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P12412

- CYSEP_VIGMU

UniProt

P12412 - CYSEP_VIGMU

Protein

Vignain

Gene
N/A
Organism
Vigna mungo (Black gram) (Phaseolus mungo)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    Hydrolysis of proteins, such as azocasein. Preferential cleavage: Asn-|-Xaa in small molecule substrates such as Boc-Asn-|-OPHNO2.

    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
    Sulfhydryl-endopeptidase
    Short name:
    SH-EP
    Cleaved into the following 2 chains:
    OrganismiVigna mungo (Black gram) (Phaseolus mungo)
    Taxonomic identifieri3915 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

    Subcellular locationi

    Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation. Vacuolealeurone grain 1 Publication

    GO - Cellular componenti

    1. aleurone grain Source: UniProtKB-SubCell
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    3. vacuole Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 126106Activation peptide1 PublicationPRO_0000026445Add
    BLAST
    Chaini127 – 352226Vignain-1PRO_0000026446Add
    BLAST
    Chaini128 – 352225Vignain-2PRO_0000026447Add
    BLAST
    Propeptidei353 – 36210PRO_0000026448

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi149 ↔ 191By similarity
    Disulfide bondi183 ↔ 224By similarity
    Disulfide bondi282 ↔ 334By similarity

    Post-translational modificationi

    The mature protein is not glycosylated.
    The precursor stored in the endoplasmic reticulum lumen is processed during the transport to proteins bodies to two dominant mature forms that differ by a single amino acid residue at the N-terminus.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliP12412.
    SMRiP12412. Positions 127-352.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi359 – 3624Prevents secretion from ER

    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.

    P12412-1 [UniParc]FASTAAdd to Basket

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    MAMKKLLWVV LSLSLVLGVA NSFDFHEKDL ESEESLWDLY ERWRSHHTVS    50
    RSLGEKHKRF NVFKANVMHV HNTNKMDKPY KLKLNKFADM TNHEFRSTYA 100
    GSKVNHHKMF RGSQHGSGTF MYEKVGSVPA SVDWRKKGAV TDVKDQGQCG 150
    SCWAFSTIVA VEGINQIKTN KLVSLSEQEL VDCDKEENQG CNGGLMESAF 200
    EFIKQKGGIT TESNYPYTAQ EGTCDESKVN DLAVSIDGHE NVPVNDENAL 250
    LKAVANQPVS VAIDAGGSDF QFYSEGVFTG DCNTDLNHGV AIVGYGTTVD 300
    GTNYWIVRNS WGPEWGEQGY IRMQRNISKK EGLCGIAMMA SYPIKNSSDN 350
    PTGSLSSPKD EL 362
    Length:362
    Mass (Da):40,222
    Last modified:October 1, 1989 - v1
    Checksum:iB7C3B92868D5E3C8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15732 mRNA. Translation: CAA33753.1.
    X51900 Genomic DNA. Translation: CAA36181.1.
    PIRiS12581.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15732 mRNA. Translation: CAA33753.1 .
    X51900 Genomic DNA. Translation: CAA36181.1 .
    PIRi S12581.

    3D structure databases

    ProteinModelPortali P12412.
    SMRi P12412. 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 cDNA for sulfhydryl-endopeptidase (SH-EP) from cotyledons of germinating Vigna mungo seeds."
      Akasofu H., Yamauchi D., Mitsuhashi W., Minamikawa T.
      Nucleic Acids Res. 17:6733-6733(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 132-140.
      Tissue: Seed cotyledon.
    2. "Nucleotide sequence of the gene for the Vigna mungo sulfhydryl-endopeptidase (SH-EP)."
      Akasofu H., Yamauchi D., Minamikawa T.
      Nucleic Acids Res. 18:1892-1892(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Leaf.
    3. "Posttranslational processing of a carboxy-terminal propeptide containing a KDEL sequence of plant vacuolar cysteine endopeptidase (SH-EP)."
      Okamoto T., Nakayama H., Seta K., Isobe T., Minamikawa T.
      FEBS Lett. 351:31-34(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 127-140; 197-216; 324-333 AND 339-352, SUBCELLULAR LOCATION.
    4. Erratum
      Okamoto T., Nakayama H., Seta K., Isobe T., Minamikawa T.
      FEBS Lett. 356:152-152(1994)

    Entry informationi

    Entry nameiCYSEP_VIGMU
    AccessioniPrimary (citable) accession number: P12412
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    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