| IED ID | IndEnz0002001930 |
| Enzyme Type ID | protease001930 |
| Protein Name |
ATPase H + -transporting accessory protein 2 Renin homolog receptor dPRR Cleaved into: ATPase H + -transporting accessory protein 2 N-terminal fragment; ATPase H + -transporting accessory protein 2 C-terminal fragment |
| Gene Name | ATP6AP2 VhaM8-9 VhaM8.9 VhaPRR CG8444 |
| Organism | Drosophila melanogaster (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly) |
| Enzyme Sequence | MLRVFVIFSLFIAAINASGEFTVLNRPKAISFKGNDALESHYVGDVLYASMGNAVSGDTNWNGLTINDPFNLAKGVILVHVQGIGHVTTAGNVKTYELTGSGTDASLNALAAELEAANEPVCDINFEQFDDGVQAWKSCFGDFEAPAAKPTKHLNPSLHTADKQFLQEVGFINSAADHLAEMAKPSNVLMLRVSVDGVAKAHGEKSVAVEEANKLLSAAISRLLAASQKSSDSVLFVQTTEKDVAASRAKRDTIAASTTNPYNLAVYYGSDYPVIFNIILWFMVVFGLSLLAICYAIAAMDPGRDSIIYRMTSTRIKKDN |
| Enzyme Length | 320 |
| Uniprot Accession Number | Q9VHG4 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Multifunctional protein which functions as transmembrane receptor in the planar cell polarity (PCP) and is involved in the assembly of the proton-transporting vacuolar (V)-ATPase protein pump (PubMed:20579883, PubMed:20579879, PubMed:29127204, PubMed:29995586). As transmembrane receptor mediates fz/PCP signaling through interaction with fz and stabilizes asymmetric PCP domains through its interaction with stan (PubMed:20579883, PubMed:20579879, PubMed:23292348, PubMed:29995586). Also mediates Wnt/beta-cat signaling through interaction with fz/fz2 (PubMed:20579883, PubMed:20579879). Probably by controlling the assembly of the V-ATPase pump and thus the acidification of the endo-lysosomal system, plays a role in many neuronal processes including synapse morphology and synaptic transmission (PubMed:26376863). {ECO:0000269|PubMed:20579879, ECO:0000269|PubMed:20579883, ECO:0000269|PubMed:23292348, ECO:0000269|PubMed:26376863, ECO:0000269|PubMed:29127204, ECO:0000269|PubMed:29995586}.; FUNCTION: [ATPase H(+)-transporting accessory protein 2 N-terminal fragment]: Stabilizes asymmetric Planar Cell Polarity (PCP) domains through its interaction with stan. {ECO:0000269|PubMed:23292348}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Motif (1); Mutagenesis (5); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) |
| Keywords | Cell membrane;Cleavage on pair of basic residues;Endoplasmic reticulum;Golgi apparatus;Membrane;Receptor;Reference proteome;Secreted;Signal;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [ATPase H(+)-transporting accessory protein 2]: Cell membrane {ECO:0000269|PubMed:20579879, ECO:0000269|PubMed:20579883}; Single-pass type I membrane protein {ECO:0000269|PubMed:20579883}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20579883, ECO:0000269|PubMed:23292348, ECO:0000269|PubMed:29995586}; Single-pass type I membrane protein {ECO:0000269|PubMed:20579883}. Vesicle {ECO:0000269|PubMed:23292348}. Apical cell membrane {ECO:0000269|PubMed:23292348}; Single-pass type I membrane protein {ECO:0000269|PubMed:23292348}. Golgi apparatus membrane {ECO:0000269|PubMed:29995586}; Single-pass type I membrane protein {ECO:0000269|PubMed:29995586}. Note=Co-localizes at the apical junctions with stan. {ECO:0000269|PubMed:23292348}.; SUBCELLULAR LOCATION: [ATPase H(+)-transporting accessory protein 2 N-terminal fragment]: Secreted {ECO:0000269|PubMed:23292348}. Note=Localization to the planar cell polarity domains depends by stan. {ECO:0000269|PubMed:23292348}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved by a furin-like convertase in the trans-Golgi network to generate N- and C-terminal fragments (PubMed:23292348, PubMed:29127204). Cleavage is reduced in the fat body (PubMed:29127204). {ECO:0000269|PubMed:23292348, ECO:0000269|PubMed:29127204}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15855386; 17194782; 17660546; 20220848; 20371351; 20540764; 21074052; 23071443; 24400720; 24502977; 24506874; 24780858; 24953654; 25312911; 25580252; 25959678; 26092939; 26173873; 26551273; 26761346; 26870755; 27172210; 30111579; 30804504; 31722958; 31875549; 32196731; 32901612; 34620624; |
| Motif | MOTIF 317..320; /note="Mediates retrograde transport to the ER"; /evidence="ECO:0000269|PubMed:29127204, ECO:0000269|PubMed:29995586" |
| Gene Encoded By | |
| Mass | 34,421 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |