| IED ID | IndEnz0002018309 |
| Enzyme Type ID | protease018309 |
| Protein Name |
Calcium-activated chloride channel regulator 1 EC 3.4.-.- Calcium-activated chloride channel family member 3 mCLCA3 Protein gob-5 |
| Gene Name | Clca1 Clca3 Gob5 |
| 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 | MESLKSPVFLLILHLLEGVLSESLIQLNNNGYEGIVIAIDHDVPEDEALIQHIKDMVTQASPYLFEATGKRFYFKNVAILIPESWKAKPEYTRPKLETFKNADVLVSTTSPLGNDEPYTEHIGACGEKGIRIHLTPDFLAGKKLTQYGPQDRTFVHEWAHFRWGVFNEYNNDEKFYLSKGKPQAVRCSAAITGKNQVRRCQGGSCITNGKCVIDRVTGLYKDNCVFVPDPHQNEKASIMFNQNINSVVEFCTEKNHNQEAPNDQNQRCNLRSTWEVIQESEDFKQTTPMTAQPPAPTFSLLQIGQRIVCLVLDKSGSMLNDDRLNRMNQASRLFLLQTVEQGSWVGMVTFDSAAYVQSELKQLNSGADRDLLIKHLPTVSAGGTSICSGLRTAFTVIKKKYPTDGSEIVLLTDGEDNTISSCFDLVKQSGAIIHTVALGPAAAKELEQLSKMTGGLQTYSSDQVQNNGLVDAFAALSSGNAAIAQHSIQLESRGVNLQNNQWMNGSVIVDSSVGKDTLFLITWTTHPPTIFIWDPSGVEQNGFILDTTTKVAYLQVPGTAKVGFWKYSIQASSQTLTLTVTSRAASATLPPITVTPVVNKNTGKFPSPVTVYASIRQGASPILRASVTALIESVNGKTVTLELLDNGAGADATKNDGVYSRFFTAFDANGRYSVKIWALGGVTSDRQRAAPPKNRAMYIDGWIEDGEVRMNPPRPETSYVQDKQLCFSRTSSGGSFVATNVPAAAPIPDLFPPCQITDLKASIQGQNLVNLTWTAPGDDYDHGRASNYIIRMSTSIVDLRDHFNTSLQVNTTGLIPKEASSEEIFEFELGGNTFGNGTDIFIAIQAVDKSNLKSEISNIARVSVFIPAQEPPIPEDSTPPCPDISINSTIPGIHVLKIMWKWLGEMQVTLGLH |
| Enzyme Length | 913 |
| Uniprot Accession Number | Q9D7Z6 |
| Absorption | |
| Active Site | ACT_SITE 157; /evidence=ECO:0000250|UniProtKB:A8K7I4 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: May be involved in mediating calcium-activated chloride conductance. May play critical roles in goblet cell metaplasia, mucus hypersecretion, cystic fibrosis and AHR. May be involved in the regulation of mucus production and/or secretion by goblet cells. Involved in the regulation of tissue inflammation in the innate immune response. May play a role as a tumor suppressor. Induces MUC5AC. {ECO:0000269|PubMed:11296262, ECO:0000269|PubMed:11694454, ECO:0000269|PubMed:16645179}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Glycosylation (6); Metal binding (3); Region (1); Sequence conflict (1); Signal peptide (1); Site (1) |
| Keywords | Autocatalytic cleavage;Calcium;Calcium transport;Chloride;Glycoprotein;Hydrolase;Ion transport;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Transport;Zinc |
| Interact With | |
| Induction | INDUCTION: By IL3, IL4 and IL9 in the lung. Increases in the bronchiolar epithelium of asbestos-induced fibrogenesis. Decreases in cystic fibrosis knockout mice. {ECO:0000269|PubMed:11694454, ECO:0000269|PubMed:16099848, ECO:0000269|PubMed:16251409}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:12019299, ECO:0000269|PubMed:15919655, ECO:0000269|PubMed:16895902}. Note=The 75 kDa N-terminal and a 35 kDa C-terminal products are fully secreted into extracellular environment as a soluble complex of two glycoproteins. |
| Modified Residue | |
| Post Translational Modification | PTM: The 110 kDa translation product is autoproteolytically cleaved by the metalloprotease domain in the endoplasmic reticulum into a 75 kDa N-terminal and a 35 kDa C-terminal products that remain physically associated with each other. The cleavage is necessary for calcium-activated chloride channel (CaCC) activation activity. {ECO:0000250|UniProtKB:A8K7I4, ECO:0000269|PubMed:12019299}.; PTM: Glycosylated. {ECO:0000269|PubMed:12019299, ECO:0000269|PubMed:16895902}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10828589; 11217851; 12466851; 12568493; 15163632; 15947424; 16569774; 16868010; 16936271; 16985003; 17522155; 18923035; 19210762; 20479003; 20819519; 21267068; 22080371; 22362387; 22675208; 23213461; 23266329; 23449471; 23691121; 24033950; 24905173; 25033194; 25855264; 26075897; 26162072; 27010197; 27173853; 27224029; 29610986; 29885864; 31201093; 31570526; 34066250; |
| Motif | |
| Gene Encoded By | |
| Mass | 100,071 |
| Kinetics | |
| Metal Binding | METAL 156; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:A8K7I4; METAL 160; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:A8K7I4; METAL 167; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:A8K7I4 |
| Rhea ID | |
| Cross Reference Brenda |