Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P28517 (CYPR_CALVI)

Last modified October 13, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Gene names
Name: NINAA
OrganismCalliphora vicina (Blue blowfly) (Calliphora erythrocephala)
Taxonomic identifier7373 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaOestroideaCalliphoridaeCalliphorinaeCalliphora

Protein attributes

Sequence length234 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processSensory transduction
Vision
   Cellular componentMembrane
   DomainSignal
Transmembrane
   Molecular functionIsomerase
Rotamase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processprotein 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 componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 234215Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme
PRO_0000025492

Regions

Transmembrane202 – 22221 Potential
Domain29 – 187159PPIase cyclophilin-type

Amino acid modifications

Glycosylation671N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P28517-1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 61992B951A8E5E19

FASTA23426,380
        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 

« Hide

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.

Cross-references

3D structure databases

HSSPHSSP built from PDB template 1CYN based on UniProtKB P23284.
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.2.1.8. 2654.

Family and domain databases

InterProIPR002130. PPIase_cyclophilin.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYPR_CALVI
AccessionPrimary (citable) accession number: P28517
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: October 13, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents