P15425 (CYPR_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	237 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Membrane
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Isomerase Rotamase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	'de novo' protein folding Traceable author statement. Source: FlyBase apoptosis in response to endoplasmic reticulum stress Inferred from mutant phenotype. Source: FlyBase phototransduction Inferred from physical interaction. Source: FlyBase rhodopsin biosynthetic process Inferred from mutant phenotype. Source: FlyBase transport Traceable author statement. Source: FlyBase visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasmic membrane-bounded vesicle Inferred from direct assay. Source: FlyBase endoplasmic reticulum lumen Inferred from direct assay. Source: FlyBase integral to membrane Inferred from direct assay Ref.5. Source: FlyBase membrane fraction Inferred from direct assay Ref.5. Source: FlyBase
Molecular function	cyclosporin A binding Inferred from mutant phenotype Ref.1. Source: FlyBase peptidyl-prolyl cis-trans isomerase activity Traceable author statement. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 237	217	Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme		PRO_0000025493
Regions
	Transmembrane	205 – 225	21	Helical; Potential
	Domain	30 – 190	161	PPIase cyclophilin-type
Amino acid modifications
	Glycosylation	68	1	N-linked (GlcNAc...)

Sequences

	Sequence		Length	Mass (Da)
	P15425 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 1BF3CD01C31119B4	FASTA	237	26,351
	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

References

	« Hide 'large scale' referencesShow '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: 2493138] [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: 2664782] [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. , 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: 10731132] [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. , 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: 12537572] [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: 1707759] [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: 1644830] [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.
PIR	CYFFBE. A33906.
RefSeq	NP_476656.1. NM_057308.3.
UniGene	Dm.19760.
3D structure databases
ProteinModelPortal	P15425.
SMR	P15425. Positions 22-191.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-18923N.
IntAct	P15425. 1 interaction.
MINT	MINT-306426.
STRING	P15425.
Proteomic databases
PRIDE	P15425.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0078023; FBpp0077688; FBgn0002936.
GeneID	33271.
KEGG	dme:Dmel_CG3966.
Organism-specific databases
CTD	33271.
FlyBase	FBgn0002936. ninaA.
Phylogenomic databases
eggNOG	inNOG05692.
InParanoid	P15425.
OMA	TVANFRH.
OrthoDB	EOG42Z362.
PhylomeDB	P15425.
Gene expression databases
Bgee	P15425.
GermOnline	CG3966. Drosophila melanogaster.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
KO	K01802.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	782782.

Entry information

Entry name

CYPR_DROME

Accession

Primary (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:	January 25, 2012
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project