ABCA7
entrez
10347
canonical
uniprot
Q8IZY2
canonical
ensembl
ENSG00000064687
resolver
ensp
ENSP00000263094
resolver
genesymbol
ABCA7
resolver
hgnc
HGNC:37
resolver
uniprot
B3KUJ3
resolver
uniprot
Q96S58
resolver
uniprot
Q9BZC4
resolver
uniprot
Q9NR73
resolver
uniprot
Q9UKP8
resolver
uniprot_entry
ABCA7_HUMAN
resolver
uniprot_entry
B3KUJ3_HUMAN
resolver
uniprot_sec
Q96S58
resolver
uniprot_sec
Q9BZC4
resolver
uniprot_sec
Q9NR73
resolver
uniprot_sec
Q9UKP8
resolver
activity_regulation
ACTIVITY REGULATION: ATPase activity is decreased by cholesterol and ceramide. ATPase activity is stimulated by phosphatidylserine, phosphatidylcholine and sphingomyelin, but phosphatidylserine is more effective. {ECO:0000269|PubMed:24097981}.
uniprot
proteins
amino_acid_sequence
MAFWTQLMLLLWKNFMYRRRQPVQLLVELLWPLFLFFILVAVRHSHPPLEHHECHFPNKPLPSAGTVPWLQGLICNVNNTCFPQLTPGEEPGRLSNFNDSLVSRLLADARTVLGGASAHRTLAGLGKLIATLRAARSTAQPQPTKQSPLEPPMLDVAELLTSLLRTESLGLALGQAQEPLHSLLEAAEDLAQELLALRSLVELRALLQRPRGTSGPLELLSEALCSVRGPSSTVGPSLNWYEASDLMELVGQEPESALPDSSLSPACSELIGALDSHPLSRLLWRRLKPLILGKLLFAPDTPFTRKLMAQVNRTFEELTLLRDVREVWEMLGPRIFTFMNDSSNVAMLQRLLQMQDEGRRQPRPGGRDHMEALRSFLDPGSGGYSWQDAHADVGHLVGTLGRVTECLSLDKLEAAPSEAALVSRALQLLAEHRFWAGVVFLGPEDSSDPTEHPTPDLGPGHVRIKIRMDIDVVTRTNKIRDRFWDPGPAADPLTDLRYVWGGFVYLQDLVERAAVRVLSGANPRAGLYLQQMPYPCYVDDVFLRVLSRSLPLFLTLAWIYSVTLTVKAVVREKETRLRDTMRAMGLSRAVLWLGWFLSCLGPFLLSAALLVLVLKLGDILPYSHPGVVFLFLAAFAVATVTQSFLLSAFFSRANLAAACGGLAYFSLYLPYVLCVAWRDRLPAGGRVAASLLSPVAFGFGCESLALLEEQGEGAQWHNVGTRPTADVFSLAQVSGLLLLDAALYGLATWYLEAVCPGQYGIPEPWNFPFRRSYWCGPRPPKSPAPCPTPLDPKVLVEEAPPGLSPGVSVRSLEKRFPGSPQPALRGLSLDFYQGHITAFLGHNGAGKTTTLSILSGLFPPSGGSAFILGHDVRSSMAAIRPHLGVCPQYNVLFDMLTVDEHVWFYGRLKGLSAAVVGPEQDRLLQDVGLVSKQSVQTRHLSGGMQRKLSVAIAFVGGSQVVILDEPTAGVDPASRRGIWELLLKYREGRTLILSTHHLDEAELLGDRVAVVAGGRLCCCGSPLFLRRHLGSGYYLTLVKARLPLTTNEKADTDMEGSVDTRQEKKNGSQGSRVGTPQLLALVQHWVPGARLVEELPHELVLVLPYTGAHDGSFATLFRELDTRLAELRLTGYGISDTSLEEIFLKVVEECAADTDMEDGSCGQHLCTGIAGLDVTLRLKMPPQETALENGEPAGSAPETDQGSGPDAVGRVQGWALTRQQLQALLLKRFLLARRSRRGLFAQIVLPALFVGLALVFSLIVPPFGHYPALRLSPTMYGAQVSFFSEDAPGDPGRARLLEALLQEAGLEEPPVQHSSHRFSAPEVPAEVAKVLASGNWTPESPSPACQCSRPGARRLLPDCPAAAGGPPPPQAVTGSGEVVQNLTGRNLSDFLVKTYPRLVRQGLKTKKWVNEVRYGGFSLGGRDPGLPSGQELGRSVEELWALLSPLPGGALDRVLKNLTAWAHSLDAQDSLKIWFNNKGWHSMVAFVNRASNAILRAHLPPGPARHAHSITTLNHPLNLTKEQLSEGALMASSVDVLVSICVVFAMSFVPASFTLVLIEERVTRAKHLQLMGGLSPTLYWLGNFLWDMCNYLVPACIVVLIFLAFQQRAYVAPANLPALLLLLLLYGWSITPLMYPASFFFSVPSTAYVVLTCINLFIGINGSMATFVLELFSDQKLQEVSRILKQVFLIFPHFCLGRGLIDMVRNQAMADAFERLGDRQFQSPLRWEVVGKNLLAMVIQGPLFLLFTLLLQHRSQLLPQPRVRSLPLLGEEDEDVARERERVVQGATQGDVLVLRNLTKVYRGQRMPAVDRLCLGIPPGECFGLLGVNGAGKTSTFRMVTGDTLASRGEAVLAGHSVAREPSAAHLSMGYCPQSDAIFELLTGREHLELLARLRGVPEAQVAQTAGSGLARLGLSWYADRPAGTYSGGNKRKLATALALVGDPAVVFLDEPTTGMDPSARRFLWNSLLAVVREGRSVMLTSHSMEECEALCSRLAIMVNGRFRCLGSPQHLKGRFAAGHTLTLRVPAARSQPAAAFVAAEFPGAELREAHGGRLRFQLPPGGRCALARVFGELAVHGAEHGVEDFSVSQTMLEEVFLYFSKDQGKDEDTEEQKEAGVGVDPAPGLQHPKRVSQFLDDPSTAETVL
uniprot
proteins
disease_involvement
DISEASE: Alzheimer disease 9 (AD9) [MIM:608907]: A familial, late-onset form of Alzheimer disease. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituents of these plaques are neurotoxic amyloid-beta protein 40 and amyloid-beta protein 42, that are produced by the proteolysis of the transmembrane APP protein. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products, such as C31, are also implicated in neuronal death. {ECO:0000269|PubMed:25807283, ECO:0000269|PubMed:26141617, ECO:0000269|PubMed:29577078}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
7.6.2.1
uniprot
proteins
function
FUNCTION: Catalyzes the translocation of specific phospholipids from the cytoplasmic to the extracellular/lumenal leaflet of membrane coupled to the hydrolysis of ATP (PubMed:24097981). Transports preferentially phosphatidylserine over phosphatidylcholine (PubMed:24097981). Plays a role in lipid homeostasis and macrophage-mediated phagocytosis (PubMed:12917409, PubMed:12925201, PubMed:14570867, PubMed:14592415). Binds APOA1 and may function in apolipoprotein-mediated phospholipid efflux from cells (PubMed:12917409, PubMed:14570867, PubMed:14592415). May also mediate cholesterol efflux (PubMed:14570867). May regulate cellular ceramide homeostasis during keratinocyte differentiation (PubMed:12925201). Involved in lipid raft organization and CD1D localization on thymocytes and antigen-presenting cells, which plays an important role in natural killer T-cell development and activation (By similarity). Plays a role in phagocytosis of apoptotic cells by macrophages (By similarity). Macrophage phagocytosis is stimulated by APOA1 or APOA2, probably by stabilization of ABCA7 (By similarity). Also involved in phagocytic clearance of amyloid-beta by microglia cells and macrophages (By similarity). Further limits amyloid-beta production by playing a role in the regulation of amyloid-beta A4 precursor protein (APP) endocytosis and/or processing (PubMed:26260791). Amyloid-beta is the main component of amyloid plaques found in the brains of Alzheimer patients (PubMed:26260791). {ECO:0000250|UniProtKB:Q91V24, ECO:0000269|PubMed:12917409, ECO:0000269|PubMed:12925201, ECO:0000269|PubMed:14570867, ECO:0000269|PubMed:14592415, ECO:0000269|PubMed:24097981, ECO:0000269|PubMed:26260791}.
uniprot
proteins
mass_dalton
234350
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q91V24}.
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCA family
uniprot
proteins
pubmed
10873640
uniprot
proteins
pubmed
11095984
uniprot
proteins
pubmed
11355874
uniprot
proteins
pubmed
11435699
uniprot
proteins
pubmed
12111378
uniprot
proteins
pubmed
12917409
uniprot
proteins
pubmed
12925201
uniprot
proteins
pubmed
14570867
uniprot
proteins
pubmed
14592415
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
24097981
uniprot
proteins
pubmed
25807283
uniprot
proteins
pubmed
26141617
uniprot
proteins
pubmed
26260791
uniprot
proteins
pubmed
27472885
uniprot
proteins
pubmed
29577078
uniprot
proteins
sequence_length
2146
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12917409, ECO:0000269|PubMed:14592415}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q91V24}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q91V24}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q91V24}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q91V24}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q91V24}. Note=Localizes to cell membrane ruffles and phagocytic cups of macrophages stimulated with C1q or apoptotic cells. Localizes to the cytoplasm of resting macrophages, probably in Golgi and endosomes. Localizes to the apical brush border of cells in the proximal tubules of kidney (By similarity). {ECO:0000250|UniProtKB:Q91V24}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:14592415}. Endoplasmic reticulum {ECO:0000269|PubMed:14592415}. Note=May localize to the endoplasmic reticulum. {ECO:0000269|PubMed:14592415}.
uniprot
proteins
transmembrane_region
TRANSMEM 22..42; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 550..570; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 593..613; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 626..646; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 655..675; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 687..707; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 727..747; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 849..869; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1243..1263; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1538..1558; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1584..1604; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1621..1641; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1649..1669; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1683..1703; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1729..1749; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins