| IED ID | IndEnz0002018572 |
| Enzyme Type ID | protease018572 |
| Protein Name |
Disintegrin and metalloproteinase domain-containing protein 12 ADAM 12 EC 3.4.24.- Meltrin-alpha |
| Gene Name | ADAM12 MLTN UNQ346/PRO545 |
| 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 | MAARPLPVSPARALLLALAGALLAPCEARGVSLWNQGRADEVVSASVGSGDLWIPVKSFDSKNHPEVLNIRLQRESKELIINLERNEGLIASSFTETHYLQDGTDVSLARNYTVILGHCYYHGHVRGYSDSAVSLSTCSGLRGLIVFENESYVLEPMKSATNRYKLFPAKKLKSVRGSCGSHHNTPNLAAKNVFPPPSQTWARRHKRETLKATKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMKLLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTLDRGCSCQMAVEKGGCIMNASTGYPFPMVFSSCSRKDLETSLEKGMGVCLFNLPEVRESFGGQKCGNRFVEEGEECDCGEPEECMNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPANVYLHDGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKVSKSSFAKCEMRDAKCGKIQCQGGASRPVIGTNAVSIETNIPLQQGGRILCRGTHVYLGDDMPDPGLVLAGTKCADGKICLNRQCQNISVFGVHECAMQCHGRGVCNNRKNCHCEAHWAPPFCDKFGFGGSTDSGPIRQADNQGLTIGILVTILCLLAAGFVVYLKRKTLIRLLFTNKKTTIEKLRCVRPSRPPRGFQPCQAHLGHLGKGLMRKPPDSYPPKDNPRRLLQCQNVDISRPLNGLNVPQPQSTQRVLPPLHRAPRAPSVPARPLPAKPALRQAQGTCKPNPPQKPLPADPLARTTRLTHALARTPGQWETGLRLAPLRPAPQYPHQVPRSTHTAYIK |
| Enzyme Length | 909 |
| Uniprot Accession Number | O43184 |
| Absorption | |
| Active Site | ACT_SITE 351 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (5); Chain (1); Disulfide bond (7); Domain (3); Glycosylation (5); Metal binding (4); Modified residue (1); Motif (4); Natural variant (6); Propeptide (1); Region (1); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;Cell adhesion;Cell membrane;Cleavage on pair of basic residues;Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;SH3-binding;Secreted;Signal;Transmembrane;Transmembrane helix;Zinc;Zymogen |
| Interact With | Q8N157; P08631; P07948; P12931; O95633; Q6UY14-3; A8MQ03; Q9NQ30; Q5TD97; Q96NT3-2; P49639; P78385; Q07627; P60410; P59991; Q9BYR8; Q9BYR7; Q9BQ66; Q6L8G9; P26371; Q3LI66; Q9BYQ4; Q9BYQ0; Q5TCM9; O60336; P0DPK4; P32242; Q6P9E2; Q16348; O43609; Q9C004; Q7Z6R9 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000305}. |
| Modified Residue | MOD_RES 907; /note=Phosphotyrosine; by SRC; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12717386; 12915587; 12952982; 15242759; 15280379; 15358598; 15364951; 15381692; 15509542; 15574885; 15930294; 16054021; 16139919; 16213489; 16385451; 16453284; 16455653; 16495931; 16869727; 17440933; 17465398; 17620406; 17701664; 17846126; 17987603; 18081311; 18241035; 18264948; 18311789; 18365756; 18382998; 18395873; 18519826; 18604515; 18801731; 18978109; 19003798; 19040574; 19213876; 19268722; 19278423; 19544290; 19544357; 19609547; 19736612; 19769962; 19837132; 20090292; 20187159; 20218926; 20305677; 20379614; 20457602; 20509156; 20509157; 20688878; 21034452; 21103624; 21173277; 21240579; 21258805; 21277576; 21330122; 21493715; 21501859; 21518768; 21617380; 21875931; 22015022; 22089237; 22267082; 22284607; 22662180; 22676623; 22678798; 22767580; 22808268; 22882974; 22903068; 22926263; 22927907; 23135915; 23324579; 23421942; 23458101; 23491141; 23578941; 23589494; 23645517; 23680494; 23771733; 24006261; 24116709; 24243624; 24402778; 24465799; 24690292; 24695627; 24830297; 24899472; 24998958; 25139103; 25197389; 25591790; 25667922; 25886595; 25909890; 25926422; 26051455; 26407179; 26503019; 26553447; 26697810; 26722530; 26875044; 27144841; 27270327; 27432471; 27685922; 28005267; 28148288; 28395594; 28468988; 28637509; 28748424; 28765266; 28852196; 28929114; 29136943; 29476791; 29729432; 29731509; 30415904; 31013576; 32019179; 32025520; 32250658; 32319603; 33507683; 33616346; 33930608; 33952697; 34145804; 34592197; |
| Motif | MOTIF 177..184; /note=Cysteine switch; /evidence=ECO:0000250; MOTIF 828..834; /note=SH3-binding; class II; /evidence=ECO:0000250; MOTIF 834..841; /note=SH3-binding; class I; /evidence=ECO:0000250; MOTIF 885..891; /note=SH3-binding; class I; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 99,542 |
| Kinetics | |
| Metal Binding | METAL 179; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 350; /note=Zinc; catalytic; METAL 354; /note=Zinc; catalytic; METAL 360; /note=Zinc; catalytic |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B10; |