| IED ID | IndEnz0002014001 |
| Enzyme Type ID | protease014001 |
| Protein Name |
ADAM DEC1 EC 3.4.24.- A disintegrin and metalloproteinase domain-like protein decysin-1 ADAM-like protein decysin-1 |
| Gene Name | ADAMDEC1 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MLRGISQLPAVATMSWVLLPVLWLIVQTQAIAIKQTPELTLHEIVCPKKLHILHKREIKNNQTEKHGKEERYEPEVQYQMILNGEEIILSLQKTKHLLGPDYTETLYSPRGEEITTKPENMEHCYYKGNILNEKNSVASISTCDGLRGYFTHHHQRYQIKPLKSTDEKEHAVFTSNQEEQDPANHTCGVKSTDGKQGPIRISRSLKSPEKEDFLRAQKYIDLYLVLDNAFYKNYNENLTLIRSFVFDVMNLLNVIYNTIDVQVALVGMEIWSDGDKIKVVPSASTTFDNFLRWHSSNLGKKIHDHAQLLSGISFNNRRVGLAASNSLCSPSSVAVIEAKKKNNVALVGVMSHELGHVLGMPDVPFNTKCPSGSCVMNQYLSSKFPKDFSTSCRAHFERYLLSQKPKCLLQAPIPTNIMTTPVCGNHLLEVGEDCDCGSPKECTNLCCEALTCKLKPGTDCGGDAPNHTTE |
| Enzyme Length | 470 |
| Uniprot Accession Number | O15204 |
| Absorption | |
| Active Site | ACT_SITE 353; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: May play an important role in the control of the immune response and during pregnancy. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (2); Glycosylation (4); Metal binding (3); Natural variant (2); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Alternative splicing;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | INDUCTION: Induced during DC maturation and up-regulated in response to T-cell signals. In macrophage up-regulated by bacterial lipopolysaccharides (LPS). Up-regulated by 1-alpha,25-dihydroxyvitamin D3 during differentiation of primary monocyte into macrophage. {ECO:0000269|PubMed:14632642, ECO:0000269|PubMed:9271581}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12037602; 18449420; 19218196; 20711500; 23754285; 25564618; 28455445; 29941981; 30352365; 31434712; 31627897; 32378728; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,775 |
| Kinetics | |
| Metal Binding | METAL 352; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 356; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 362; /note=Zinc; catalytic; /evidence=ECO:0000255 |
| Rhea ID | |
| Cross Reference Brenda |