| IED ID | IndEnz0002001929 |
| Enzyme Type ID | protease001929 |
| Protein Name |
Renin receptor ATPase H + -transporting lysosomal accessory protein 2 ATPase H + -transporting lysosomal-interacting protein 2 Renin/prorenin receptor Cleaved into: Renin receptor extracellular fragment; Renin receptor cytoplasmic fragment |
| Gene Name | Atp6ap2 Atp6ip2 |
| 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 | MAVLVVLLFFLVAGALGNEFSILRSPGSVVFRNGNWPIPGDRIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATIMVMVKGVDKLALPAGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSLLNSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDELGKRYGEDSEQFRDASKILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLVRKSRTILEAKQENTQSPYNLAYKYNLEYSVVFNLVLWIMIGLALAVIITSYNIWNMDPGYDSIIYRMTNQKIRID |
| Enzyme Length | 350 |
| Uniprot Accession Number | Q9CYN9 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (By similarity). May mediate renin-dependent cellular responses by activating ERK1 and ERK2 (By similarity). By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, may also play a role in the renin-angiotensin system (RAS) (By similarity). Through its function in V-type ATPase (v-ATPase) assembly and acidification of the lysosome it regulates protein degradation and may control different signaling pathways important for proper brain development, synapse morphology and synaptic transmission (PubMed:26376863, PubMed:29127204, PubMed:30985297). {ECO:0000250|UniProtKB:O75787, ECO:0000269|PubMed:26376863, ECO:0000269|PubMed:29127204, ECO:0000269|PubMed:30985297}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Motif (1); Sequence conflict (2); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) |
| Keywords | Cell junction;Cell membrane;Cell projection;Cleavage on pair of basic residues;Cytoplasmic vesicle;Endoplasmic reticulum;Endosome;Lysosome;Membrane;Phosphoprotein;Postsynaptic cell membrane;Receptor;Reference proteome;Signal;Synapse;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26376863}; Single-pass type I membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:26376863, ECO:0000269|PubMed:30985297}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:26376863}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, dendritic spine membrane {ECO:0000269|PubMed:26376863}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:26376863}. Endosome membrane {ECO:0000269|PubMed:30985297}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q6AXS4}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q6AXS4}; Single-pass type I membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: Phosphorylated. {ECO:0000250|UniProtKB:O75787}.; PTM: Proteolytically cleaved by a furin-like convertase in the trans-Golgi network to generate N- and C-terminal fragments. {ECO:0000250|UniProtKB:O75787}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 12520002; 12904583; 14610273; 15226823; 18799693; 18974301; 19474391; 19765626; 19879325; 20093472; 20570919; 21267068; 21737546; 22034640; 22052048; 22203739; 22526255; 23357953; 23516464; 23704941; 23734002; 24223829; 24246383; 24305829; 24400720; 24451661; 24830537; 24990896; 25046440; 25074986; 25249154; 25463323; 25810528; 25903133; 25994957; 25995108; 26063165; 26081285; 26272612; 26658320; 26824839; 27000064; 27044666; 27053687; 27185751; 28031172; 28129027; 28215051; 28814438; 28851918; 29473106; 29488348; 29611334; 29667908; 29790390; 30118514; 30142028; 30317586; 30550352; 30925093; 30943054; 30965084; 31042081; 31274353; 31282603; 31406124; 31527264; 31800607; 32174138; 32228320; 32423811; 33459178; 33890822; 34024121; 34059756; 34534267; 9556572; |
| Motif | MOTIF 346..350; /note=Mediates retrograde transport to the ER; /evidence=ECO:0000250|UniProtKB:O75787 |
| Gene Encoded By | |
| Mass | 39,092 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |