Detail Information for IndEnz0002018868
IED ID IndEnz0002018868
Enzyme Type ID protease018868
Protein Name Cucumisin
EC 3.4.21.25
allergen Cuc m 1
Gene Name
Organism Cucumis melo (Muskmelon)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Cucurbitales Cucurbitaceae Benincaseae Cucumis Cucumis melo (Muskmelon)
Enzyme Sequence MSSSLIFKLFFFSLFFSNRLASRLDSDDDGKNIYIVYMGRKLEDPDSAHLHHRAMLEQVVGSTFAPESVLHTYKRSFNGFAVKLTEEEAEKIASMEGVVSVFLNEMNELHTTRSWDFLGFPLTVPRRSQVESNIVVGVLDTGIWPESPSFDDEGFSPPPPKWKGTCETSNNFRCNRKIIGARSYHIGRPISPGDVNGPRDTNGHGTHTASTAAGGLVSQANLYGLGLGTARGGVPLARIAAYKVCWNDGCSDTDILAAYDDAIADGVDIISLSVGGANPRHYFVDAIAIGSFHAVERGILTSNSAGNGGPNFFTTASLSPWLLSVAASTMDRKFVTQVQIGNGQSFQGVSINTFDNQYYPLVSGRDIPNTGFDKSTSRFCTDKSVNPNLLKGKIVVCEASFGPHEFFKSLDGAAGVLMTSNTRDYADSYPLPSSVLDPNDLLATLRYIYSIRSPGATIFKSTTILNASAPVVVSFSSRGPNRATKDVIKPDISGPGVEILAAWPSVAPVGGIRRNTLFNIISGTSMSCPHITGIATYVKTYNPTWSPAAIKSALMTTASPMNARFNPQAEFAYGSGHVNPLKAVRPGLVYDANESDYVKFLCGQGYNTQAVRRITGDYSACTSGNTGRVWDLNYPSFGLSVSPSQTFNQYFNRTLTSVAPQASTYRAMISAPQGLTISVNPNVLSFNGLGDRKSFTLTVRGSIKGFVVSASLVWSDGVHYVRSPITITSLV
Enzyme Length 731
Uniprot Accession Number Q39547
Absorption
Active Site ACT_SITE 140; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000305|Ref.6"; ACT_SITE 204; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000305|Ref.6"; ACT_SITE 525; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000305|Ref.6"
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity.; EC=3.4.21.25; Evidence={ECO:0000305|PubMed:7806492};
DNA Binding
EC Number 3.4.21.25
Enzyme Function
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Melting point at 81 degrees Celsius. {ECO:0000269|Ref.6};
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (42); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (2); Helix (19); Propeptide (2); Sequence conflict (1); Signal peptide (1); Turn (7)
Keywords 3D-structure;Allergen;Autocatalytic cleavage;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000255}.
Modified Residue
Post Translational Modification PTM: The C-terminal propeptide is autocleaved. {ECO:0000269|PubMed:7806492}.
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000255
Structure 3D X-ray crystallography (2)
Cross Reference PDB 3VTA; 4YN3;
Mapped Pubmed ID 27616715;
Motif
Gene Encoded By
Mass 78,820
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.25;