ATP11C
entrez
286410
canonical
uniprot
Q8NB49
canonical
ensembl
ENSG00000101974
resolver
ensp
ENSP00000332756
resolver
ensp
ENSP00000355165
resolver
ensp
ENSP00000394573
resolver
ensp
ENSP00000507250
resolver
ensp
ENSP00000718772
resolver
enst
ENST00000422228
resolver
enst
ENST00000682941
resolver
genesymbol
ATP11C
resolver
genesymbol_syn
ATPIG
resolver
genesymbol_syn
ATPIQ
resolver
hgnc
HGNC:13554
resolver
uniprot
A0A804HIW2
resolver
uniprot
H7C0E8
resolver
uniprot
Q5JT69
resolver
uniprot
Q5JT70
resolver
uniprot
Q5JT71
resolver
uniprot
Q5JT72
resolver
uniprot
Q5JT73
resolver
uniprot
Q6ZND5
resolver
uniprot
Q6ZU50
resolver
uniprot
Q6ZUP7
resolver
uniprot
Q70IJ9
resolver
uniprot
Q70IK0
resolver
uniprot
Q8WX24
resolver
uniprot_entry
A0A804HIW2_HUMAN
resolver
uniprot_entry
AT11C_HUMAN
resolver
uniprot_entry
H7C0E8_HUMAN
resolver
uniprot_sec
Q5JT69
resolver
uniprot_sec
Q5JT70
resolver
uniprot_sec
Q5JT71
resolver
uniprot_sec
Q5JT72
resolver
uniprot_sec
Q5JT73
resolver
uniprot_sec
Q6ZND5
resolver
uniprot_sec
Q6ZU50
resolver
uniprot_sec
Q6ZUP7
resolver
uniprot_sec
Q70IJ9
resolver
uniprot_sec
Q70IK0
resolver
uniprot_sec
Q8WX24
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:24904167, ECO:0000269|PubMed:26567335}.
uniprot
proteins
amino_acid_sequence
MQMVPSLPPASECAGEEKRVGTRTVFVGNHPVSETEAYIAQRFCDNRIVSSKYTLWNFLPKNLFEQFRRIANFYFLIIFLVQVTVDTPTSPVTSGLPLFFVITVTAIKQGYEDCLRHRADNEVNKSTVYIIENAKRVRKESEKIKVGDVVEVQADETFPCDLILLSSCTTDGTCYVTTASLDGESNCKTHYAVRDTIALCTAESIDTLRAAIECEQPQPDLYKFVGRINIYSNSLEAVARSLGPENLLLKGATLKNTEKIYGVAVYTGMETKMALNYQGKSQKRSAVEKSINAFLIVYLFILLTKAAVCTTLKYVWQSTPYNDEPWYNQKTQKERETLKVLKMFTDFLSFMVLFNFIIPVSMYVTVEMQKFLGSFFISWDKDFYDEEINEGALVNTSDLNEELGQVDYVFTDKTGTLTENSMEFIECCIDGHKYKGVTQEVDGLSQTDGTLTYFDKVDKNREELFLRALCLCHTVEIKTNDAVDGATESAELTYISSSPDEIALVKGAKRYGFTFLGNRNGYMRVENQRKEIEEYELLHTLNFDAVRRRMSVIVKTQEGDILLFCKGADSAVFPRVQNHEIELTKVHVERNAMDGYRTLCVAFKEIAPDDYERINRQLIEAKMALQDREEKMEKVFDDIETNMNLIGATAVEDKLQDQAAETIEALHAAGLKVWVLTGDKMETAKSTCYACRLFQTNTELLELTTKTIEESERKEDRLHELLIEYRKKLLHEFPKSTRSFKKAWTEHQEYGLIIDGSTLSLILNSSQDSSSNNYKSIFLQICMKCTAVLCCRMAPLQKAQIVRMVKNLKGSPITLSIGDGANDVSMILESHVGIGIKGKEGRQAARNSDYSVPKFKHLKKLLLAHGHLYYVRIAHLVQYFFYKNLCFILPQFLYQFFCGFSQQPLYDAAYLTMYNICFTSLPILAYSLLEQHINIDTLTSDPRLYMKISGNAMLQLGPFLYWTFLAAFEGTVFFFGTYFLFQTASLEENGKVYGNWTFGTIVFTVLVFTVTLKLALDTRFWTWINHFVIWGSLAFYVFFSFFWGGIIWPFLKQQRMYFVFAQMLSSVSTWLAIILLIFISLFPEILLIVLKNVRRRSARRNLSCRRASDSLSARPSVRPLLLRTFSDESNVL
uniprot
proteins
disease_involvement
DISEASE: Hemolytic anemia, congenital, X-linked (HACXL) [MIM:301015]: An X-linked hematologic disease characterized by shortened survival of erythrocytes due to congenital hemolysis that cannot be compensated by bone marrow activity. Clinical features are mild jaundice and anemia. Red cells morphology is normal. {ECO:0000269|PubMed:26944472}. Note=The disease is 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:24904167, PubMed:25315773, PubMed:26567335, PubMed:32493773). Major PS-flippase in immune cell subsets. In erythrocyte plasma membrane, it is required to maintain PS in the inner leaflet preventing its exposure on the surface. This asymmetric distribution is critical for the survival of erythrocytes in circulation since externalized PS is a phagocytic signal for erythrocyte clearance by splenic macrophages (PubMed:26944472). Required for B cell differentiation past the pro-B cell stage (By similarity). Seems to mediate PS flipping in pro-B cells (By similarity). May be involved in the transport of cholestatic bile acids (By similarity). {ECO:0000250|UniProtKB:Q9QZW0, ECO:0000269|PubMed:24904167, ECO:0000269|PubMed:25315773, ECO:0000269|PubMed:26944472, ECO:0000269|PubMed:32493773}.
