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P15425 (CYPR_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme
Short name=PPIase
EC=5.2.1.8
Alternative name(s):
Rotamase
Gene names
Name:ninaA
ORF Names:CG3966
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.5

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Subcellular location

Membrane; Single-pass membrane protein Ref.5.

Tissue specificity

Expressed specifically in photoreceptor cells.

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 237217Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme
PRO_0000025493

Regions

Transmembrane205 – 22521Helical; Potential
Domain30 – 190161PPIase cyclophilin-type

Amino acid modifications

Glycosylation681N-linked (GlcNAc...)

Sequences

Sequence LengthMass (Da)Tools
P15425 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 1BF3CD01C31119B4

FASTA23726,351
        10         20         30         40         50         60 
MKSLLNRIIL CSAFLAVASG LSFTVTSRIY MDVKHNKKPV GRITFGLFGK LAPKTVANFR 

        70         80         90        100        110        120 
HICLRGINGT SYVGSRFHRV VDRFLVQGGD IVNGDGTGSI SIYGDYFPDE DKALAVEHNR 

       130        140        150        160        170        180 
PGYLGMANRG PDTNGCQFYV TTVGAKWLDG KHTVFGKVLE GMDTIYAIED VKTDTDDFPV 

       190        200        210        220        230 
EPVVISNCGE IPTEQFEFYP DDFNILGWIK AAGLPVTSSF CVLLIFHYFF RQLNMYC

« Hide

References

« Hide 'large scale' references
[1]"The ninaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein."
Shieh B.-H., Stamnes M.A., Seavello S., Harris G.L., Zuker C.S.
Nature 338:67-70(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Head.
[2]"Drosophila ninaA gene encodes an eye-specific cyclophilin (cyclosporine A binding protein)."
Schneuwly S., Shortridge R.D., Larrivee D.C., Ono T., Ozaki M., Pak W.L.
Proc. Natl. Acad. Sci. U.S.A. 86:5390-5394(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The genome sequence of Drosophila melanogaster."
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. expand/collapse author list , 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.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins."
Stamnes M.A., Shieh B.-H., Chuman L., Harris G.L., Zuker C.S.
Cell 65:219-227(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, TRANSMEMBRANE REGION.
[6]"Genetic dissection of cyclophilin function. Saturation mutagenesis of the Drosophila cyclophilin homolog ninaA."
Ondek B., Hardy R.W., Baker E.K., Stamnes M.A., Shieh B.-H., Zuker C.S.
J. Biol. Chem. 267:16460-16466(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X14769 Genomic DNA. Translation: CAA32877.1.
M22851 Genomic DNA. Translation: AAA28717.1.
AE014134 Genomic DNA. Translation: AAF51437.1.
PIRCYFFBE. A33906.
RefSeqNP_476656.1. NM_057308.4.
UniGeneDm.19760.

3D structure databases

ProteinModelPortalP15425.
SMRP15425. Positions 25-191.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-18923N.
IntActP15425. 1 interaction.
MINTMINT-306426.

Proteomic databases

PaxDbP15425.
PRIDEP15425.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0078023; FBpp0077688; FBgn0002936.
GeneID33271.
KEGGdme:Dmel_CG3966.

Organism-specific databases

CTD33271.
FlyBaseFBgn0002936. ninaA.

Phylogenomic databases

eggNOGCOG0652.
GeneTreeENSGT00670000097658.
InParanoidP15425.
KOK01802.
OMATVANFRH.
OrthoDBEOG42Z362.
PhylomeDBP15425.

Gene expression databases

BgeeP15425.
GermOnlineCG3966. Drosophila melanogaster.

Family and domain databases

InterProIPR002130. Cyclophilin-like_PPIase_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. CSA_PPIase. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi33271.
NextBio782782.

Entry information

Entry nameCYPR_DROME
AccessionPrimary (citable) accession number: P15425
Secondary accession number(s): Q9VPV0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents