ATP8A1
entrez
10396
canonical
uniprot
Q9Y2Q0
canonical
ensembl
ENSG00000124406
resolver
ensp
ENSP00000264449
resolver
ensp
ENSP00000371084
resolver
ensp
ENSP00000515003
resolver
ensp
ENSP00000575811
resolver
ensp
ENSP00000575812
resolver
genesymbol
ATP8A1
resolver
genesymbol_syn
ATPIA
resolver
hgnc
HGNC:13531
resolver
uniprot
Q32M35
resolver
uniprot
Q32M36
resolver
uniprot
Q4W5J7
resolver
uniprot
Q4W5P2
resolver
uniprot_entry
AT8A1_HUMAN
resolver
uniprot_sec
Q32M35
resolver
uniprot_sec
Q32M36
resolver
uniprot_sec
Q4W5J7
resolver
uniprot_sec
Q4W5P2
resolver
activity_regulation
ACTIVITY REGULATION: ATPase activity is stimulated by phosphatidylserine (PS) and minimally by phosphatidylethanolamine (PE). ATPase activity is inhibited by beryllium fluoride and aluminum trifluoride (PubMed:31416931). {ECO:0000250, ECO:0000269|PubMed:31416931}.
uniprot
proteins
amino_acid_sequence
MPTMRRTVSEIRSRAEGYEKTDDVSEKTSLADQEEVRTIFINQPQLTKFCNNHVSTAKYNIITFLPRFLYSQFRRAANSFFLFIALLQQIPDVSPTGRYTTLVPLLFILAVAAIKEIIEDIKRHKADNAVNKKQTQVLRNGAWEIVHWEKVAVGEIVKVTNGEHLPADLISLSSSEPQAMCYIETSNLDGETNLKIRQGLPATSDIKDVDSLMRISGRIECESPNRHLYDFVGNIRLDGHGTVPLGADQILLRGAQLRNTQWVHGIVVYTGHDTKLMQNSTSPPLKLSNVERITNVQILILFCILIAMSLVCSVGSAIWNRRHSGKDWYLNLNYGGASNFGLNFLTFIILFNNLIPISLLVTLEVVKFTQAYFINWDLDMHYEPTDTAAMARTSNLNEELGQVKYIFSDKTGTLTCNVMQFKKCTIAGVAYGHVPEPEDYGCSPDEWQNSQFGDEKTFSDSSLLENLQNNHPTAPIICEFLTMMAVCHTAVPEREGDKIIYQAASPDEGALVRAAKQLNFVFTGRTPDSVIIDSLGQEERYELLNVLEFTSARKRMSVIVRTPSGKLRLYCKGADTVIYDRLAETSKYKEITLKHLEQFATEGLRTLCFAVAEISESDFQEWRAVYQRASTSVQNRLLKLEESYELIEKNLQLLGATAIEDKLQDQVPETIETLMKADIKIWILTGDKQETAINIGHSCKLLKKNMGMIVINEGSLDGTRETLSRHCTTLGDALRKENDFALIIDGKTLKYALTFGVRQYFLDLALSCKAVICCRVSPLQKSEVVEMVKKQVKVVTLAIGDGANDVSMIQTAHVGVGISGNEGLQAANSSDYSIAQFKYLKNLLMIHGAWNYNRVSKCILYCFYKNIVLYIIEIWFAFVNGFSGQILFERWCIGLYNVMFTAMPPLTLGIFERSCRKENMLKYPELYKTSQNALDFNTKVFWVHCLNGLFHSVILFWFPLKALQYGTAFGNGKTSDYLLLGNFVYTFVVITVCLKAGLETSYWTWFSHIAIWGSIALWVVFFGIYSSLWPAIPMAPDMSGEAAMLFSSGVFWMGLLFIPVASLLLDVVYKVIKRTAFKTLVDEVQELEAKSQDPGAVVLGKSLTERAQLLKNVFKKNHVNLYRSESLQQNLLHGYAFSQDENGIVSQSEVIRAYDTTKQRPDEW
uniprot
proteins
ec_number
7.6.2.1
uniprot
proteins
function
FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids (PubMed:31416931). Phospholipid translocation also seems to be implicated in vesicle formation and in uptake of lipid signaling molecules. In vitro, its ATPase activity is selectively and stereospecifically stimulated by phosphatidylserine (PS) (PubMed:31416931). The flippase complex ATP8A1:CDC50A seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the cell membrane (By similarity). Acts as aminophospholipid translocase at the cell membrane in neuronal cells (By similarity). {ECO:0000250|UniProtKB:P70704, ECO:0000269|PubMed:31416931}.
uniprot
proteins
mass_dalton
131369
uniprot
proteins
post_translational_modification
PTM: Cleaved by calpain in a caspase- and calcium influx-dependent manner during platelet apoptosis leading to a 100 kDa polypeptide. {ECO:0000269|PubMed:30674456}.
uniprot
proteins
protein_family
Cation transport ATPase (P-type) (TC 3.A.3) family
uniprot
proteins
protein_family
Type IV subfamily
uniprot
proteins
pubmed
10198212
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20947505
uniprot
proteins
pubmed
20961850
uniprot
proteins
pubmed
21914794
uniprot
proteins
pubmed
30674456
uniprot
proteins
pubmed
31416931
uniprot
proteins
sequence_length
1164
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000250|UniProtKB:P70704}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P70704}. Cytoplasmic granule {ECO:0000269|PubMed:20947505}. Cell membrane {ECO:0000269|PubMed:20947505, ECO:0000269|PubMed:21914794}. Endoplasmic reticulum {ECO:0000269|PubMed:20947505, ECO:0000269|PubMed:21914794}. Golgi apparatus {ECO:0000269|PubMed:20947505, ECO:0000269|PubMed:21914794}. Note=Exit from the endoplasmic reticulum requires the presence of CDC50A, but not CDC50B (PubMed:20947505). In the presence of CDC50A, predominantly located in cytoplasmic punctate structures and localizes to the cell membrane (PubMed:20947505). Localizes to plasma membranes of red blood cells (By similarity). {ECO:0000250|UniProtKB:P70704, ECO:0000269|PubMed:20947505}.
uniprot
proteins
transmembrane_region
TRANSMEM 66..86; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 93..115; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 298..319; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 345..366; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 858..878; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 891..910; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 941..962; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 977..999; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1006..1026; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1045..1070; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins