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Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme (PPIase) (EC 5.2.1.8) (Rotamase)

 CYPR_DROME              Reviewed;         237 AA.
P15425; Q9VPV0;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
23-MAY-2018, entry version 159.
RecName: Full=Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme;
Short=PPIase;
EC=5.2.1.8;
AltName: Full=Rotamase;
Flags: Precursor;
Name=ninaA; ORFNames=CG3966;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Head;
PubMed=2493138; DOI=10.1038/338067a0;
Shieh B.-H., Stamnes M.A., Seavello S., Harris G.L., Zuker C.S.;
"The ninaA gene required for visual transduction in Drosophila encodes
a homologue of cyclosporin A-binding protein.";
Nature 338:67-70(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2664782; DOI=10.1073/pnas.86.14.5390;
Schneuwly S., Shortridge R.D., Larrivee D.C., Ono T., Ozaki M.,
Pak W.L.;
"Drosophila ninaA gene encodes an eye-specific cyclophilin
(cyclosporine A binding protein).";
Proc. Natl. Acad. Sci. U.S.A. 86:5390-5394(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND TRANSMEMBRANE
REGION.
PubMed=1707759; DOI=10.1016/0092-8674(91)90156-S;
Stamnes M.A., Shieh B.-H., Chuman L., Harris G.L., Zuker C.S.;
"The cyclophilin homolog ninaA is a tissue-specific integral membrane
protein required for the proper synthesis of a subset of Drosophila
rhodopsins.";
Cell 65:219-227(1991).
[6]
MUTAGENESIS.
PubMed=1644830;
Ondek B., Hardy R.W., Baker E.K., Stamnes M.A., Shieh B.-H.,
Zuker C.S.;
"Genetic dissection of cyclophilin function. Saturation mutagenesis of
the Drosophila cyclophilin homolog ninaA.";
J. Biol. Chem. 267:16460-16466(1992).
-!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
the cis-trans isomerization of proline imidic peptide bonds in
oligopeptides. Acts on the folding of rhodopsin RH1 and RH2 (but
not RH3) and is required for visual transduction.
{ECO:0000269|PubMed:1707759}.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:1707759};
Single-pass membrane protein {ECO:0000269|PubMed:1707759}.
-!- TISSUE SPECIFICITY: Expressed specifically in photoreceptor cells.
-!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
{ECO:0000305}.
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; X14769; CAA32877.1; -; Genomic_DNA.
EMBL; M22851; AAA28717.1; -; Genomic_DNA.
EMBL; AE014134; AAF51437.1; -; Genomic_DNA.
PIR; A33906; CYFFBE.
RefSeq; NP_476656.1; NM_057308.4.
UniGene; Dm.19760; -.
ProteinModelPortal; P15425; -.
SMR; P15425; -.
BioGrid; 59525; 11.
DIP; DIP-18923N; -.
IntAct; P15425; 2.
MINT; P15425; -.
STRING; 7227.FBpp0077688; -.
iPTMnet; P15425; -.
PaxDb; P15425; -.
PRIDE; P15425; -.
EnsemblMetazoa; FBtr0078023; FBpp0077688; FBgn0002936.
GeneID; 33271; -.
KEGG; dme:Dmel_CG3966; -.
CTD; 33271; -.
FlyBase; FBgn0002936; ninaA.
eggNOG; KOG0880; Eukaryota.
eggNOG; ENOG410Z0G4; LUCA.
InParanoid; P15425; -.
KO; K01802; -.
OMA; RIILCSA; -.
OrthoDB; EOG091G0BGL; -.
PhylomeDB; P15425; -.
GenomeRNAi; 33271; -.
PRO; PR:P15425; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0002936; -.
ExpressionAtlas; P15425; differential.
Genevisible; P15425; DM.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:FlyBase.
GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
GO; GO:0016018; F:cyclosporin A binding; IMP:FlyBase.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:FlyBase.
GO; GO:0006458; P:'de novo' protein folding; TAS:FlyBase.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:FlyBase.
GO; GO:0006491; P:N-glycan processing; IMP:FlyBase.
GO; GO:0007602; P:phototransduction; IMP:FlyBase.
GO; GO:0007603; P:phototransduction, visible light; IMP:FlyBase.
GO; GO:0006517; P:protein deglycosylation; IMP:FlyBase.
GO; GO:0016063; P:rhodopsin biosynthetic process; IMP:FlyBase.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
Gene3D; 2.40.100.10; -; 1.
InterPro; IPR029000; Cyclophilin-like_dom_sf.
InterPro; IPR024936; Cyclophilin-type_PPIase.
InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
PANTHER; PTHR11071; PTHR11071; 1.
Pfam; PF00160; Pro_isomerase; 1.
PRINTS; PR00153; CSAPPISMRASE.
SUPFAM; SSF50891; SSF50891; 1.
PROSITE; PS00170; CSA_PPIASE_1; 1.
PROSITE; PS50072; CSA_PPIASE_2; 1.
1: Evidence at protein level;
Complete proteome; Glycoprotein; Isomerase; Membrane;
Reference proteome; Rotamase; Sensory transduction; Signal;
Transmembrane; Transmembrane helix; Vision.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 237 Peptidyl-prolyl cis-trans isomerase,
rhodopsin-specific isozyme.
/FTId=PRO_0000025493.
TRANSMEM 205 225 Helical. {ECO:0000255}.
DOMAIN 30 190 PPIase cyclophilin-type.
{ECO:0000255|PROSITE-ProRule:PRU00156}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1707759}.
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


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