Detail Information for IndEnz0002001931
IED ID IndEnz0002001931
Enzyme Type ID protease001931
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Ponginae Pongo Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Enzyme Sequence MAVFVVLLALVAGVLGNEFSILKSPGSVVFRNGNWPIPGERIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATVMVMVKGVNKLALPPGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLSSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDEIGKRYGEDSEQFRDASKILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLIRKTRTILEAKQAKNPASPYNLAYKYNFEYSVVFNMVLWIMIALALAVIITSYNIWNMDPGYDSIIYRMTNQKIRMD
Enzyme Length 350
Uniprot Accession Number Q5R563
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. May mediate renin-dependent cellular responses by activating ERK1 and ERK2. 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 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:O75787}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75787}. Lysosome membrane {ECO:0000250|UniProtKB:O75787}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75787}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75787}. Cell projection, dendritic spine membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75787}. Cell projection, axon {ECO:0000250|UniProtKB:Q9CYN9}. Endosome membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75787}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q6AXS4}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75787}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q6AXS4}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75787}.
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..16; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 346..350; /note=Mediates retrograde transport to the ER; /evidence=ECO:0000250|UniProtKB:O75787
Gene Encoded By
Mass 39,008
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda