| IED ID | IndEnz0002018321 |
| Enzyme Type ID | protease018321 |
| Protein Name |
Calcium-activated chloride channel regulator 2 EC 3.4.-.- Calcium-activated chloride channel family member 5 mCLCA5 |
| Gene Name | Clca2 Clca5 |
| 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 | MTHRDSTGPVIGLKLVTLLFTLSPELLFLGAGLKLKENGYDGLLVAINPRVPEDLKLITNIKEMITEASFYLFNATKRRVFFRNVQILVPATWTDHNYSRVRQESYDKANVIVAEQSEEHGDDPYTLQHRGCGQEGRYIHFTPSFLLNDELAAGYGARGRVFVHEWAHLRWGVFDEYNNDKPFYVNGRNEIQVTRCSSDITGVFVCEKGLCPHEDCIISKIFREGCTFLYNSTQNATGSIMFMPSLPSVVEFCNESTHNQEAPNLQNQVCSLRSTWDVITASSDLNHSLPVHGVGLPAPPTFSLLQAGDRVVCLVIDVSRKMAEGDRLLRLQQAAELYLMQVVEAHTFVGIVTFDSKGEIRASLQQIYSDDDRKLLVSYLPTAVSTDAETNICAGVKKGFEVVEERNGRADGSVLILVTSGADEHIANCLLTSMNSGSTIHSMALGSSAARKVGELSRLTGGLKFFIPDKFTSNGMTEAFVRISSGTGDIFQQSLQVESVCETVQPQHQLADTMTVDSAVGNDTLFLVTWQTGGPPEIALLDPSGRKYNTGDFIINLAFRTASLKIPGTAKHGHWTYTLNNTHHSPQALKVTVASRASSLAMSPATLEAFVERDSTYFPQPVIIYANVRKGLHPILNATVVATVEPEAGDPVVLQLLDGGAGADVIRNDGIYSRYFSSFAVSGSYSLTVHVRHSPSTSTLALPVPGNHAMYVPGYITNDNIQMNAPKNLGHRPVKERWGFSRVSSGGSFSVLGVPDGPHPDMFPPCKITDLEAMKVEDDVVLSWTAPGEDFDQGQTTSYEIRMSRSLWNIRDDFDNAILVNSSELVPQHAGTRETFTFSPKLVTHELDHELAEDAQEPYIVYVALRAMDRSSLRSAVSNIALVSMSLPPNSSPVVSRDDLILKGVLTTVGLIAILCLIMVVAHCIFNRKKRPSRKENETKFL |
| Enzyme Length | 942 |
| Uniprot Accession Number | Q8BG22 |
| Absorption | |
| Active Site | ACT_SITE 165; /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, and cell adhesion. Involved in basal cell adhesion and/or stratification of squamous epithelia. May act as a tumor suppressor in breast and colorectal cancer. Plays a key role for cell adhesion in the beginning stages of lung metastasis via the binding to ITGB4. {ECO:0000269|PubMed:15284223, ECO:0000269|PubMed:15292178}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Chain (1); Domain (1); Glycosylation (10); Metal binding (3); Region (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;Autocatalytic cleavage;Calcium;Cell adhesion;Cell junction;Cell membrane;Chloride;Glycoprotein;Hydrolase;Ion transport;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix;Transport;Zinc |
| Interact With | |
| Induction | INDUCTION: By 30-fold when cells are deprived of growth factors or anchorage in mammary epithelial cell. Down-regulated in metastatic mammary tumor cell lines. {ECO:0000269|PubMed:15292178}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15284223}; Single-pass type I membrane protein {ECO:0000269|PubMed:15284223}. Basal cell membrane {ECO:0000269|PubMed:15284223}; Single-pass type I membrane protein {ECO:0000269|PubMed:15284223}. Cell junction {ECO:0000269|PubMed:15284223}. |
| Modified Residue | |
| Post Translational Modification | PTM: The translation product is autoproteolytically cleaved by the metalloprotease domain in the endoplasmic reticulum into a N-terminal and a 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}.; PTM: N-glycosylated. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..32; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16569774; 19210762; 20012443; 21267068; 21862448; 22647633; 25828855; 26075897; 27711075; 29743348; |
| Motif | |
| Gene Encoded By | |
| Mass | 103,626 |
| Kinetics | |
| Metal Binding | METAL 164; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:A8K7I4; METAL 168; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:A8K7I4; METAL 175; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:A8K7I4 |
| Rhea ID | |
| Cross Reference Brenda |