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Protein

Vignain

Gene

CYSEP

Organism
Ricinus communis (Castor bean)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei1501
Active sitei2861
Active sitei3071

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.B1. 1204.

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
PropeptideiPRO_000002644221 – 124Activation peptideAdd BLAST104
ChainiPRO_0000026443125 – 353VignainAdd BLAST229
PropeptideiPRO_0000026444354 – 3607

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1360
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni132 – 136Combined sources5
Beta strandi146 – 148Combined sources3
Helixi150 – 167Combined sources18
Helixi175 – 181Combined sources7
Helixi194 – 204Combined sources11
Turni210 – 212Combined sources3
Helixi224 – 227Combined sources4
Beta strandi236 – 239Combined sources4
Helixi245 – 254Combined sources10
Beta strandi257 – 261Combined sources5
Helixi266 – 269Combined sources4
Beta strandi273 – 276Combined sources4
Beta strandi286 – 295Combined sources10
Beta strandi301 – 306Combined sources6
Beta strandi318 – 322Combined sources5
Helixi331 – 333Combined sources3
Beta strandi339 – 342Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S4VX-ray2.00A/B125-353[»]
ProteinModelPortaliO65039.
SMRiO65039.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO65039.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni357 – 360Prevents secretion from ERBy similarity4

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:
EMBLi
GenBanki
DDBJi
Links Updated
AF050756 mRNA. Translation: AAC62396.1.
PIRiT08122.
RefSeqiNP_001310675.1. NM_001323746.1.

Genome annotation databases

GeneIDi8278243.
KEGGircu:8278243.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF050756 mRNA. Translation: AAC62396.1.
PIRiT08122.
RefSeqiNP_001310675.1. NM_001323746.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S4VX-ray2.00A/B125-353[»]
ProteinModelPortaliO65039.
SMRiO65039.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC01.010.

Proteomic databases

PRIDEiO65039.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8278243.
KEGGircu:8278243.

Phylogenomic databases

InParanoidiO65039.
KOiK16292.

Enzyme and pathway databases

BRENDAi3.4.22.B1. 1204.

Miscellaneous databases

EvolutionaryTraceiO65039.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 87 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.