Detail Information for IndEnz0002001932
IED ID IndEnz0002001932
Enzyme Type ID protease001932
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 Rattus norvegicus (Rat)
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 Rattus Rattus norvegicus (Rat)
Enzyme Sequence MAVLVVLLSSLVSSALANEFSILRSPGSVVFRNGNWPIPGDRIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATIMVTVKGVDKLALPTGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLNSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDELGKRYGEDSEQFRDASRILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLVRKSRTILETKQENTQSPYNLAYKYNLEYSVVFNLVLWIMTGLALAVIITSYNIWNMDPGYDSIIYRMTNQKIRMD
Enzyme Length 350
Uniprot Accession Number Q6AXS4
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 (By similarity). {ECO:0000250|UniProtKB:O75787, ECO:0000250|UniProtKB:Q9CYN9}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (3); Motif (1); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1)
Keywords 3D-structure;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:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, dendritic spine membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000250|UniProtKB:Q9CYN9}. Endosome membrane {ECO:0000250|UniProtKB:Q9CYN9}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32165585}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:32165585}; 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 Electron microscopy (6)
Cross Reference PDB 6VQ6; 6VQ7; 6VQ8; 6VQC; 6VQG; 6VQH;
Mapped Pubmed ID 18326551; 21321306;
Motif MOTIF 346..350; /note=Mediates retrograde transport to the ER; /evidence=ECO:0000250|UniProtKB:O75787
Gene Encoded By
Mass 39,082
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda