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Protein

Ervatamin-C

Gene
N/A
Organism
Tabernaemontana divaricata (Crepe jasmine) (Ervatamia coronaria)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cysteine proteinase. Hydrolyzes denatured natural substrates such as casein, hemoglobin, azoalbumin and azocasein with a high specific activity. Has little or no activity against synthetic substrates.1 Publication

Enzyme regulationi

Activated by thio-specific activators such as cysteine, beta-mercaptoethanol, DTT and glutathione. Inhibited by the thiol-specific inhibitors leupeptin, iodoacetamide, PCMB, NEM, mercuric chloride and sodium tetrathionate.1 Publication

Kineticsi

  1. KM=9.09 µM for azoalbumin

    pH dependencei

    Optimum pH is 7.5-8.0 with azoalbumin or hemoglobin as substrate. Active and stable from pH 2.0 to 12.0.

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius with azoalbumin as substrate. Thermostable up to 70 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei25 – 251By similarity
    Active sitei157 – 1571By similarity
    Active sitei173 – 1731By similarity

    GO - Molecular functioni

    • cysteine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    • proteolysis Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    SABIO-RKP83654.

    Protein family/group databases

    MEROPSiC01.116.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ervatamin-C (EC:3.4.22.-)
    Short name:
    ERV-C
    OrganismiTabernaemontana divaricata (Crepe jasmine) (Ervatamia coronaria)Curated
    Taxonomic identifieri52861 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesApocynaceaeRauvolfioideaeTabernaemontaneaeTabernaemontaninaeTabernaemontana

    Subcellular locationi

    • Secreted Curated1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 208208Ervatamin-CPRO_0000050559Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi22 ↔ 631 Publication
    Disulfide bondi56 ↔ 961 Publication
    Disulfide bondi114 ↔ 1931 Publication
    Disulfide bondi151 ↔ 1961 Publication

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Laticifer.Curated1 Publication

    Interactioni

    Subunit structurei

    Monomer.Curated1 Publication

    Structurei

    Secondary structure

    1
    208
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 104Combined sources
    Beta strandi21 – 233Combined sources
    Helixi25 – 4218Combined sources
    Helixi50 – 567Combined sources
    Helixi68 – 7811Combined sources
    Turni84 – 863Combined sources
    Beta strandi107 – 1104Combined sources
    Helixi116 – 12510Combined sources
    Beta strandi128 – 1325Combined sources
    Helixi137 – 1404Combined sources
    Beta strandi144 – 1474Combined sources
    Beta strandi157 – 1648Combined sources
    Beta strandi166 – 1727Combined sources
    Beta strandi184 – 1885Combined sources
    Helixi195 – 1973Combined sources
    Beta strandi203 – 2064Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1O0EX-ray1.90A/B1-208[»]
    2PNSX-ray1.90A/B1-208[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP83654.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Family and domain databases

    InterProiIPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    [Graphical view]
    PANTHERiPTHR12411. PTHR12411. 1 hit.
    PfamiPF00112. Peptidase_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00645. Pept_C1. 1 hit.
    [Graphical view]
    PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P83654-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    LPEQIDWRKK GAVTPVKNQG SCGSCWAFST VSTVESINQI RTGNLISLSE
    60 70 80 90 100
    QELVDCDKKN HGCLGGAFVF AYQYIINNGG IDTQANYPYK AVQGPCQAAS
    110 120 130 140 150
    KVVSIDGYNG VPFCNEXALK QAVAVQPSTV AIDASSAQFQ QYSSGIFSGP
    160 170 180 190 200
    CGTKLNHGVT IVGYQANYWI VRNSWGRYWG EKGYIRMLRV GGCGLCGIAR

    LPYYPTKA
    Length:208
    Mass (Da):22,523
    Last modified:April 26, 2004 - v1
    Checksum:i13CD944089802C12
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171K → W AA sequence (PubMed:9836431).Curated
    Sequence conflicti21 – 211S → W AA sequence (PubMed:9836431).Curated

    Mass spectrometryi

    Molecular mass is 23000 Da from positions 1 - 208. Determined by MALDI. 1 Publication

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1O0EX-ray1.90A/B1-208[»]
    2PNSX-ray1.90A/B1-208[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    MEROPSiC01.116.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    SABIO-RKP83654.

    Miscellaneous databases

    EvolutionaryTraceiP83654.

    Family and domain databases

    InterProiIPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    [Graphical view]
    PANTHERiPTHR12411. PTHR12411. 1 hit.
    PfamiPF00112. Peptidase_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00645. Pept_C1. 1 hit.
    [Graphical view]
    PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiERVC_TABDI
    AccessioniPrimary (citable) accession number: P83654
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: April 26, 2004
    Last modified: January 7, 2015
    This is version 54 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

    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.