Detail Information for IndEnz0002016807
IED ID IndEnz0002016807
Enzyme Type ID protease016807
Protein Name Collectrin
Transmembrane protein 27
Gene Name Cltrn Nx17 Tmem27
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 MLWALFFLVTTIHAELCHPDAENAFKVRLSIRAALGDKAYVWDTDQEYLFRAMVAFSMRKVPNREATEISHVLLCNITQRVSFWFVVTDPSNNYTLPAAEVQSAIRKNRNRINSAFFLDDHTLEFLKIPSTLAPPMEPSVPVWIIVFGVIFCIVTVAIALLVLSGIRQRRRNNKGPPGVEDAEDKCENIITIENGIPCDPLDMKGGHINDGFLTEDERLTPL
Enzyme Length 222
Uniprot Accession Number Q9ESG4
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Plays an important role in amino acid transport by acting as binding partner of amino acid transporters SLC6A18 and SLC6A19, regulating their trafficking on the cell surface and their activity (PubMed:17167413, PubMed:16985211). May also play a role in trafficking of amino acid transporters SLC3A1 and SLC7A9 to the renal cortical cell membrane (PubMed:16985211). Regulator of SNARE complex function (PubMed:16330323). Stimulator of beta cell replication (PubMed:16330324). {ECO:0000269|PubMed:16330323, ECO:0000269|PubMed:16330324, ECO:0000269|PubMed:16985211, ECO:0000269|PubMed:17167413}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Glycosylation (2); Modified residue (2); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1)
Keywords Cell membrane;Glycoprotein;Membrane;Phosphoprotein;Reference proteome;Signal;Transmembrane;Transmembrane helix
Interact With
Induction INDUCTION: Up-regulated by high glucose concentration in beta-cells (at protein level). {ECO:0000269|PubMed:19715677}.
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16330324, ECO:0000269|PubMed:17167413}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes to the brush border membranes of cells in the proximal tubules of kidney (PubMed:17167413). Colocalizes with SLC6A19 in the early proximal S1 tubule (PubMed:17167413). {ECO:0000269|PubMed:17167413}.
Modified Residue MOD_RES 214; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 220; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:21183079
Post Translational Modification PTM: Glycosylated. Glycosylation is required for plasma membrane localization and for its cleavage by BACE2. {ECO:0000250|UniProtKB:Q9HBJ8}.; PTM: Proteolytically processed in pancreatic beta cells by BACE2 leading to the generation and extracellular release of soluble CLTRN, and a corresponding cell-associated C-terminal fragment which is later cleaved by gamma-secretase (PubMed:16330324, PubMed:21907142). This shedding process inactivates CLTRN (PubMed:16330324). Three cleavage sites have been identified for BACE2, two clustered sites after Phe-116 and Leu-118 and a more membrane proximal site at Phe-125; the preferred BACE2 cleavage site seems to be between Phe-125 and Leu-126, Phe-116 and Leu-118 act as alternative sites (By similarity). {ECO:0000250|UniProtKB:Q9HBJ8, ECO:0000269|PubMed:16330324, ECO:0000269|PubMed:21907142}.
Signal Peptide SIGNAL 1..14; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11217851; 12466851; 15172686; 16615898; 17476336; 17693757; 19185582; 19246514; 20003319; 20562862; 21343540; 21677750; 21814048; 21947380; 22837003; 24048198; 26240152; 26901059; 28159899; 32179912; 33737325;
Motif
Gene Encoded By
Mass 25,070
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda