Detail Information for IndEnz0002016153
IED ID IndEnz0002016153
Enzyme Type ID protease016153
Protein Name A disintegrin and metalloproteinase with thrombospondin motifs gon-1
ADAMTS gon-1
EC 3.4.24.-
Abnormal gonad development protein 1
Gene Name gon-1 F25H8.3
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 MRSIGGSFHLLQPVVAALILLVVCLVYALQSGSGTISEFSSDVLFSRAKYSGVPVHHSRWRQDAGIHVIDSHHIVRRDSYGRRGKRDVTSTDRRRRLQGVARDCGHACHLRLRSDDAVYIVHLHRWNQIPDSHNKSVPHFSNSNFAPMVLYLDSEEEVRGGMSRTDPDCIYRAHVKGVHQHSIVNLCDSEDGLYGMLALPSGIHTVEPIISGNGTEHDGASRHRQHLVRKFDPMHFKSFDHLNSTSVNETETTVATWQDQWEDVIERKARSRRAANSWDHYVEVLVVADTKMYEYHGRSLEDYVLTLFSTVASIYRHQSLRASINVVVVKLIVLKTENAGPRITQNAQQTLQDFCRWQQYYNDPDDSSVQHHDVAILLTRKDICRSQGKCDTLGLAELGTMCDMQKSCAIIEDNGLSAAFTIAHELGHVFSIPHDDERKCSTYMPVNKNNFHIMAPTLEYNTHPWSWSPCSAGMLERFLENNRGQTQCLFDQPVERRYYEDVFVRDEPGKKYDAHQQCKFVFGPASELCPYMPTCRRLWCATFYGSQMGCRTQHMPWADGTPCDESRSMFCHHGACVRLAPESLTKIDGQWGDWRSWGECSRTCGGGVQKGLRDCDSPKPRNGGKYCVGQRERYRSCNTQECPWDTQPYREVQCSEFNNKDIGIQGVASTNTHWVPKYANVAPNERCKLYCRLSGSAAFYLLRDKVVDGTPCDRNGDDICVAGACMPAGCDHQLHSTLRRDKCGVCGGDDSSCKVVKGTFNEQGTFGYNEVMKIPAGSANIDIRQKGYNNMKEDDNYLSLRAANGEFLLNGHFQVSLARQQIAFQDTVLEYSGSDAIIERINGTGPIRSDIYVHVLSVGSHPPDISYEYMTAAVPNAVIRPISSALYLWRVTDTWTECDRACRGQQSQKLMCLDMSTHRQSHDRNCQNVLKPKQATRMCNIDCSTRWITEDVSSCSAKCGSGQKRQRVSCVKMEGDRQTPASEHLCDRNSKPSDIASCYIDCSGRKWNYGEWTSCSETCGSNGKMHRKSYCVDDSNRRVDESLCGREQKEATERECNRIPCPRWVYGHWSECSRSCDGGVKMRHAQCLDAADRETHTSRCGPAQTQEHCNEHACTWWQFGVWSDCSAKCGDGVQYRDANCTDRHRSVLPEHRCLKMEKIITKPCHRESCPKYKLGEWSQCSVSCEDGWSSRRVSCVSGNGTEVDMSLCGTASDRPASHQTCNLGTCPFWRNTDWSACSVSCGIGHRERTTECIYREQSVDASFCGDTKMPETSQTCHLLPCTSWKPSHWSPCSVTCGSGIQTRSVSCTRGSEGTIVDEYFCDRNTRPRLKKTCEKDTCDGPRVLQKLQADVPPIRWATGPWTACSATCGNGTQRRLLKCRDHVRDLPDEYCNHLDKEVSTRNCRLRDCSYWKMAEWEECPATCGTHVQQSRNVTCVSAEDGGRTILKDVDCDVQKRPTSARNCRLEPCPKGEEHIGSWIIGDWSKCSASCGGGWRRRSVSCTSSSCDETRKPKMFDKCNEELCPPLTNNSWQISPWTHCSVSCGGGVQRRKIWCEDVLSGRKQDDIECSEIKPREQRDCEMPPCRSHYHNKTSSASMTSLSSSNSNTTSSASASSLPILPPVVSWQTSAWSACSAKCGRGTKRRVVECVNPSLNVTVASTECDQTKKPVEEVRCRTKHCPRWKTTTWSSCSVTCGRGIRRREVQCYRGRKNLVSDSECNPKTKLNSVANCFPVACPAYRWNVTPWSKCKDECARGQKQTRRVHCISTSGKRAAPRMCELARAPTSIRECDTSNCPYEWVPGDWQTCSKSCGEGVQTREVRCRRKINFNSTIPIIFMLEDEPAVPKEKCELFPKPNESQTCELNPCDSEFKWSFGPWGECSKNCGQGIRRRRVKCVANDGRRVERVKCTTKKPRRTQYCFERNCLPSTCQELKSQNVKAKDGNYTILLDGFTIEIYCHRMNSTIPKAYLNVNPRTNFAEVYGKKLIYPHTCPFNGDRNDSCHCSEDGDASAGLTRFNKVRIDLLNRKFHLADYTFAKREYGVHVPYGTAGDCYSMKDCPQGIFSIDLKSAGLKLVDDLNWEDQGHRTSSRIDRFYNNAKVIGHCGGFCGKCSPERYKGLIFEVNTKLLNHVKNGGHIDDELDDDGFSGDMD
Enzyme Length 2150
Uniprot Accession Number Q19791
Absorption
