Reviewed,
UniProtKB/Swiss-Prot Q9LEK8 (PIN1_DIGLA)
Last modified
June 16, 2009.
Version 36.
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 1 EC=5.2.1.8 Alternative name(s): Rotamase Pin1 PPIase Pin1 DlPar13 | ||
| Gene names |
| ||
| Organism | Digitalis lanata (Foxglove) | ||
| Taxonomic identifier | 49450 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Lamiales › Plantaginaceae › Digitalideae › Digitalis |
Protein attributes
| Sequence length | 118 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Prolyl cis/trans isomerase with specificity for phospho-Ser-Pro bonds. Ref.1 |
| Catalytic activity | Peptidylproline (omega=180) = peptidylproline (omega=0). |
| Enzyme regulation | Inhibited in vitro by juglone. |
| Subcellular location | |
| Tissue specificity | Expressed in roots, stems, leaves, flowers and seedlings. Ref.1 |
| Post-translational modification | The N-terminus is blocked. |
| Miscellaneous | Like all plant Pin1-type PPIases, do not contain the N-terminal WW domain found in other eukaryotic parvulins, but contains a four-amino acid insertion next to the phospho-specific recognition site of the active site. These extra amino acids may be important for mediating the substrate interaction of plant enzymes. Three amino acid residues (P79S, E91D and A95G) differ when compared with the partial sequence of purified protein. The existence of two or more genes coding for this protein is not exluded. |
| Sequence similarities | Belongs to the ppiC/parvulin rotamase family. Contains 1 PpiC domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Nucleus |
| Molecular function | Isomerase Rotamase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | protein folding Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleusInferred 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)
Sequences
References
| [1] | "Functional replacement of the essential ess1 in yeast by the plant parvulin DlPar13." Metzner M., Stoller G., Ruecknagel P., Lu K.P., Fischer G., Luckner M., Kuellertz G. J. Biol. Chem. 276:13524-13529(2001) [PubMed: 11118437] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION. Strain: cv. VIII. |
Cross-references
Sequence databases | |
|---|---|
| AJ133755 mRNA. Translation: CAB94994.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1J6Y based on UniProtKB Q9SL42. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 5.2.1.8. 255268. |
Family and domain databases | |
| InterPro | IPR000297. PPIase_PpiC. [Graphical view] |
| Pfam | PF00639. Rotamase. 1 hit. [Graphical view] |
| PROSITE | PS01096. PPIC_PPIASE_1. 1 hit. PS50198. PPIC_PPIASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PIN1_DIGLA | ||||||||
| Accession | Primary (citable) accession number: Q9LEK8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


