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O65039

- CYSEP_RICCO

UniProt

O65039 - CYSEP_RICCO

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Protein

Vignain

Gene

CYSEP

Organism
Ricinus communis (Castor bean)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in programmed cell death.

Catalytic activityi

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 regulationi

Low pH triggers activation of the protease and removal of the propeptide and the KDEL motif.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei150 – 1501
Active sitei286 – 2861
Active sitei307 – 3071

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Protein family/group databases

MEROPSiC01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Vignain (EC:3.4.22.-)
Alternative name(s):
Cysteine endopeptidase
Gene namesi
Name:CYSEP
OrganismiRicinus communis (Castor bean)
Taxonomic identifieri3988 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

Subcellular locationi

Cytoplasmic vesicle 1 Publication
Note: The pro-endopeptidase accumulates in the ricinosomes.

GO - Cellular componenti

  1. cytoplasmic vesicle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Propeptidei21 – 124104Activation peptidePRO_0000026442Add
BLAST
Chaini125 – 353229VignainPRO_0000026443Add
BLAST
Propeptidei354 – 3607PRO_0000026444

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi147 ↔ 189
Disulfide bondi181 ↔ 222
Disulfide bondi280 ↔ 332

Post-translational modificationi

The potential N-glycosylation site at Asn-115 is not glycosylated.

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiO65039.

Expressioni

Developmental stagei

Released during the final stage of cellular desintegration in the senescing endosperm of germinating bean.

Structurei

Secondary structure

1
360
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni132 – 1365
Beta strandi146 – 1483
Helixi150 – 16718
Helixi175 – 1817
Helixi194 – 20411
Turni210 – 2123
Helixi224 – 2274
Beta strandi236 – 2394
Helixi245 – 25410
Beta strandi257 – 2615
Helixi266 – 2694
Beta strandi273 – 2764
Beta strandi286 – 29510
Beta strandi301 – 3066
Beta strandi318 – 3225
Helixi331 – 3333
Beta strandi339 – 3424

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S4VX-ray2.00A/B125-353[»]
ProteinModelPortaliO65039.
SMRiO65039. Positions 125-350.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO65039.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni357 – 3604Prevents secretion from ERBy similarity

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiO65039.
KOiK16292.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O65039-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQKFILLALS LALVLAITES FDFHEKELES EESLWGLYER WRSHHTVSRS
60 70 80 90 100
LHEKQKRFNV FKHNAMHVHN ANKMDKPYKL KLNKFADMTN HEFRNTYSGS
110 120 130 140 150
KVKHHRMFRG GPRGNGTFMY EKVDTVPASV DWRKKGAVTS VKDQGQCGSC
160 170 180 190 200
WAFSTIVAVE GINQIKTNKL VSLSEQELVD CDTDQNQGCN GGLMDYAFEF
210 220 230 240 250
IKQRGGITTE ANYPYEAYDG TCDVSKENAP AVSIDGHENV PENDENALLK
260 270 280 290 300
AVANQPVSVA IDAGGSDFQF YSEGVFTGSC GTELDHGVAI VGYGTTIDGT
310 320 330 340 350
KYWTVKNSWG PEWGEKGYIR MERGISDKEG LCGIAMEASY PIKKSSNNPS
360
GIKSSPKDEL
Length:360
Mass (Da):40,111
Last modified:August 1, 1998 - v1
Checksum:i6EC61C1A010FE8A1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF050756 mRNA. Translation: AAC62396.1.
PIRiT08122.
RefSeqiXP_002511277.1. XM_002511231.1.

Genome annotation databases

GeneIDi8278243.
KEGGircu:RCOM_1507820.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF050756 mRNA. Translation: AAC62396.1 .
PIRi T08122.
RefSeqi XP_002511277.1. XM_002511231.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1S4V X-ray 2.00 A/B 125-353 [» ]
ProteinModelPortali O65039.
SMRi O65039. Positions 125-350.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C01.010.

Proteomic databases

PRIDEi O65039.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 8278243.
KEGGi rcu:RCOM_1507820.

Phylogenomic databases

InParanoidi O65039.
KOi K16292.

Miscellaneous databases

EvolutionaryTracei O65039.

Family and domain databases

InterProi 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 ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
Pfami PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view ]
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCYSEP_RICCO
AccessioniPrimary (citable) accession number: O65039
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: August 1, 1998
Last modified: October 29, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3