Q09734 (MIP_TRYCR) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 65.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Macrophage infectivity potentiator EC=5.2.1.8 Alternative name(s): Peptidyl-prolyl cis-trans isomerase Short name=PPIase Rotamase | ||
| Gene names |
| ||
| Organism | Trypanosoma cruzi | ||
| Taxonomic identifier | 5693 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma › Schizotrypanum![]() |
Protein attributes
| Sequence length | 196 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 | Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity. |
| Catalytic activity | Peptidylproline (omega=180) = peptidylproline (omega=0). |
| Enzyme regulation | Strongly inhibited by FK506 and L-685,818. |
| Subcellular location | |
| Sequence similarities | Belongs to the FKBP-type PPIase family. Contains 1 PPIase FKBP-type domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Virulence |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Isomerase Rotamase |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological_process | pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW protein foldingInferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerizationInferred from electronic annotation. Source: GOC |
| Cellular_component | extracellular space 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 – 29 | 29 | Potential | |||||||||||||||||||||||||||||||||||
| Chain | 30 – 196 | 167 | Macrophage infectivity potentiator | PRO_0000025535 | ||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||
| Domain | 85 – 171 | 87 | PPIase FKBP-type | |||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||
| Helix | 36 – 57 | 22 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 61 – 63 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 69 – 74 | 6 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 88 – 95 | 8 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 101 – 104 | 4 | ||||||||||||||||||||||||||||||||||||
| Helix | 105 – 108 | 4 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 112 – 114 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 116 – 118 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 121 – 127 | 7 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 135 – 140 | 6 | ||||||||||||||||||||||||||||||||||||
| Helix | 142 – 144 | 3 | ||||||||||||||||||||||||||||||||||||
| Turn | 145 – 149 | 5 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 151 – 155 | 5 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 161 – 170 | 10 | ||||||||||||||||||||||||||||||||||||
| Helix | 171 – 173 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 179 – 191 | 13 | ||||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Secretion by Trypanosoma cruzi of a peptidyl-prolyl cis-trans isomerase involved in cell infection." Moro A., Ruiz-Cabello F., Fernandez-Cano A., Stock R.P., Gonzalez A. EMBO J. 14:2483-2490(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Y. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X69655 Genomic DNA. Translation: CAA49346.1. | ||||||||||||
| PIR | S55332. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q09734. | ||||||||||||
| SMR | Q09734. Positions 33-192. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR023566. PPIase_FKBP. IPR001179. PPIase_FKBP_dom. [Graphical view] | ||||||||||||
| PANTHER | PTHR10516. PTHR10516. 1 hit. | ||||||||||||
| Pfam | PF00254. FKBP_C. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS50059. FKBP_PPIASE. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | Q09734. | ||||||||||||
Entry information
| Entry name | MIP_TRYCR | ||||||||
| Accession | Primary (citable) accession number: Q09734 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