uniprot
proteins
mass_dalton
129477
uniprot
proteins
mutagenesis
MUTAGEN 66; /note="Q->A: Decreases ATPase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 69; /note="R->A: Decreases ATPase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 72; /note="N->A: Decreases ATPase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 75; /note="F->A: Impairs ATPase flippase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 93; /note="T->A: Decreases ATPase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 101; /note="V->A: Impairs ATPase flippase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 184; /note="E->Q: Has no effect on endoplasmic reticulum to plasma membrane trafficking. Impairs ATPase flippase activity."; /evidence="ECO:0000269|PubMed:25315773"; MUTAGEN 352; /note="V->F: Impairs ATPase flippase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 353; /note="L->F: Decreases ATPase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 355; /note="N->A: Impairs ATPase flippase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 356; /note="F->N: Has no effect on ATPase flippase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 360; /note="V->F: Decreases ATPase flippase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 360; /note="V->I: Has minor effect on ATPase flippase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 412; /note="D->N: Impairs endoplasmic reticulum to plasma membrane trafficking."; /evidence="ECO:0000269|PubMed:25315773"; MUTAGEN 442; /note="D->A: Impairs caspase-mediated cleavage; when associated with A-448 and A-484."; /evidence="ECO:0000269|PubMed:24904167"; MUTAGEN 448; /note="D->A: Impairs caspase-mediated cleavage; when associated with A-442 and A-484."; /evidence="ECO:0000269|PubMed:24904167"; MUTAGEN 484; /note="D->A: Impairs caspase-mediated cleavage; when associated with A-442 and A-448."; /evidence="ECO:0000269|PubMed:24904167"; MUTAGEN 883; /note="K->A: Decreases ATPase flippase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 884; /note="N->A: Decreases ATPase flippase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 915; /note="N->A: Decreases ATPase flippase activity."; /evidence="ECO:0000269|PubMed:32493773"; MUTAGEN 1116; /note="S->A: Impairs sorting to endosomal compartments in response to ca(2+) signaling."; /evidence="ECO:0000269|PubMed:29123098"; MUTAGEN 1116; /note="S->D: Localizes to endosomal compartments in the absence of ca(2+) signaling."; /evidence="ECO:0000269|PubMed:29123098"; MUTAGEN 1120; /note="L->A: Impairs sorting to endosomal compartments in response to ca(2+) signaling."; /evidence="ECO:0000269|PubMed:29123098"; MUTAGEN 1121; /note="L->A: Impairs sorting to endosomal compartments in response to ca(2+) signaling."; /evidence="ECO:0000269|PubMed:29123098"; MUTAGEN 1122; /note="L->A: Has no effect on sorting to endosomal compartments in response to ca(2+) signaling."; /evidence="ECO:0000269|PubMed:29123098"; MUTAGEN 1126; /note="S->A: Decreases sorting to endosomal compartments in response to ca(2+) signaling."; /evidence="ECO:0000269|PubMed:29123098
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved by CASP3, CASP6 and CASP7. {ECO:0000269|PubMed:24904167}.; PTM: Phosphorylated at Ser-1116 likely by PRKCA; this creates a functional di-leucine motif that is sufficient for endocytosis. {ECO:0000269|PubMed:29123098}.
uniprot
proteins
protein_family
Cation transport ATPase (P-type) (TC 3.A.3) family
uniprot
proteins
protein_family
Type IV subfamily
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15533723
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21914794
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24904167
uniprot
proteins
pubmed
25315773
uniprot
proteins
pubmed
26567335
uniprot
proteins
pubmed
26944472
uniprot
proteins
pubmed
29123098
uniprot
proteins
pubmed
32493773
uniprot
proteins
sequence_length
1132
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25315773}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25315773}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:29123098}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:29123098}; Multi-pass membrane protein {ECO:0000255}. Note=Efficient exit from the endoplasmic reticulum requires the presence of CDC50A. Internalized via clathrin-dependent endocytosis in response to ca(2+) signaling induced by G protein coupled serotonin and histamine receptors. {ECO:0000269|PubMed:29123098}.
uniprot
proteins
transmembrane_region
TRANSMEM 67..85; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 87..107; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 291..311; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 347..367; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 880..900; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 909..929; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 956..976; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 996..1016; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1027..1047; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1070..1090; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins