P98197 · AT11A_MOUSE
- ProteinPhospholipid-transporting ATPase IH
- GeneAtp11a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1187 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of the plasma membrane (By similarity).
Does not show flippase activity toward phosphatidylcholine (PC) (By similarity).
Contributes to the maintenance of membrane lipid asymmetry with a specific role in morphogenesis of muscle cells. In myoblasts, mediates PS enrichment at the inner leaflet of plasma membrane, triggering PIEZO1-dependent Ca2+ influx and Rho GTPases signal transduction, subsequently leading to the assembly of cortical actomyosin fibers and myotube formation (PubMed:29799007).
Does not show flippase activity toward phosphatidylcholine (PC) (By similarity).
Contributes to the maintenance of membrane lipid asymmetry with a specific role in morphogenesis of muscle cells. In myoblasts, mediates PS enrichment at the inner leaflet of plasma membrane, triggering PIEZO1-dependent Ca2+ influx and Rho GTPases signal transduction, subsequently leading to the assembly of cortical actomyosin fibers and myotube formation (PubMed:29799007).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
- a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
Cofactor
Features
Showing features for active site, binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 414 | 4-aspartylphosphate intermediate | ||||
Sequence: D | ||||||
Binding site | 414 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 414 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 415 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 416 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 416 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Site | 457-458 | Cleavage; by CASP3 | ||||
Sequence: DS | ||||||
Site | 493-494 | Cleavage; by CASP3 | ||||
Sequence: DG | ||||||
Binding site | 513 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 555 | ATP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 578 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 609 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 689 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 690 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 691 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 801 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 807 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 828 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 831 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 832 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 832 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | early endosome | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | Golgi apparatus | |
Cellular Component | phospholipid-translocating ATPase complex | |
Cellular Component | plasma membrane | |
Cellular Component | recycling endosome | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATPase-coupled intramembrane lipid transporter activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphatidylethanolamine flippase activity | |
Molecular Function | phosphatidylserine flippase activity | |
Molecular Function | phosphatidylserine floppase activity | |
Biological Process | in utero embryonic development | |
Biological Process | phospholipid translocation | |
Biological Process | positive regulation of myotube differentiation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhospholipid-transporting ATPase IH
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP98197
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Note: Efficient exit from the endoplasmic reticulum requires the presence of TMEM30A.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-61 | Cytoplasmic | ||||
Sequence: MDCSLLRTLVRRYCAGEENWVDSRTIYVGHKEPPPGAEAYIPQRYPDNRIVSSKYTFWNFI | ||||||
Transmembrane | 62-82 | Helical | ||||
Sequence: PKNLFEQFRRIANFYFLIIFL | ||||||
Topological domain | 83-88 | Extracellular | ||||
Sequence: VQLIID | ||||||
Transmembrane | 89-110 | Helical | ||||
Sequence: TPTSPVTSGLPLFFVITVTAIK | ||||||
Topological domain | 111-296 | Cytoplasmic | ||||
Sequence: QGYEDWLRHKADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRADGTCHVTTASLDGESSHKTHYAVQDTKGFHTEADVDSLHATIECEQPQPDLYKFVGRINVYNDLNDPVVRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNTF | ||||||
Transmembrane | 297-318 | Helical | ||||
Sequence: LIVYLCILVSKALINTVLKYVW | ||||||
