IED ID | IndEnz0002018312 |
Enzyme Type ID | protease018312 |
Protein Name |
Calcium-activated chloride channel regulator 1 EC 3.4.-.- Calcium-activated chloride channel family member 1 pCLCA1 |
Gene Name | CLCA1 AECC |
Organism | Sus scrofa (Pig) |
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 Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
Enzyme Sequence | MGSFRSSLFILVLHLLEGAQSNSLIQLNGNGYEGIVIAIDPNVPEDERLIQNIKDMVTKASPYLFEATEKRFYFKNVAILIPASWKAKPEYVKPKLETYKNADVVVTEPNPPENDGPYTEQMGNCGEKGEKIYFTPDFVAGKKVLQYGPQGRVFVHEWAHLRWGVFNEYNNEQKFYLSNKKEQPVICSAAIRGTNVLPQCQGGSCVTKPCRADRVTGLFQKECEFIPDPQQSEKASIMFAQSIDTVVEFCKEKNHNKEAPNDQNQKCNLRSTWEVIQDSEDFKKTTPMTTQPPAPTFSLLQIGQRIVCLVLDKSGSMTVGGRLKRLNQAGKLFLLQTVEQGAWVGMVAFDSAAYVKSELVQINSAAERDALARSLPTAASGGTSICSGLRSAFTVIKKKYPTDGSEIVLLTDGEDNTISACFPEVKQNGAIIHTVALGPSAAKELEELSQMTGGLQTYASDQAENNGLIDAFGALSSGNRAASQRSIQLESQGLTLQNNEWMNGTVVVDSTVGKDTLFLITLERKFLSPIPFFGVPSGRSQDSFLVGKHNKMAYFQVPGTAKVGMWKYSLQASSQTLTLTVSSRRSSATLPPVTVTSKMNKDTGKFPSPMVVYTKIHQGTLPILRAKVTALIESENGKTVTLELLDNGAGADATKNDGIYSRYFTAYDANGRYSVKVWALGGVNTPRRRAPPLWSGAMYIRGWIENGEIKWNPPRPDINKDDLQGKQVCFSRTASGGSFVASDVPKSPIPDLFPPCKITDLKAGIQGDNLINLTWTAPGDDYDHGRADRYIIRISTNILDLRDKFNDSVQVNTTDLIPKEANSEEVFVFKPEGIPFTNGTDLFIAVQAVDKTNLKSEISNIAQVSLFLPPEAPPETPPETPAPSLPCPEIQVNSTIPGIHILKIMWKWLGELQLSIA |
Enzyme Length | 917 |
Uniprot Accession Number | Q9TUB5 |
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. Induces a cAMP-dependent chloride conductance possibly through effects on CFTR in colon carcinoma cells. {ECO:0000269|PubMed:11015605, ECO:0000269|PubMed:12107050, ECO:0000269|PubMed:12408984, ECO:0000269|PubMed:14988065}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Domain (1); Glycosylation (6); Metal binding (3); Region (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 | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | PTM: Glycosylated. {ECO:0000250}.; 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}. |
Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 19755716; |
Motif | |
Gene Encoded By | |
Mass | 100,736 |
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 |