P28517 (CYPR_CALVI) 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

Organism

Calliphora vicina (Blue blowfly) (Calliphora erythrocephala)

Taxonomic identifier

7373 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Oestroidea › Calliphoridae › Calliphorinae › Calliphora

Protein attributes

Sequence length	234 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subcellular location	Membrane; Single-pass membrane protein.
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
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW response to stimulus Inferred from electronic annotation. Source: UniProtKB-KW visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 234	215	Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme		PRO_0000025492
Regions
	Transmembrane	202 – 222	21	Helical; Potential
	Domain	29 – 187	159	PPIase cyclophilin-type
Amino acid modifications
	Glycosylation	67	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P28517 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 61992B951A8E5E19	FASTA	234	26,380
	10 20 30 40 50 60 MNILKILILL ELIYTCVSGL SFTVTSKIYM DVKHQKKPLG RIVFGLFGKR APKTVTNFRH 70 80 90 100 110 120 ICLRGINGTT YVGSEFHRVI SRFLIQGGDI VNNDGTGSTS IYGDFFQDEA LDVEHLRPGY 130 140 150 160 170 180 LGMANRGPDT NGCQFYVTTV AAQWLNGKHT VFGKVIEGMD TVYAIEDVKT DTDDHPIDPV 190 200 210 220 230 IIVNCGEMPT EPYEFYPDDF SILGWIKAAG LPFCSSFIVL MIFHYFFRQL NMYC

References

[1]	"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: NUCLEOTIDE SEQUENCE.
+	Additional computationally mapped references.

Cross-references

3D structure databases
ProteinModelPortal	P28517.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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.
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...

Entry information

Entry name

CYPR_CALVI

Accession

Primary (citable) accession number: P28517

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)