Reviewed,
UniProtKB/Swiss-Prot P28517 (CYPR_CALVI)
Last modified
October 13, 2009.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Peptidyl-prolyl cis-trans isomerase, rhodopsin-specific isozyme Short name=PPIase Short name=Rotamase EC=5.2.1.8 | ||
| Gene names |
| ||
| 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 | |
| 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 |
| Molecular function | Isomerase Rotamase |
| PTM | Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | protein folding Inferred from electronic annotation. Source: UniProtKB-KW response to stimulusInferred from electronic annotation. Source: UniProtKB-KW visual perceptionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| 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 | Potential | ||||||
| Domain | 29 – 187 | 159 | PPIase cyclophilin-type | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 67 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
| ||||||||||||||||||
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 | |
|---|---|
| HSSP | HSSP built from PDB template 1CYN based on UniProtKB P23284. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 5.2.1.8. 2654. |
Family and domain databases | |
| InterPro | IPR002130. PPIase_cyclophilin. [Graphical view] |
| Gene3D | G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit. |
| Pfam | PF00160. Pro_isomerase. 1 hit. [Graphical view] |
| PRINTS | PR00153. CSAPPISMRASE. |
| 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 |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

Clusters with


