Atp8a1
entrez
11980
canonical
uniprot
P70704
canonical
ensembl
ENSMUSG00000037685
resolver
ensp
ENSMUSP00000042215
resolver
ensp
ENSMUSP00000072738
resolver
ensp
ENSMUSP00000109282
resolver
ensp
ENSMUSP00000118379
resolver
ensp
ENSMUSP00000199462
resolver
ensp
ENSMUSP00000199483
resolver
enst
ENSMUST00000072971
resolver
enst
ENSMUST00000113652
resolver
genesymbol
Atp8a1
resolver
genesymbol_syn
Atpc1
resolver
uniprot
A0A0M3HEP7
resolver
uniprot
F6W375
resolver
uniprot
Q3U9N5
resolver
uniprot
Q52KQ7
resolver
uniprot
Q8BR88
resolver
uniprot
Q8CA15
resolver
uniprot_entry
A0A0M3HEP7_MOUSE
resolver
uniprot_entry
AT8A1_MOUSE
resolver
uniprot_entry
F6W375_MOUSE
resolver
uniprot_entry
Q3U9N5_MOUSE
resolver
uniprot_entry
Q52KQ7_MOUSE
resolver
uniprot_entry
Q8CA15_MOUSE
resolver
uniprot_sec
Q8BR88
resolver
activity_regulation
ACTIVITY REGULATION: ATPase activity is stimulated by phosphatidylserine (PS) and minimally by phosphatidylethanolamine (PE) (PubMed:16618126, PubMed:20224745). ATPase activity is inhibited by the vanadate and by the presence of calcium (PubMed:20224745). {ECO:0000269|PubMed:16618126, ECO:0000269|PubMed:20224745}.
uniprot
proteins
amino_acid_sequence
MPTMRRTVSEIRSRAEGYEKTDDVSEKTSLADQEEVRTIFINQPQLTKFCNNHVSTAKYNVITFLPRFLYSQFRRAANSFFLFIALLQQIPDVSPTGRYTTLVPLLFILAVAAIKEIIEDIKRHKADNAVNKKQTQVLRNGAWEIVHWEKVAVGEIVKVTNGEHLPADLLSLSSSEPQAMCYIETSNLDGETNLKIRQGLPATSDIKDIDSLMRISGRIECESPNRHLYDFVGNIRLDGHGTVPLGADQILLRGAQLRNTQWVHGIVVYTGHDTKLMQNSTSPPLKLSNVERITNVQILILFCILIAMSLVCSVGSAIWNRRHSGKDWYLHLHYGGASNFGLNFLTFIILFNNLIPISLLVTLEVVKFTQAYFINWDLDMHYEPTDTAAMARTSNLNEELGQVKYIFSDKTGTLTCNVMQFKKCTIAGVAYGHVPEPEDYGCSPDEWQSSQFGDEKTFNDPSLLDNLQNNHPTAPIICEFLTMMAVCHTAVPEREGDKIIYQAASPDEGALVRAAKQLNFVFTGRTPDSVIIDSLGQEERYELLNVLEFTSARKRMSVVVRTPSGKLRLYCKGADTVIYERLAETSKYKEITLKHLEQFATEGLRTLCFAVAEISESDFEEWRAVYHRASTSVQNRLLKLEESYELIEKNLQLLGATAIEDKLQDQVPETIETLMKADIKIWILTGDKQETAINIGHSCRLLKRNMGMIVINEGSLDGTRETLSRHCTTLGDALRKENDFALIIDGKTLKYALTFGVRQYFLDLALSCKAVICCRVSPLQKSEVVEMVKKQVKVITLAIGDGANDVSMIQTAHVGVGISGNEGLQAANSSDYSIAQFKYLKNLLMVHGAWNYNRVSKCILYCFYKNIVLYIIEIWFAFVNGFSGQILFERWCIGLYNVMFTAMPPLTLGIFERSCRKENMLKYPELYKTSQNALDFNTKVFWVHCLNGLFHSVILFWFPLKALQYGTVFGNGKTSDYLLLGNFVYTFVVITVCLKAGLETSYWTWFSHIAIWGSIALWVVFFGIYSSLWPAVPMAPDMSGEAAMLFSSGVFWVGLLSIPVASLLLDVLYKVIKRTAFKTLVDEVQELEAKSQDPGAVVLGKSLTERAQLLKNVFKKNHVNLYRSESLQQNLLHGYAFSQDENGIVSQSEVIRAYDTTKQRPDEW
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:16618126, PubMed:20224745). 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:16618126, PubMed:20224745). 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 (PubMed:23269685). Acts as aminophospholipid translocase at the cell membrane in neuronal cells; the activity is associated with hippocampus-dependent learning (PubMed:22007859). May play a role in brain connectivity (PubMed:27287255). {ECO:0000269|PubMed:16618126, ECO:0000269|PubMed:20224745, ECO:0000269|PubMed:22007859, ECO:0000269|PubMed:23269685, ECO:0000269|PubMed:27287255}.
uniprot
proteins
mass_dalton
131413
uniprot
proteins
mutagenesis
MUTAGEN 409; /note="D->K: Decreases plasma membrane aminophospholipid translocation in neuronal cells."; /evidence="ECO:0000269|PubMed:22007859
uniprot
proteins
post_translational_modification
PTM: Cleaved by calpain in a caspase- and calcium influx-dependent manner only during platelet apoptosis and may lead to inactivation. {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
16141072
uniprot
proteins
pubmed
16618126
uniprot
proteins
pubmed
16643453
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20224745
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22007859
uniprot
proteins
pubmed
23269685
uniprot
proteins
pubmed
27287255
uniprot
proteins
pubmed
30674456
uniprot
proteins
pubmed
9548971
uniprot
proteins
sequence_length
1164
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000269|PubMed:16643453}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic granule {ECO:0000269|PubMed:16643453}. Cell membrane {ECO:0000269|PubMed:27287255}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y2Q0}. Golgi apparatus {ECO:0000250|UniProtKB:Q9Y2Q0}. Cytoplasmic vesicle {ECO:0000269|PubMed:20224745, ECO:0000269|PubMed:27287255}. Endomembrane system {ECO:0000269|PubMed:30674456}. Note=Exit from the endoplasmic reticulum requires the presence of CDC50A, but not CDC50B. In the presence of CDC50A, predominantly located in cytoplasmic punctate structures (By similarity). Localizes to plasma membranes of red blood cells (PubMed:16643453). Localizes predominantly in the intracellular membranes, rather than the cell membrane of platelets (PubMed:30674456). {ECO:0000250, ECO:0000269|PubMed:16643453, ECO:0000269|PubMed:30674456}.
uniprot
proteins
transmembrane_region
TRANSMEM 76..96; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 101..121; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 298..318; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 340..360; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 867..887; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 891..911; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 940..960; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 978..998; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1009..1029; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1045..1065; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins