| IED ID | IndEnz0002014069 |
| Enzyme Type ID | protease014069 |
| Protein Name |
Procardosin-A EC 3.4.23.- Cleaved into: Cardosin-A intermediate form 35 kDa subunit; Cardosin-A heavy chain Cardosin-A 31 kDa subunit ; Cardosin-A intermediate form 30 kDa subunit; Cardosin-A light chain Cardosin-A 15 kDa subunit |
| Gene Name | cardA |
| Organism | Cynara cardunculus (Cardoon) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids campanulids Asterales Asteraceae Carduoideae Cardueae Carduinae Cynara Cynara cardunculus (Cardoon) |
| Enzyme Sequence | MGTSIKANVLALFLFYLLSPTVFSVSDDGLIRIGLKKRKVDRIDQLRGRRALMEGNARKDFGFRGTVRDSGSAVVALTNDRDTSYFGEIGIGTPPQKFTVIFDTGSSVLWVPSSKCINSKACRAHSMYESSDSSTYKENGTFGAIIYGTGSITGFFSQDSVTIGDLVVKEQDFIEATDEADNVFLHRLFDGILGLSFQTISVPVWYNMLNQGLVKERRFSFWLNRNVDEEEGGELVFGGLDPNHFRGDHTYVPVTYQYYWQFGIGDVLIGDKSTGFCAPGCQAFADSGTSLLSGPTAIVTQINHAIGANGVMNQQCKTVVSRYGRDIIEMLRSKIQPDKICSHMKLCTFDGARDVSSIIESVVDKNNDKSSGGIHDEMCTFCEMAVVWMQNEIKQSETEDNIINYANELCEHLSTSSEELQVDCNTLSSMPNVSFTIGGKKFGLTPEQYILKVGKGEATQCISGFTAMDATLLGPLWILGDVFMRPYHTVFDYGNLLVGFAEAA |
| Enzyme Length | 504 |
| Uniprot Accession Number | Q9XFX3 |
| Absorption | |
| Active Site | ACT_SITE 103; /evidence="ECO:0000250|UniProtKB:P42210, ECO:0000255|PROSITE-ProRule:PRU10094"; ACT_SITE 286; /evidence="ECO:0000250|UniProtKB:P42210, ECO:0000255|PROSITE-ProRule:PRU10094" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the specific aspartic proteinase inhibitors diazoacetyl-noleucine methyl ester and pepstatin. {ECO:0000269|PubMed:8654427}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.23.- |
| Enzyme Function | FUNCTION: Aspartic proteinase with a high preference for bonds between hydrophobic residues. Cleaves alpha-lactalbumin but not beta-lactoglobulin. {ECO:0000250|UniProtKB:P85136, ECO:0000269|PubMed:16428617, ECO:0000269|PubMed:8654427}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Stable at temperatures of up to 60 degrees Celsius. {ECO:0000269|PubMed:8654427}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. Active from pH 2.0-7.0. {ECO:0000269|PubMed:8654427}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (24); Chain (5); Disulfide bond (6); Domain (2); Glycosylation (2); Helix (9); Motif (2); Propeptide (2); Sequence conflict (7); Signal peptide (1); Site (3); Turn (6) |
| Keywords | 3D-structure;Aspartyl protease;Cell wall;Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Extracellular matrix;Glycoprotein;Hydrolase;Membrane;Microsome;Protease;Secreted;Signal;Vacuole;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:10497243, ECO:0000269|PubMed:18767217, ECO:0000269|PubMed:9362566}. Protein storage vacuole {ECO:0000269|PubMed:10497243, ECO:0000269|PubMed:18767217, ECO:0000269|PubMed:9362566}. Secreted, cell wall {ECO:0000269|PubMed:10497243, ECO:0000269|PubMed:18767217, ECO:0000269|PubMed:9362566}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:10497243, ECO:0000269|PubMed:18767217, ECO:0000269|PubMed:9362566}. Note=Procardosin-A is associated with the microsomal membranes, the mature form is secreted. {ECO:0000269|PubMed:10497243, ECO:0000269|PubMed:18767217, ECO:0000269|PubMed:9362566}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. Glycans found at Asn-139 include approximately 6% oligomannose, 82% oligosaccharides of the plant modified type with proximal fucose but without xylose and 6% oligosaccharides of the plant modified type with proximal fucose and xylose. Glycans found at Asn-432 include 14% oligosaccharides of the plant modified type with proximal fucose but without xylose and 86% oligosaccharides of the plant modified type with proximal fucose and xylose. {ECO:0000269|PubMed:10488111, ECO:0000269|PubMed:9057834}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1B5F; |
| Mapped Pubmed ID | - |
| Motif | MOTIF 246..248; /note=RGD motif; /evidence=ECO:0000269|PubMed:16279943; MOTIF 455..457; /note=KGE motif; /evidence=ECO:0000269|PubMed:16279943 |
| Gene Encoded By | |
| Mass | 55,504 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.64 mM for Leu-Ser-Phe(NO2)-Ahx-Ala-Leu {ECO:0000269|PubMed:8654427}; KM=0.108 mM for Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu {ECO:0000269|PubMed:8654427}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.40; |