| IED ID | IndEnz0002014382 |
| Enzyme Type ID | protease014382 |
| Protein Name |
Polyamine-transporting ATPase 13A2 EC 7.6.2.- |
| Gene Name | Atp13a2 |
| 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 | MSADSSLLMGSTPPSYGTLTTGTSIDPLSSSASSVRLSGYCGSPWRAIGYHAAVWMLAGIPWLLFRWKPLWGVRLRLKPCSLAHAETLVIEIKDKEGSSRQLFTVQVQTEAVVQGSLELPPQAQAEDGRSQAAVGVTPEGTWQDTSELHRQEEAKQVLRYYVLQGQRYVWMETQQAFCQVSLLDHGRTCDDVHCSSSGLSLQDQATRKTIYGPNVISIPVKSYLQLLADEALNPYYGFQAFSIALWLADHYYWYALCIFLISAISICLALYKTRKQSLTLRDMVKLSVRVQVCRPGGEEEWVDSSELVPGDCLVLPQEGGVMPCDAALVAGECVVNESSLTGESTPVLKTALPEGPKPYCPETHRRHTLFCGTLILQARAYVGPRVLAVVTRTGFCTAKGGLVSSILHPRPISFKFYKHSMKFVAALSVLALLGTVYSIIILYRNRVPVREIVIRALDLVTVVVPPALPAAMTVCTLYAQSRLRTQGIFCIHPLRINLGGKLRLVCFDKTGTLTEDGLDVMGVVPLKGQVLLPLVPEPCHLPLGPLLRALATCHALSQLHDTPVGDPMDLKMVESTGWVLEEGPAAGSAPGSQVLVVMRPPPGGPRQQEEPPVPVSVLCRFPFSSALQRMDVVVTWPGATQPEAYVKGSPELVASLCSPETVPSDFSQVLQSYTAAGYRVVALAGKPLPIAPSLAAAQQLTRDTVERELSLLGLLVMRNLLKPQTAPVIQTLRKTGIRTVMVTGDNLQTAVTVARACGMVGAQEHLAVIHATHPEQGQPAALEFLPTESSAVMNGAKATGYPTVPEPQSCHLALSGSTFAVLRKHFPKLLPKVLVQATVFARMAPEQKTELVCELQRLQYCVGMCGDGANDCGALKAADVGISLSQAEASVVSPFTSSMASIECVPTVIREGRCSLDTSFSVFKYMALYSLTQFISVLILYTINTNLGDLQFLAIDLVITTTVAVLMSRTGPALTLVRARPPGALLSVPVLGSLLLQVALVAGIQLGGYFLVIAQPWFVPLNRTVPAPDNLPNYENTVVFSLSGFQYLILAAAVSKGAPFRQPLYTNVPFLVALALLGSVLVGLILVPGLLQGPLGLRNIVDSSFKLLLLGLVAFNFVGAFMLESVLDQCLPACLRWLRPKRASKKQFKRLQQELAEHPWPTLPVGSVR |
| Enzyme Length | 1169 |
| Uniprot Accession Number | Q9CTG6 |
| Absorption | |
| Active Site | ACT_SITE 508; /note=4-aspartylphosphate intermediate; /evidence=ECO:0000250|UniProtKB:Q9NQ11 |
| Activity Regulation | ACTIVITY REGULATION: Accumulates in an inactive autophosphorylated state. The presence of spermine results in a dose-dependent reduction in autophosphorylation. {ECO:0000250|UniProtKB:Q9NQ11}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + H2O + spermidine(out) = ADP + H(+) + phosphate + spermidine(in); Xref=Rhea:RHEA:29999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57834, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9NQ11}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + spermine(out) = ADP + H(+) + phosphate + spermine(in); Xref=Rhea:RHEA:63368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:45725, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9NQ11}; |
| DNA Binding | |
| EC Number | 7.6.2.- |
| Enzyme Function | FUNCTION: ATPase which acts as a lysosomal polyamine exporter with high affinity for spermine (By similarity). Also stimulates cellular uptake of polyamines and protects against polyamine toxicity (By similarity). Plays a role in intracellular cation homeostasis and the maintenance of neuronal integrity (By similarity). Contributes to cellular zinc homeostasis (By similarity). Confers cellular protection against Mn(2+) and Zn(2+) toxicity and mitochondrial stress (By similarity). Required for proper lysosomal and mitochondrial maintenance (By similarity). Regulates the autophagy-lysosome pathway through the control of SYT11 expression at both transcriptional and post-translational levels (PubMed:27278822). Facilitates recruitment of deacetylase HDAC6 to lysosomes to deacetylate CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy (PubMed:30538141). Promotes secretion of exosomes as well as secretion of SCNA via exosomes (By similarity). Plays a role in lipid homeostasis (By similarity). {ECO:0000250|UniProtKB:Q9NQ11, ECO:0000269|PubMed:27278822, ECO:0000269|PubMed:30538141}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Glycosylation (1); Intramembrane (1); Metal binding (2); Sequence conflict (8); Topological domain (12); Transmembrane (10) |
| Keywords | ATP-binding;Cytoplasmic vesicle;Endosome;Glycoprotein;Lysosome;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Translocase;Transmembrane;Transmembrane helix;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9NQ11}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q9NQ11}; Multi-pass membrane protein {ECO:0000255}. Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:Q9NQ11}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q9NQ11}; Multi-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | PTM: Autophosphorylated. Accumulates in an inactive autophosphorylated state and autophosphorylation is stimulated by phosphatidic acid and phosphatidylinositol 3,5-bisphosphate but not by Mn(2+) or Zn(2+). The presence of spermine results in a dose-dependent reduction in autophosphorylation. {ECO:0000250|UniProtKB:Q9NQ11}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 14610273; 15381061; 17614941; 21267068; 21308776; 21677750; 22186024; 22198378; 22442086; 23393156; 24194600; 24334770; 25392495; 25855184; 26848562; 27619535; 27770614; 28595912; 29407413; 29859891; 34536552; |
| Motif | |
| Gene Encoded By | |
| Mass | 126,443 |
| Kinetics | |
| Metal Binding | METAL 867; /note=Magnesium; /evidence=ECO:0000250; METAL 871; /note=Magnesium; /evidence=ECO:0000250 |
| Rhea ID | RHEA:29999; RHEA:63368 |
| Cross Reference Brenda |