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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)DescriptionActionsGraphical viewLength
    Active sitei25By similarity1
    Active sitei157By similarity1
    Active sitei173By similarity1

    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)DescriptionActionsGraphical viewLength
    ChainiPRO_00000505591 – 208Ervatamin-CAdd BLAST208

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi22 ↔ 631 Publication
    Disulfide bondi56 ↔ 961 Publication
    Disulfide bondi114 ↔ 1931 Publication
    Disulfide bondi151 ↔ 1961 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP83654.

    Expressioni

    Tissue specificityi

    Laticifer.Curated1 Publication

    Interactioni

    Subunit structurei

    Monomer.Curated1 Publication

    Structurei

    Secondary structure

    1208
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi7 – 10Combined sources4
    Beta strandi21 – 23Combined sources3
    Helixi25 – 42Combined sources18
    Helixi50 – 56Combined sources7
    Helixi68 – 78Combined sources11
    Turni84 – 86Combined sources3
    Beta strandi107 – 110Combined sources4
    Helixi116 – 125Combined sources10
    Beta strandi128 – 132Combined sources5
    Helixi137 – 140Combined sources4
    Beta strandi144 – 147Combined sources4
    Beta strandi157 – 164Combined sources8
    Beta strandi166 – 172Combined sources7
    Beta strandi184 – 188Combined sources5
    Helixi195 – 197Combined sources3
    Beta strandi203 – 206Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1O0EX-ray1.90A/B1-208[»]
    2PNSX-ray1.90A/B1-208[»]
    SMRiP83654.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti17K → W AA sequence (PubMed:9836431).Curated1
    Sequence conflicti21S → W AA sequence (PubMed:9836431).Curated1

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1O0EX-ray1.90A/B1-208[»]
    2PNSX-ray1.90A/B1-208[»]
    SMRiP83654.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    MEROPSiC01.116.

    Proteomic databases

    PRIDEiP83654.

    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: November 2, 2016
    This is version 56 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.