| IED ID | IndEnz0002016382 |
| Enzyme Type ID | protease016382 |
| Protein Name |
Calcium-activated chloride channel regulator 3A-1 EC 3.4.-.- |
| Gene Name | Clca3a1 Clca1 |
| 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 | MVPGLQVLLFLTLHLLQNTESSMVHLNSNGYEGVVIAINPSVPEDERLIPSIKEMVTQASTYLFEASQGRVYFRNISILVPMTWKSKPEYLMPKRESYDKADVIVADPHLQHGDDPYTLQYGQCGDRGQYIHFTPNFLLTDNLRIYGPRGRVFVHEWAHLRWGVFDEYNVDQPFYMSRKNTIEATRCSTRITGTNVVHNCERGNCVTRACRRDSKTRLYEPKCTFIPDKIQTAGASIMFMQNLNSVVEFCTEKNHNAEAPNLQNKMCNRRSTWDVIKTSADFQNAPPMRGTEAPPPPTFSLLKSRRRVVCLVLDKSGSMDKEDRLIRMNQAAELYLTQIVEKESMVGLVTFDSAAHIQNYLIKITSSSDYQKITANLPQQASGGTSICHGLQAGFQAITSSDQSTSGSEIVLLTDGEDNGIRSCFEAVSRSGAIIHTIALGPSAARELETLSDMTGGLRFYANKDLNSLIDAFSRISSTSGSVSQQALQLESKAFDVRAGAWINGTVPLDSTVGNDTFFVITWMVKKPEIILQDPKGKKYTTSDFQDDKLNIRSARLQIPGTAETGTWTYSITGTKSQLITMTVTTRARSPTMEPLLATAHMSQSTAQYPSRMIVYARVSQGFLPVLGANVTALIEAEHGHQVTLELWDNGAGADTVKNDGIYTRYFTDYHGNGRYSLKVRVQAQRNKTRLSLRQKNKSLYIPGYVENGKIVLNPPRPDVQEEAIEATVEDFNRVTSGGSFTVSGAPPDGDHARVFPPSKVTDLEAEFIGDYIHLTWTAPGKVLDNGRAHRYIIRMSQHPLDLQEDFNNATLVNASSLIPKEAGSKETFKFKPETFKIANGIQLYIAIQADNEASLTSEVSNIAQAVKLTSLEDSISALGDDISAISMTIWGLTVIFNSILN |
| Enzyme Length | 902 |
| Uniprot Accession Number | Q9QX15 |
| Absorption | |
| Active Site | ACT_SITE 156; /evidence=ECO:0000250|UniProtKB:A8K7I4 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Plays a role in modulating chloride current across the plasma membrane in a calcium-dependent manner. {ECO:0000269|PubMed:10072771, ECO:0000269|PubMed:9822685}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Glycosylation (8); Metal binding (3); Region (1); Sequence conflict (9); Signal peptide (1); Site (1) |
| Keywords | Autocatalytic cleavage;Calcium;Cell membrane;Chloride;Glycoprotein;Hydrolase;Ion transport;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Transport;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000269|PubMed:9822685}.; PTM: The 130-kDa product is autoproteolytically processed by the metalloprotease domain and yields two subunits, a 90-kDa protein and a group of 32- to 38-kDa proteins (PubMed:9822685). The cleavage is necessary for calcium-activated chloride channel (CaCC) activation activity (By similarity). {ECO:0000250|UniProtKB:A8K7I4, ECO:0000269|PubMed:9822685}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10828589; 11217851; 11483609; 11994272; 12110680; 12122442; 12466851; 12944538; 16075368; 16569774; 16985003; 17111356; 17130451; 18616988; 19210762; 20385786; 20937843; 21267068; 22647633; 25899321; 29081444; 32586976; 4309975; |
| Motif | |
| Gene Encoded By | |
| Mass | 100,108 |
| Kinetics | |
| Metal Binding | METAL 155; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:A8K7I4; METAL 159; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:A8K7I4; METAL 166; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:A8K7I4 |
| Rhea ID | |
| Cross Reference Brenda |