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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...

GO - Biological processi

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

    GO - Cellular componenti

    1. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasmic vesicle

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020
    Add
    BLAST
    Propeptidei21 – 124104Activation peptide
    PRO_0000026442Add
    BLAST
    Chaini125 – 353229Vignain
    PRO_0000026443Add
    BLAST
    Propeptidei354 – 3607
    PRO_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

    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.

    Miscellaneous databases

    EvolutionaryTraceiO65039.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the peptidase C1 family.

    Keywords - Domaini

    Signal

    Phylogenomic databases

    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

    MQKFILLALS LALVLAITES FDFHEKELES EESLWGLYER WRSHHTVSRS    50
    LHEKQKRFNV FKHNAMHVHN ANKMDKPYKL KLNKFADMTN HEFRNTYSGS 100
    KVKHHRMFRG GPRGNGTFMY EKVDTVPASV DWRKKGAVTS VKDQGQCGSC 150
    WAFSTIVAVE GINQIKTNKL VSLSEQELVD CDTDQNQGCN GGLMDYAFEF 200
    IKQRGGITTE ANYPYEAYDG TCDVSKENAP AVSIDGHENV PENDENALLK 250
    AVANQPVSVA IDAGGSDFQF YSEGVFTGSC GTELDHGVAI VGYGTTIDGT 300
    KYWTVKNSWG PEWGEKGYIR MERGISDKEG LCGIAMEASY PIKKSSNNPS 350
    GIKSSPKDEL 360
    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...

    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

    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: May 14, 2014
    This is version 75 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

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