| IED ID | IndEnz0002005459 |
| Enzyme Type ID | protease005459 |
| Protein Name |
ADAMTS-like protein 4 ADAMTSL-4 |
| Gene Name | Adamtsl4 |
| Organism | Rattus norvegicus (Rat) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MELWLGRLWLYVMLLLLLLQLCQDQELLGPSLQTPSEEDQVPEGLWGPWGRWASCSQPCGVGVQRRSRTCELHPALSLPPRPPRHPEAPQPRGQGSRPQTPRDPQSLYRPQPRGRGGPLRGPASQVGREETQEPRGAQRFRVRDPIKPGMFGYGRVPFALPLHRSRRLAHKPGQPKDSSTAEETLPSQPPSTEPASEKHSPHMQPPELRAQSRSPSAETPRSGTAQTEVPSRTSSAPSDMGIPAPTSSFRDSRSFQGSPEPRMPTSQGAERQPHPFSPVTRSQLSRRHWRPPGSPHRSPDGWLPLTRDSSPHWSLFAPSSPTPECSGESEQMRACSQEPCPPEQPDPRALQCAAFDSQEFMGQLYQWEPFTEVQGSQRCELNCRPRGFRFYVRHTEKVQDGTLCQPGSLDICVAGHCLSPGCDGILGSGRRPDGCGVCGGDGSTCRLVSGNLTDRGGPLGYQKILWIPAGASHLRISQFRPSSNYLALRGPGGRSIINGNWAVDPPGSYAAVGTVFQYNRPPREEGKGETLSAEGPTTQPVDVYMIFQEDNPGVFYQYVTSAAPESPSTMPPALQLQPEMLRGEPLLPSAPRPVRAPGTLQRQARIPQVPPPTHVRTAMGSSAGYWKQVGHSECSASCGKGVWRPIFLCVSRESGEELDEQSCAVGARPPASPESCHRPPCPPYWEAGEWTSCSRSCGPGTQHRQLLCRQEFGGGGSSVPPERCGHLPRPNITQSCQLRLCGHWEISSPWSQCSVRCGRGQRSRQVRCVGSNGHEVGKQECASGPPPPPSREACDMGPCTTAWFYSDWSSKCSAECGTGIQRRAVVCLRSGETLQGDPEAGSTEQGCPLRSRPPDMRACSLGPCEKTWRWYTGPWSECSSECGSGTQHRDIICVSKLGTKFNVTSPSNCSHLPRPPALQPCQGQACEDQWFSTLWSPCSQSCQGGVQTREVQCLSSNHTLSSRCPPHLRPSRKRPCNSQPCNQRPDDQCKDSSPHCPLVVQARLCVYPYYTATCCRSCAHVLEQSQLEPA |
| Enzyme Length | 1030 |
| Uniprot Accession Number | Q4FZU4 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Positive regulation of apoptosis. May facilitate FBN1 microfibril biogenesis (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (2); Domain (7); Glycosylation (2); Region (2); Signal peptide (1) |
| Keywords | Apoptosis;Extracellular matrix;Glycoprotein;Reference proteome;Repeat;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Colocalizes with FMN1 microfibrils in the eye ECM. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated (By similarity). Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 112,785 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |