IED ID | IndEnz0002018762 |
Enzyme Type ID | protease018762 |
Protein Name |
A disintegrin and metalloproteinase with thrombospondin motifs adt-2 ADAMTS adt-2 EC 3.4.24.- |
Gene Name | adt-2 sma-21 F08C6.1 |
Organism | Caenorhabditis elegans |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
Enzyme Sequence | MLLPLLISGLLFRNADAFLPFFNEDDLKYTFGVDTHAEVPNHEEIDPVPYYHQNGSLHKLEFMAFNKKYNLSLEPTLAKLLSSGVTVVKKNEKKGGSLDFGSTLDSCHYHHYGEKVYAAISNCDGRIKGTVIDDGEIIVVHPFPDHHAHRSKRATENGAHVVYKRETLAGEPKDFCGLDNVVTEESLVEDESAIFEDVFVTGQRLTQQSDLIVELAVFVDENLWRHFSSKHGGMADRKLQDYTLTLLNNIQIMYYQPTASPPLTFRVIRYEVLTRQPSALAGYLHNHGNAQMYLDRFCRYQRNLAVRDWDHAIMLTGYDIHRGAGSRSISGIARLDGMCDPWNTCTLAEGLDFTSAFIGTHELGHSVGMRHDEPYCQSKHIMSSSLGPGKVTWSTCSLRDYHQFLQRLDGRGKNCLRVSNMPNKLEISSNVKPGQIYDANLQCELMHGNGYQQVTPRQDSYDGICYMMWCGQSSFGRIITSHPALEGTFCGPSKWCQLGRCVPWTGTNEIQPTVQHVAPVVTTLPSRIDGSWSGWGATICSQCTCNGILGSVGLAIARRTCSAPYPANGGSDCVGSTSRAVLCSRQCGRASKSVDEYISDKCMEQKRLKNDRELTGKGSQLNRFPQRACKVFCDVQQHYGSQRNYRFFGDNLPDGTSCGYDRYCLDGECLALNCNNNALISRDQSCPTDTCPITDQSSSVYRGQWGTWSLWTSCTATCGGGYRKRNRACSITGQCEGNEDETEVCSSESCPSVLRVGNEWSTWTEWNHCSVSCGRGSQARYRKCLSPHRTLAFDCPEKNIEVRSCDNGPCNAIGVWGTWGGWSTCSTSCGPGTLVRQRTCNREPCDGSAHERRSCNVATCQNDGIWSLWNEWSDCSRVCGKGLRSRSRSCFGSGCMGASSEQQFCNEQACASSSANDWGTWSGWSQCSVSCGAGVKRRTRTCRTGNCPGNYKESAICNDRDCENKNAAWGGWGYWSSCSETCGDGVRKRVRKCYGSGNCDGQQYEKQYCNLRVCDFRRKF |
Enzyme Length | 1020 |
Uniprot Accession Number | Q19204 |
Absorption | |
Active Site | ACT_SITE 362; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: Regulates body size probably independently of the TGF beta-like dbl-1 pathway. However, may regulate some dbl-1-mediated transcription. Plays a role in cuticle collagen fibril organization. Required for embryonic development. {ECO:0000269|PubMed:21256840}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Disulfide bond (19); Domain (8); Glycosylation (2); Metal binding (3); Motif (1); Mutagenesis (1); Propeptide (1); Signal peptide (1) |
Keywords | Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10778742; 11381264; 12529635; 14551910; 14704431; 15791247; 16122351; 17164286; 18425118; 19343510; 20439774; 20439776; 21177967; 22267497; 22347378; 22500807; 22560298; 23800452; 24884423; 25487147; 6593563; |
Motif | MOTIF 174..181; /note=Cysteine switch; /evidence=ECO:0000250|UniProtKB:P03956 |
Gene Encoded By | |
Mass | 113,527 |
Kinetics | |
Metal Binding | METAL 361; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 365; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 371; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276 |
Rhea ID | |
Cross Reference Brenda |