ATP11A
entrez
23250
canonical
uniprot
P98196
canonical
ensembl
ENSG00000068650
resolver
ensp
ENSP00000364781
resolver
ensp
ENSP00000364796
resolver
ensp
ENSP00000420387
resolver
ensp
ENSP00000575273
resolver
ensp
ENSP00000687503
resolver
ensp
ENSP00000798240
resolver
enst
ENST00000375630
resolver
enst
ENST00000375645
resolver
enst
ENST00000487903
resolver
enst
ENST00000905214
resolver
genesymbol
ATP11A
resolver
genesymbol_syn
ATPIH
resolver
genesymbol_syn
ATPIS
resolver
genesymbol_syn
KIAA1021
resolver
hgnc
HGNC:13552
resolver
uniprot
E9PEJ6
resolver
uniprot
Q5VXT2
resolver
uniprot
Q6PJ25
resolver
uniprot_entry
AT11A_HUMAN
resolver
uniprot_entry
E9PEJ6_HUMAN
resolver
uniprot_entry
Q6PJ25_HUMAN
resolver
uniprot_sec
Q5VXT2
resolver
activity_regulation
ACTIVITY REGULATION: The flippase activity is inactivated by caspase-mediated cleavage in apoptotic cells, allowing for PS exposure on the cell surface and engulfment of apoptotic cells by macrophages. The ATPase activity is up-regulated by aminophospholipids PS and PE and down-regulated by increasing intracellular Ca2+ levels. {ECO:0000269|PubMed:26567335, ECO:0000269|PubMed:30018401}.
uniprot
proteins
amino_acid_sequence
MDCSLVRTLVHRYCAGEENWVDSRTIYVGHREPPPGAEAYIPQRYPDNRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHKADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTTASLDGESSHKTHYAVQDTKGFHTEEDIGGLHATIECEQPQPDLYKFVGRINVYSDLNDPVVRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNAFLIVYLCILISKALINTVLKYMWQSEPFRDEPWYNQKTESERQRNLFLKAFTDFLAFMVLFNYIIPVSMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMEFKECCIEGHVYVPHVICNGQVLPESSGIDMIDSSPSVNGREREELFFRALCLCHTVQVKDDDSVDGPRKSPDGGKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNRENHIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGKVDQIRARVERNAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTKRIEEQSLHDVLFELSKTVLRHSGSLTRDNLSGLSADMQDYGLIIDGAALSLIMKPREDGSSGNYRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGIGVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALLRWRVFIYWTLLGLFDALVFFFGAYFVFENTTVTSNGQIFGNWTFGTLVFTVMVFTVTLKLALDTHYWTWINHFVIWGSLLFYVVFSLLWGGVIWPFLNYQRMYYVFIQMLSSGPAWLAIVLLVTISLLPDVLKKVLCRQLWPTATERVQTKSQCLSVEQSTIFMLSQTSSSLSF
uniprot
proteins
disease_involvement
DISEASE: Deafness, autosomal dominant, 84 (DFNA84) [MIM:619810]: A form of non-syndromic, sensorineural hearing loss. Sensorineural hearing loss results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA84 is characterized by slowly progressive, postlingual hearing loss. {ECO:0000269|PubMed:35278131}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Leukodystrophy, hypomyelinating, 24 (HLD24) [MIM:619851]: An autosomal dominant disorder characterized by global developmental delay apparent in infancy, impaired intellectual development, and loss of developmental milestones and ambulation. Brain imaging shows non-progressive severe cerebral atrophy, ventriculomegaly, hypomyelinating leukodystrophy, and thinning of the corpus callosum. {ECO:0000269|PubMed:34403372}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Auditory neuropathy, autosomal dominant 2 (AUNA2) [MIM:620384]: A form of sensorineural hearing loss with absent or severely abnormal auditory brainstem response, in the presence of normal cochlear outer hair cell function and normal otoacoustic emissions. Auditory neuropathies result from a lesion in the area including the inner hair cells, connections between the inner hair cells and the cochlear branch of the auditory nerve, the auditory nerve itself and auditory pathways of the brainstem. Affected individuals typically respond to sound but have difficulties in speech discrimination. AUNA2 is characterized by postlingual onset of progressive bilateral sensorineural hearing loss in the second decade, leading to profound deafness in the fifth decade. The outer hair cell function is preserved initially but declines with age. {ECO:0000269|PubMed:36300302}. Note=The disease may be caused by variants affecting the gene represented in this entry.
