O65039 (CYSEP_RICCO) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 72.
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: Vignain EC=3.4.22.- Alternative name(s): Cysteine endopeptidase | ||
| Gene names |
| ||
| Organism | Ricinus communis (Castor bean) [Complete proteome] | ||
| Taxonomic identifier | 3988 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Euphorbiaceae › Acalyphoideae › Acalypheae › Ricinus![]() |
Protein attributes
| Sequence length | 360 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 | Involved in programmed cell death. |
| Catalytic activity | Pronounced preference for hydrophobic residues in the P2 position and no obvious preference in the P1 position of the cleavage site. Accepts proline at the P1 and P1' positions. |
| Enzyme regulation | Low pH triggers activation of the protease and removal of the propeptide and the KDEL motif. |
| Subcellular location | Cytoplasmic vesicle. Note: The pro-endopeptidase accumulates in the ricinosomes. Ref.2 |
| Developmental stage | Released during the final stage of cellular desintegration in the senescing endosperm of germinating bean. |
| Post-translational modification | The potential N-glycosylation site at Asn-115 is not glycosylated. |
| Miscellaneous | The pro-endopeptidase goes directly from the ER lumen to the ricinosome, and the secretory pathway via the Golgi apparatus is not involved in the ricinosome biogenesis. |
| Sequence similarities | Belongs to the peptidase C1 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasmic vesicle |
| Domain | Signal |
| Molecular function | Hydrolase Protease Thiol protease |
| PTM | Disulfide bond |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | cysteine-type peptidase 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 – 20 | 20 | |||||||||||||||||||||||||||||||||||||||||
| Propeptide | 21 – 124 | 104 | Activation peptide | PRO_0000026442 | |||||||||||||||||||||||||||||||||||||||
| Chain | 125 – 353 | 229 | Vignain | PRO_0000026443 | |||||||||||||||||||||||||||||||||||||||
| Propeptide | 354 – 360 | 7 | PRO_0000026444 | ||||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||
| Region | 357 – 360 | 4 | Prevents secretion from ER By similarity | ||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||
| Active site | 150 | 1 | |||||||||||||||||||||||||||||||||||||||||
| Active site | 286 | 1 | |||||||||||||||||||||||||||||||||||||||||
| Active site | 307 | 1 | |||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 147 ↔ 189 | ||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 181 ↔ 222 | ||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 280 ↔ 332 | ||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||
| Turn | 132 – 136 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 146 – 148 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 150 – 167 | 18 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 175 – 181 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 194 – 204 | 11 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 210 – 212 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 224 – 227 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 236 – 239 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 245 – 254 | 10 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 257 – 261 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 266 – 269 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 273 – 276 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 286 – 295 | 10 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 301 – 306 | 6 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 318 – 322 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 331 – 333 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 339 – 342 | 4 | |||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "A cysteine endopeptidase with a C-terminal KDEL motif isolated from castor bean endosperm is a marker enzyme for the ricinosome, a putative lytic compartment." Schmid M., Simpson D., Kalousek F., Gietl C. Planta 206:466-475(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Endosperm. |
| [2] | "The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum." Schmid M., Simpson D.J., Sarioglu H., Lottspeich F., Gietl C. Proc. Natl. Acad. Sci. U.S.A. 98:5353-5358(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 337-360, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION. |
| [3] | "The 2.0 A crystal structure and substrate specificity of the KDEL-tailed cysteine endopeptidase functioning in programmed cell death of Ricinus communis endosperm." Than M.E., Helm M., Simpson D.J., Lottspeich F., Huber R., Gietl C. J. Mol. Biol. 336:1103-1116(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 125-350 IN COMPLEX WITH CHLOROMETHYLKETONE (CMK) INHIBITOR. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF050756 mRNA. Translation: AAC62396.1. | ||||||||||||
| PIR | T08122. | ||||||||||||
| RefSeq | XP_002511277.1. XM_002511231.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | O65039. | ||||||||||||
| SMR | O65039. Positions 125-350. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| MEROPS | C01.010. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 8278243. | ||||||||||||
| KEGG | rcu:RCOM_1507820. | ||||||||||||
Phylogenomic databases | |||||||||||||
| KO | K16292. | ||||||||||||
| ProtClustDB | CLSN2689970. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR025661. Pept_asp_AS. IPR000169. Pept_cys_AS. IPR025660. Pept_his_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. IPR013201. Prot_inhib_I29. [Graphical view] | ||||||||||||
| PANTHER | PTHR12411. PTHR12411. 1 hit. | ||||||||||||
| Pfam | PF08246. Inhibitor_I29. 1 hit. PF00112. Peptidase_C1. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00705. PAPAIN. | ||||||||||||
| SMART | SM00848. Inhibitor_I29. 1 hit. SM00645. Pept_C1. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS00014. ER_TARGET. 1 hit. PS00640. THIOL_PROTEASE_ASN. 1 hit. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | O65039. | ||||||||||||
Entry information
| Entry name | CYSEP_RICCO | ||||||||
| Accession | Primary (citable) accession number: O65039 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
