IED ID | IndEnz0002017970 |
Enzyme Type ID | protease017970 |
Protein Name |
Calcium-activated chloride channel regulator 4A EC 3.4.-.- Calcium-activated chloride channel regulator 6 mClca6 Cleaved into: Calcium-activated chloride channel regulator 4A, 110 kDa form; Calcium-activated chloride channel regulator 4A, 30 kDa form |
Gene Name | Clca4a Clca6 |
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 | MAFSRGPVFLLLLLYLLWGSDTSLIRLNENGYEDIIIAIDPAVPEDTTIIEHIKGMVTKASTYLFEATEKRFFFKNVSILIPESWKDSPQYRRPKQESYKHADIKVAPPTVEGRDEPYTRQFTQCEEKAEYIHFTPDFVLGRKQDEYGDSGKVLVHEWAHLRWGVFDEYNEDQPFYSASSKKIEATRCSTGITGTNRVYACQGGSCAMRRCRTNSTTKLYEKDCQFFPDKVQSEKASIMFMQSIDSVTEFCKKENHNREAPTLHNKKCNYRSTWEVISTSEDFNSSTPMETSPSPPFFSLLRISERIMCLVLDVSGSMTSYDRLNRMNQAAKYFLSQIIENRSWVGMVHFSSQATIVHELIQINSDIERNQLLQTLPTSANGGTSICSGIKAAFQVFKNGEYQTDGTEILLLSDGEDSTAKDCIDEVKDSGSIVHFIALGPLADLAVTNMSILTGGNHKLATDEAQNNGLIDAFGALASENADITQKSLQLESKGAILNNSLWLNDTVVIDSTLGRDTFFLVTWSKQAPAIYLRDPKGTQTTNFTMDSASKMAYLSIPGTAQVGVWTYNLEAKENSEILTITVTSRAANSSVPPITVNAKVNTDTNTFPSPMIVYAEVLQGYTPIIGARVTATIESNSGKTEELVLLDNGAGADAFKDDGVYSRFFTAYSVNGRYSLKVRADGGRNSARRSLRHPSSRAAYIPGWVVDGEIQGNPPRPETTEATQPVLENFSRTASGGAFVVSNVPSGPLPDLYPPNQITDLQATLDGEEISLTWTAPGDDYDVGRVQQYIIRTSKNIIELRDNFNNSPRVDTTNLTPKEANSEETFAFKPENITEENATYIFIAIESVDKSSLSSGPSNIAQVALFTPQAEPDPDESPSSSGVSVATIVLSVLGALVLVCIIVGTTICILKNKRSSSAAITKF |
Enzyme Length | 924 |
Uniprot Accession Number | Q6Q473 |
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. {ECO:0000269|PubMed:15284223, ECO:0000269|PubMed:18285349}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Alternative sequence (2); Chain (3); Domain (1); Glycosylation (12); Metal binding (3); Region (1); Signal peptide (1); Site (1); Transmembrane (1) |
Keywords | Alternative splicing;Autocatalytic cleavage;Cell membrane;Chloride;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Transmembrane;Transmembrane helix;Transport;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. Apical cell membrane. Secreted. Note=The C-terminus 30 kDa form is anchored to the membrane. The N-terminus 110 kDa form is released from the membrane triggered by an unknown stimulus. Associated with the microvilli of non-goblet cell enterocytes in the small and large intestine. Colocalizes with CFTR. |
Modified Residue | |
Post Translational Modification | PTM: N-Glycosylated. {ECO:0000269|PubMed:15284223, ECO:0000269|PubMed:18285349}.; 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..22; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12466851; 16569774; 19210762; 20562862; 22350745; 22647633; |
Motif | |
Gene Encoded By | |
Mass | 101,872 |
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 |