IED ID | IndEnz0002006314 |
Enzyme Type ID | protease006314 |
Protein Name |
Metalloprotease mig-17 EC 3.4.24.- Abnormal cell migration protein 17 |
Gene Name | mig-17 F57B7.4 |
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 | MHTFCILIPTFLVLVWTTESARREKQQSNDISFVKRKVQDGLKFSRVIKYTNETIQGMKTNFNSNKTQELSLDVLVVADFLSYQAFLEMSNGDSHRAIHNLKEYLHALFEQTKIIYDGISFGNETLHMVFAGTWIATQERDCPLWISWAEEEEERVLNEEIRRLEEKERDLNSTFVDDTFFMNSTDSDNSSTDALISSDMPKKLRKFVDITLEEMQENNSTEMTLKIDSKKAIDKFTIWLKEQTGLPRHEHAVLITKFDLISINGNSATQGMAYVGNICENGDSSSVVEDIGAGLTSLIMAHEIGHSLGALHDGAYETAECDSNDNYLMAVAVSGSADRQSFLNSRRMSNCSINSIIENLKEPTANCVKKWKTKKGKDVSQKDFIKKPGELVKITRQCQVAFGPTFIPCLHIGYFHEQSICERIWCSDGESDECQTLNYFPAFDGTECGYNMWCLEGSCVQNTKKWMDCKDINSKTCSKYSTSKLKHYCKSKDFREICCRTCAKKGKIY |
Enzyme Length | 509 |
Uniprot Accession Number | Q20930 |
Absorption | |
Active Site | ACT_SITE 303; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: Metalloprotease (PubMed:17491590, PubMed:18637819). Acts in the basement membrane to control directional migration of distal tip cells (DTCs) along the body wall basement membranes, a key step that promotes gonad morphogenesis (PubMed:10864868, PubMed:15556863, PubMed:17491590,PubMed:19104038, PubMed:24318535, PubMed:26994289). Regulates DTC migration probably by recruiting fibulin fbl-1, type IV collagen let-2 and nidogen nid-1 to the gonad basement membrane thereby promoting the remodeling of the basement membrane (PubMed:19104038). During larval development and probably upstream of basement membrane proteins fbl-1, let-2 and nid-1, regulates pharynx length, probably by regulating pharyngeal cell length (PubMed:26994289). Does not recruit fbl-1 to the pharynx basement membrane (PubMed:26994289). {ECO:0000269|PubMed:10864868, ECO:0000269|PubMed:15556863, ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:18637819, ECO:0000269|PubMed:19104038, ECO:0000269|PubMed:24318535, ECO:0000269|PubMed:26994289}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Disulfide bond (1); Domain (3); Glycosylation (9); Metal binding (3); Mutagenesis (17); Propeptide (1); Signal peptide (1); Site (1) |
Keywords | Basement membrane;Cleavage on pair of basic residues;Developmental protein;Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:10864868, ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:18637819, ECO:0000269|PubMed:24318535, ECO:0000269|PubMed:26994289}. Note=Secreted as a zymogen (PubMed:17491590, PubMed:18637819). The zymogen localizes to the basement membrane of gonads, intestine and hypodermis (PubMed:17491590, PubMed:18637819). The mature and active form displays a similar localization but only during the L3 larval stage (PubMed:18637819). {ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:18637819}. |
Modified Residue | |
Post Translational Modification | PTM: N-glycosylated by the COG complex; required for gonadal localization (PubMed:14688791, PubMed:16354716, PubMed:17761667, PubMed:17491590). N-glycosylation of the propeptide is required for gonadal localization but not for distal tip cell migration (PubMed:17491590). Required for the regulation of pharynx length (PubMed:26994289). N-glycosylation is not required for mig-17 secretion (PubMed:17491590). {ECO:0000269|PubMed:14688791, ECO:0000269|PubMed:16354716, ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:17761667, ECO:0000269|PubMed:26994289}.; PTM: The precursor is cleaved into the active mature form by autoproteolysis (PubMed:17491590, PubMed:18637819). Cleavage occurs after secretion and only during the L3-L4 larval stages (PubMed:18637819). {ECO:0000269|PubMed:17491590, ECO:0000269|PubMed:18637819}. |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10388818; 17848203; 19098902; 19297413; 21077329; 21177967; 22560298; 23800452; 25298520; 25487147; 33264296; |
Motif | |
Gene Encoded By | |
Mass | 57,976 |
Kinetics | |
Metal Binding | METAL 302; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 306; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 312; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276 |
Rhea ID | |
Cross Reference Brenda |