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O65039 (CYSEP_RICCO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vignain

EC=3.4.22.-
Alternative name(s):
Cysteine endopeptidase
Gene names
Name:CYSEP
OrganismRicinus communis (Castor bean)
Taxonomic identifier3988 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentCytoplasmic vesicle
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Propeptide21 – 124104Activation peptide
PRO_0000026442
Chain125 – 353229Vignain
PRO_0000026443
Propeptide354 – 3607
PRO_0000026444

Regions

Region357 – 3604Prevents secretion from ER By similarity

Sites

Active site1501
Active site2861
Active site3071

Amino acid modifications

Disulfide bond147 ↔ 189
Disulfide bond181 ↔ 222
Disulfide bond280 ↔ 332

Secondary structure

................................... 360
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O65039 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 6EC61C1A010FE8A1

FASTA36040,111
        10         20         30         40         50         60 
MQKFILLALS LALVLAITES FDFHEKELES EESLWGLYER WRSHHTVSRS LHEKQKRFNV 

        70         80         90        100        110        120 
FKHNAMHVHN ANKMDKPYKL KLNKFADMTN HEFRNTYSGS KVKHHRMFRG GPRGNGTFMY 

       130        140        150        160        170        180 
EKVDTVPASV DWRKKGAVTS VKDQGQCGSC WAFSTIVAVE GINQIKTNKL VSLSEQELVD 

       190        200        210        220        230        240 
CDTDQNQGCN GGLMDYAFEF IKQRGGITTE ANYPYEAYDG TCDVSKENAP AVSIDGHENV 

       250        260        270        280        290        300 
PENDENALLK AVANQPVSVA IDAGGSDFQF YSEGVFTGSC GTELDHGVAI VGYGTTIDGT 

       310        320        330        340        350        360 
KYWTVKNSWG PEWGEKGYIR MERGISDKEG LCGIAMEASY PIKKSSNNPS GIKSSPKDEL 

« Hide

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.
PIRT08122.
RefSeqXP_002511277.1. XM_002511231.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S4VX-ray2.00A/B125-353[»]
ProteinModelPortalO65039.
SMRO65039. Positions 125-350.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC01.010.

Proteomic databases

PRIDEO65039.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8278243.
KEGGrcu:RCOM_1507820.

Phylogenomic databases

KOK16292.
ProtClustDBCLSN2689970.

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00014. ER_TARGET. 1 hit.
PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO65039.

Entry information

Entry nameCYSEP_RICCO
AccessionPrimary (citable) accession number: O65039
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: August 1, 1998
Last modified: February 19, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references