002936.
DR GeneID; 33271; -.
DR KEGG; dme:Dmel_CG3966; -.
DR CTD; 33271; -.
DR FlyBase; FBgn0002936; ninaA.
DR VEuPathDB; VectorBase:FBgn0002936; -.
DR eggNOG; KOG0880; Eukaryota.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; P15425; -.
DR OMA; AWIKATC; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; P15425; -.
DR BioGRID-ORCS; 33271; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33271; -.
DR PRO; PR:P15425; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0002936; Expressed in head capsule and 8 other tissues.
DR ExpressionAtlas; P15425; differential.
DR Genevisible; P15425; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:FlyBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016018; F:cyclosporin A binding; IMP:FlyBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0006458; P:'de novo' protein folding; TAS:FlyBase.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:FlyBase.
DR GO; GO:0006491; P:N-glycan processing; IMP:FlyBase.
DR GO; GO:0006517; P:protein deglycosylation; IMP: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:0016063; P:rhodopsin biosynthetic process; IMP:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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 Glycoprotein; Isomerase; Membrane; Reference proteome; Rotamase;
KW Sensory transduction; Signal; Transmembrane; Transmembrane helix; Vision.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..237
FT /note="Peptidyl-prolyl cis-trans isomerase, rhodopsin-
FT specific isozyme"
FT /id="PRO_0000025493"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 30..190
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1707759"
SQ SEQUENCE 237 AA; 26351 MW; 1BF3CD01C31119B4 CRC64;
MKSLLNRIIL CSAFLAVASG LSFTVTSRIY MDVKHNKKPV GRITFGLFGK LAPKTVANFR
HICLRGINGT SYVGSRFHRV VDRFLVQGGD IVNGDGTGSI SIYGDYFPDE DKALAVEHNR
PGYLGMANRG PDTNGCQFYV TTVGAKWLDG KHTVFGKVLE GMDTIYAIED VKTDTDDFPV
EPVVISNCGE IPTEQFEFYP DDFNILGWIK AAGLPVTSSF CVLLIFHYFF RQLNMYC