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, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of the plasma membrane (PubMed:25315773, PubMed:25947375, PubMed:26567335, PubMed:29799007, PubMed:30018401, PubMed:36300302). Does not show flippase activity toward phosphatidylcholine (PC) (PubMed:34403372). 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). May be involved in the uptake of farnesyltransferase inhibitor drugs, such as lonafarnib. {ECO:0000269|PubMed:15860663, ECO:0000269|PubMed:25315773, ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:26567335, ECO:0000269|PubMed:29799007, ECO:0000269|PubMed:30018401, ECO:0000269|PubMed:34403372, ECO:0000269|PubMed:36300302, ECO:0000305}.
uniprot
proteins
mass_dalton
129756
uniprot
proteins
mutagenesis
MUTAGEN 84; /note="Q->A: Does not affect flippase activity toward phosphatidylserine. Like the wild type, it is unable to translocate phosphatidylcholine."; /evidence="ECO:0000269|PubMed:34403372"; MUTAGEN 84; /note="Q->D: Does not affect flippase activity toward phosphatidylserine. Like the wild type, it is unable to translocate phosphatidylcholine."; /evidence="ECO:0000269|PubMed:34403372"; MUTAGEN 84; /note="Q->N: Does not affect flippase activity toward phosphatidylserine. Like the wild type, it is unable to translocate phosphatidylcholine."; /evidence="ECO:0000269|PubMed:34403372"; MUTAGEN 186; /note="E->Q: Has no effect on endoplasmic reticulum to plasma membrane trafficking. Impairs flippase activity toward phosphatidylserine and phosphatidylethanolamine."; /evidence="ECO:0000269|PubMed:25315773, ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:30018401, ECO:0000269|PubMed:36300302"; MUTAGEN 414; /note="D->N: Impairs endoplasmic reticulum to plasma membrane trafficking."; /evidence="ECO:0000269|PubMed:25315773"; MUTAGEN 454; /note="D->A: Impairs caspase-mediated cleavage; when associated with A-457, A-487 and A-490."; /evidence="ECO:0000269|PubMed:26567335"; MUTAGEN 457; /note="D->A: Impairs caspase-mediated cleavage; when associated with A-454, A-487 and A-490."; /evidence="ECO:0000269|PubMed:26567335"; MUTAGEN 487; /note="D->A: Impairs caspase-mediated cleavage; when associated with A-454, A-457 and A-490."; /evidence="ECO:0000269|PubMed:26567335"; MUTAGEN 490; /note="D->A: Impairs caspase-mediated cleavage; when associated with A-454, A-457 and A-487."; /evidence="ECO:0000269|PubMed:26567335
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved by CASP3. {ECO:0000269|PubMed:26567335}.
uniprot
proteins
protein_family
Cation transport ATPase (P-type) (TC 3.A.3) family
uniprot
proteins
protein_family
Type IV subfamily
uniprot
proteins
pubmed
10470851
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15860663
uniprot
proteins
pubmed
21914794
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25315773
uniprot
proteins
pubmed
25947375
uniprot
proteins
pubmed
26567335
uniprot
proteins
pubmed
29799007
uniprot
proteins
pubmed
30018401
uniprot
proteins
pubmed
34403372
uniprot
proteins
pubmed
35278131
uniprot
proteins
pubmed
36300302
uniprot
proteins
sequence_length
1134
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25315773, ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:34403372, ECO:0000269|PubMed:36300302}; Multi-pass membrane protein {ECO:0000255}. Early endosome {ECO:0000269|PubMed:21914794}. Recycling endosome {ECO:0000269|PubMed:21914794}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25315773, ECO:0000269|PubMed:25947375}; Multi-pass membrane protein {ECO:0000255}. Note=Efficient exit from the endoplasmic reticulum requires the presence of CDC50A. {ECO:0000269|PubMed:25315773, ECO:0000269|PubMed:25947375}.
uniprot
proteins
transmembrane_region
TRANSMEM 62..82; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 89..110; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 297..318; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 350..372; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 882..902; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 915..934; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 965..986; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1001..1023; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1030..1050; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1069..1093; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins