| IED ID | IndEnz0002003172 |
| Enzyme Type ID | protease003172 |
| Protein Name |
Vignain EC 3.4.22.- Bean endopeptidase Cysteine proteinase Sulfhydryl-endopeptidase SH-EP Cleaved into: Vignain-1; Vignain-2 |
| Gene Name | |
| Organism | Vigna mungo (Black gram) (Phaseolus mungo) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Fabales Fabaceae Papilionoideae 50 kb inversion clade NPAAA clade indigoferoid/millettioid clade Phaseoleae Vigna Vigna mungo (Black gram) (Phaseolus mungo) |
| Enzyme Sequence | MAMKKLLWVVLSLSLVLGVANSFDFHEKDLESEESLWDLYERWRSHHTVSRSLGEKHKRFNVFKANVMHVHNTNKMDKPYKLKLNKFADMTNHEFRSTYAGSKVNHHKMFRGSQHGSGTFMYEKVGSVPASVDWRKKGAVTDVKDQGQCGSCWAFSTIVAVEGINQIKTNKLVSLSEQELVDCDKEENQGCNGGLMESAFEFIKQKGGITTESNYPYTAQEGTCDESKVNDLAVSIDGHENVPVNDENALLKAVANQPVSVAIDAGGSDFQFYSEGVFTGDCNTDLNHGVAIVGYGTTVDGTNYWIVRNSWGPEWGEQGYIRMQRNISKKEGLCGIAMMASYPIKNSSDNPTGSLSSPKDEL |
| Enzyme Length | 362 |
| Uniprot Accession Number | P12412 |
| Absorption | |
| Active Site | ACT_SITE 152; /evidence=ECO:0000250; ACT_SITE 288; /evidence=ECO:0000250; ACT_SITE 309; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Thought to be involved in the hydrolysis of stored seed proteins. In vitro, catalyzes the hydrolysis of proteins, such as azocasein. Shows a preferential cleavage for Asn-|-Xaa in small molecule substrates such as Boc-Asn-|-OPHNO(2). |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Disulfide bond (3); Motif (1); Propeptide (2); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Protease;Signal;Thiol protease;Vacuole;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:8076688}. Vacuole, aleurone grain {ECO:0000269|PubMed:8076688}. |
| Modified Residue | |
| Post Translational Modification | PTM: The mature protein is not glycosylated.; PTM: 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. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 359..362; /note=Prevents secretion from ER |
| Gene Encoded By | |
| Mass | 40,222 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.B1; |