Topological domain | 319-349 | Extracellular | ||||
Sequence: QSEPFRDEPWYNEKTESERQRNLFLRAFTDF | ||||||
Transmembrane | 350-372 | Helical | ||||
Sequence: LAFMVLFNYIIPVSMYVTVEMQK | ||||||
Topological domain | 373-884 | Cytoplasmic | ||||
Sequence: FLGSYFITWDEDMFDEEMGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMAFKECCIEGHVYVPHVICNGQVLPDSSGIDMIDSSPGVCGREREELFFRAICLCHTVQVKDDHCGDDVDGPQKSPDAKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNRENDIERFELLEVLTFDSVRRRMSVIVKSTTGEIYLFCKGADSSIFPRVIEGKVDQVRSRVERNAVEGLRTLCVAYKRLEPEQYEDACRLLQSAKVALQDREKKLAEAYEQIEKDLVLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETASATCYACKLFRRSTQLLELTTKKLEEQSLHDVLFDLSKTVLRCSGSMTRDSFSGLSTDMHDYGLIIDGAALSLIMKPREDGSSSGNYRELFLEICRNCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGIGVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISE | ||||||
Transmembrane | 885-905 | Helical | ||||
Sequence: LVQYFFYKNVCFIFPQFLYQF | ||||||
Topological domain | 906-917 | Extracellular | ||||
Sequence: FCGFSQQTLYDT | ||||||
Transmembrane | 918-937 | Helical | ||||
Sequence: AYLTLYNISFTSLPILLYSL | ||||||
Topological domain | 938-967 | Cytoplasmic | ||||
Sequence: MEQHVGIDVLKRDPTLYRDIAKNALLRWRV | ||||||
Transmembrane | 968-989 | Helical | ||||
Sequence: FIYWTFLGVFDALVFFFGAYFI | ||||||
Topological domain | 990-1003 | Extracellular | ||||
Sequence: FENTTVTINGQMFG | ||||||
Transmembrane | 1004-1026 | Helical | ||||
Sequence: NWTFGTLVFTVMVLTVTLKLALD | ||||||
Topological domain | 1027-1032 | Cytoplasmic | ||||
Sequence: THYWTW | ||||||
Transmembrane | 1033-1053 | Helical | ||||
Sequence: INHFVIWGSLLFYIAFSLLWG | ||||||
Topological domain | 1054-1071 | Extracellular | ||||
Sequence: GVIWPFLSYQRMYYVFIS | ||||||
Transmembrane | 1072-1096 | Helical | ||||
Sequence: MLSSGPAWLGIILLVTVGLLPDVLK | ||||||
Topological domain | 1097-1138 | Cytoplasmic | ||||
Sequence: KVLCRQLWPTATERTQNIQHQDSISEFTPLASLPSWGAQGSR |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Conditional knockout in afferent spiral ganglion neurons leads to age-progressive hearing dysfunction characterized by abnormal auditory brainstem responses and normal otoacoustic emissions. Outer and middle ear function is normal.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 84 | Mutant mice surviving beyond the perinatal period show a reduction in brain size, dilated lateral ventricles and neurologic deficits. Increased sphingomyelin levels in various regions of mutant embryos. | ||||
Sequence: Q → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 70 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000046370 | 1-1187 | Phospholipid-transporting ATPase IH | |||
Sequence: MDCSLLRTLVRRYCAGEENWVDSRTIYVGHKEPPPGAEAYIPQRYPDNRIVSSKYTFWNFIPKNLFEQFRRIANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHKADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRADGTCHVTTASLDGESSHKTHYAVQDTKGFHTEADVDSLHATIECEQPQPDLYKFVGRINVYNDLNDPVVRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNTFLIVYLCILVSKALINTVLKYVWQSEPFRDEPWYNEKTESERQRNLFLRAFTDFLAFMVLFNYIIPVSMYVTVEMQKFLGSYFITWDEDMFDEEMGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMAFKECCIEGHVYVPHVICNGQVLPDSSGIDMIDSSPGVCGREREELFFRAICLCHTVQVKDDHCGDDVDGPQKSPDAKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNRENDIERFELLEVLTFDSVRRRMSVIVKSTTGEIYLFCKGADSSIFPRVIEGKVDQVRSRVERNAVEGLRTLCVAYKRLEPEQYEDACRLLQSAKVALQDREKKLAEAYEQIEKDLVLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETASATCYACKLFRRSTQLLELTTKKLEEQSLHDVLFDLSKTVLRCSGSMTRDSFSGLSTDMHDYGLIIDGAALSLIMKPREDGSSSGNYRELFLEICRNCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGIGVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDIAKNALLRWRVFIYWTFLGVFDALVFFFGAYFIFENTTVTINGQMFGNWTFGTLVFTVMVLTVTLKLALDTHYWTWINHFVIWGSLLFYIAFSLLWGGVIWPFLSYQRMYYVFISMLSSGPAWLGIILLVTVGLLPDVLKKVLCRQLWPTATERTQNIQHQDSISEFTPLASLPSWGAQGSRLLAAQCSSPSGRVVCSRWESEECPVLPLHPGLPHKARYGCCRSSLEMPT | ||||||
Modified residue | 740 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1148 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1158 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Proteolytically cleaved by CASP3.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length1,187
- Mass (Da)135,502
- Last updated2000-05-30 v1
- Checksum999A8BE19E9296C1
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF156551 EMBL· GenBank· DDBJ | AAF09449.1 EMBL· GenBank· DDBJ | mRNA | ||
BC138715 EMBL· GenBank· DDBJ | AAI38716.1 EMBL· GenBank· DDBJ | mRNA |