Detail Information for IndEnz0002016551
IED ID IndEnz0002016551
Enzyme Type ID protease016551
Protein Name Disintegrin and metalloproteinase domain-containing protein 12
ADAM 12
EC 3.4.24.-
Meltrin-alpha
Gene Name Adam12 Mltna
Organism Mus musculus (Mouse)
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 Mus Mus Mus musculus (Mouse)
Enzyme Sequence MAERPARRAPPARALLLALAGALLAPRAARGMSLWDQRGTYEVARASLLSKDPGIPGQSIPAKDHPDVLTVQLQLESRDLILSLERNEGLIANGFTETHYLQDGTDVSLTRNHTDHCYYHGHVQGDAASVVSLSTCSGLRGLIMFENKTYSLEPMKNTTDSYKLVPAESMTNIQGLCGSQHNKSNLTMEDVSPGTSQMRARRHKRETLKMTKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDIDKCSISQDPFTSLHEFLDWRKIKLLPRKSHDNAQLISGVYFQGTTIGMAPIMSMCTAEQSGGVVMDHSDSPLGAAVTLAHELGHNFGMNHDTLERGCSCRMAAEKGGCIMNPSTGFPFPMVFSSCSRKDLEASLEKGMGMCLFNLPEVKQAFGGRKCGNGYVEEGEECDCGEPEECTNRCCNATTCTLKPDAVCAHGQCCEDCQLKPPGTACRGSSNSCDLPEFCTGTAPHCPANVYLHDGHPCQGVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKDSKSAFAKCELRDAKCGKIQCQGGASRPVIGTNAVSIETNIPQQEGGRILCRGTHVYLGDDMPDPGLVLAGTKCAEGKICLNRRCQNISVFGVHKCAMQCHGRGVCNNRKNCHCEAHWAPPFCDKFGFGGSTDSGPIRQADNQGLTVGILVSILCLLAAGFVVYLKRKTLMRLLFTHKKTTMEKLRCVHPSRTPSGPHLGQAHHTPGKGLLMNRAPHFNTPKDRHSLKCQNMDISRPLDARAVPQLQSPQRVLLPLHQTPRAPSGPARPLPASPAVRQAQGIRKPSPPQKPLPADPLSRTSRLTSALVRTPGQQEPGHRPAPIRPAPKHQVPRPSHNAYIK
Enzyme Length 903
Uniprot Accession Number Q61824
Absorption
Active Site ACT_SITE 349; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095"
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.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (7); Domain (3); Glycosylation (7); Metal binding (4); Modified residue (1); Motif (6); Propeptide (1); Region (2); Sequence conflict (3); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords Cell adhesion;Cleavage on pair of basic residues;Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;SH3-binding;Signal;Transmembrane;Transmembrane helix;Zinc;Zymogen
Interact With P35609
Induction INDUCTION: At the onset of myoblast fusion.
Subcellular Location SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
Modified Residue MOD_RES 901; /note=Phosphotyrosine; by SRC; /evidence=ECO:0000305|PubMed:11127814
Post Translational Modification PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
Signal Peptide SIGNAL 1..31; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10527948; 12000741; 12000744; 12414501; 12466851; 12482960; 12615925; 12915458; 12972593; 14993236; 15063736; 15637293; 15849365; 15907280; 15930294; 15936750; 16054021; 16079176; 16141072; 16602821; 16607276; 16869727; 16916601; 17072319; 17107962; 17344430; 17620406; 17653278; 17982130; 18241035; 19398663; 19581512; 19841944; 20457602; 20660068; 21062905; 21267068; 21491542; 21875931; 23458101; 23686306; 24006456; 24103556; 24336287; 24798404; 25892053; 26163448; 26242473; 26975138; 27487498; 29846135; 30042416; 30389854; 30753595; 30993375; 31774689; 32913205; 33952697; 9461614;
Motif MOTIF 175..182; /note=Cysteine switch; /evidence=ECO:0000250; MOTIF 824..830; /note=SH3-binding; class II; MOTIF 830..837; /note=SH3-binding; class I; MOTIF 846..852; /note=SH3-binding; class II; MOTIF 852..858; /note=SH3-binding; class I; MOTIF 881..887; /note=SH3-binding; class I
Gene Encoded By
Mass 98,504
Kinetics
Metal Binding METAL 177; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 348; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 352; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 358; /note=Zinc; catalytic; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda 3.4.24.B10;