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P25803

- CYSEP_PHAVU

UniProt

P25803 - CYSEP_PHAVU

Protein

Vignain

Gene
N/A
Organism
Phaseolus vulgaris (Kidney bean) (French bean)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Thought to be involved in the hydrolysis of stored seed proteins.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei152 – 1521By similarity
    Active sitei288 – 2881By similarity
    Active sitei309 – 3091By similarity

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: UniProtKB-KW

    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):
    Bean endopeptidase
    Cysteine proteinase EP-C1
    OrganismiPhaseolus vulgaris (Kidney bean) (French bean)
    Taxonomic identifieri3885 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 131111Activation peptideSequence AnalysisPRO_0000026440Add
    BLAST
    Chaini132 – 362231VignainPRO_0000026441Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi346 – 3461N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein, Zymogen

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliP25803.
    SMRiP25803. Positions 127-352.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi359 – 3624Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    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.

    P25803-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATKKLLWVV LSFSLVLGVA NSFDFHDKDL ASEESLWDLY ERWRSHHTVS    50
    RSLGEKHKRF NVFKANLMHV HNTNKMDKPY KLKLNKFADM TNHEFRSTYA 100
    GSKVNHPRMF RGTPHENGAF MYEKVVSVPP SVDWRKKGAV TDVKDQGQCG 150
    SCWAFSTVVA VEGINQIKTN KLVALSEQEL VDCDKEENQG CNGGLMESAF 200
    EFIKQKGGIT TESNYPYKAQ EGTCDASKVN DLAVSIDGHE NVPANDEDAL 250
    LKAVANQPVS VAIDAGGSDF QFYSEGVFTG DCSTDLNHGV AIVGYGTTVD 300
    GTNYWIVRNS WGPEWGEHGY IRMQRNISKK EGLCGIAMLP SYPIKNSSDN 350
    PTGSFSSPKD EL 362
    Length:362
    Mass (Da):40,212
    Last modified:June 1, 1994 - v2
    Checksum:i9AAF24A557FAF806
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071P → H in CAA40073. (PubMed:1863761)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63102 Genomic DNA. Translation: CAA44816.1.
    X56753 mRNA. Translation: CAA40073.1.
    PIRiS22502.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63102 Genomic DNA. Translation: CAA44816.1 .
    X56753 mRNA. Translation: CAA40073.1 .
    PIRi S22502.

    3D structure databases

    ProteinModelPortali P25803.
    SMRi P25803. Positions 127-352.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C01.010.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Nucleotide sequence of a gene for an endopeptidase (EP-C1) from Phaseolus vulgaris."
      Ogushi Y., Tanaka T., Yamauchi D., Minamikawa T.
      Plant Mol. Biol. 19:705-706(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Saxa.
      Tissue: Seedling.
    2. "Nucleotide sequence of cDNA for an endopeptidase (EP-C1) from pods of maturing Phaseolus vulgaris fruits."
      Tanaka T., Yamauchi D., Minamikawa T.
      Plant Mol. Biol. 16:1083-1084(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-362.
      Strain: cv. Goldstar.
      Tissue: Fruit.

    Entry informationi

    Entry nameiCYSEP_PHAVU
    AccessioniPrimary (citable) accession number: P25803
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 86 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3