Active Site ACT_SITE 425; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Secreted metalloprotease required for distal tip cell (DTC) migration along the body wall basement membranes, a key step that promotes gonad morphogenesis (PubMed:10588887, PubMed:10376599, PubMed:15556862). Probably acts by remodeling the basement membrane during cell migration (PubMed:10376599). Required to restrict presynaptic growth at the neuromuscular junctions (NMJ) in late larval stage and in adult motor neurons, probably by controlling collagen IV emb-9 degradation, a component of the synapse basement membrane (PubMed:25080592, PubMed:25232106). Also involved in the organization of adult muscle morphology (PubMed:25232106). Has a protease-independent function in promoting the transport from the endoplasmic reticulum to the Golgi apparatus of a variety of secretory cargos (PubMed:22419820, PubMed:26218657). Required for the secretion of insulin-like peptide ins-7, daf-28 and ins-18 and TGF beta-like protein daf-7 (PubMed:26218657). In peripheral tissues, negatively regulates insulin-mediated daf-16 translocation and thereby negatively regulates lifespan and dauer formation (PubMed:26218657). {ECO:0000269|PubMed:10376599, ECO:0000269|PubMed:10588887, ECO:0000269|PubMed:15556862, ECO:0000269|PubMed:22419820, ECO:0000269|PubMed:25080592, ECO:0000269|PubMed:25232106, ECO:0000269|PubMed:26218657}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (11); Domain (20); Glycosylation (18); Metal binding (3); Mutagenesis (1); Propeptide (1); Region (1); Signal peptide (1)
Keywords Basement membrane;Developmental protein;Disulfide bond;ER-Golgi transport;Endoplasmic reticulum;Extracellular matrix;Glycoprotein;Golgi apparatus;Hydrolase;Metal-binding;Metalloprotease;Protease;Protein transport;Reference proteome;Repeat;Secreted;Signal;Transport;Zinc;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:10376599}. Endoplasmic reticulum {ECO:0000269|PubMed:22419820}. Golgi apparatus {ECO:0000269|PubMed:22419820}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..28; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10778742; 11381264; 12097347; 12514189; 12529635; 14551910; 15338614; 17090602; 17164286; 17486083; 17850180; 19098902; 19343510; 20308279; 20439774; 21177967; 21367940; 22267497; 22286215; 22347378; 22560298; 22634595; 23800452; 24884423; 25487147; 33264296; 6593563;
Motif
Gene Encoded By
Mass 242,582
Kinetics
Metal Binding METAL 424; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 428; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 434; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276
Rhea ID
Cross Reference Brenda