Abca1
entrez
11303
canonical
uniprot
P41233
canonical
ensembl
ENSMUSG00000015243
resolver
ensp
ENSMUSP00000030010
resolver
ensp
ENSMUSP00000330492
resolver
enst
ENSMUST00000030010
resolver
genesymbol
Abca1
resolver
genesymbol_syn
Abc1
resolver
uniprot
B1AWZ8
resolver
uniprot
Q8BPY1
resolver
uniprot_entry
ABCA1_MOUSE
resolver
uniprot_entry
Q8BPY1_MOUSE
resolver
uniprot_sec
B1AWZ8
resolver
activity_regulation
ACTIVITY REGULATION: ATPase activity is decreased by cholesterol and ceramide. ATPase activity is stimulated by phosphatidylcholine and to a lesser degree by phosphatidylserine and sphingomyelin. Phospholipid translocase activity is highly reduced by berylium fluoride and aluminum flouride and reduced by N-ethylmaleimide. {ECO:0000250|UniProtKB:O95477}.
uniprot
proteins
amino_acid_sequence
MACWPQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVSRLFSDAQRLLLYSQRDTSIKDMHKVLRMLRQIKHPNSNLKLQDFLVDNETFSGFLQHNLSLPRSTVDSLLQANVGLQKVFLQGYQLHLASLCNGSKLEEIIQLGDAEVSALCGLPRKKLDAAERVLRYNMDILKPVVTKLNSTSHLPTQHLAEATTVLLDSLGGLAQELFSTKSWSDMRQEVMFLTNVNSSSSSTQIYQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNNTEEDVDTFYDNSTTPYCNDLMKNLESSPLSRIIWKALKPLLVGKILYTPDTPATRQVMAEVNKTFQELAVFHDLEGMWEELSPQIWTFMENSQEMDLVRTLLDSRGNDQFWEQKLDGLDWTAQDIMAFLAKNPEDVQSPNGSVYTWREAFNETNQAIQTISRFMECVNLNKLEPIPTEVRLINKSMELLDERKFWAGIVFTGITPDSVELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVVEQAIIRVLTGSEKKTGVYVQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKSIVYEKEARLKETMRIMGLDNGILWFSWFVSSLIPLLVSAGLLVVILKLGNLLPYSDPSVVFVFLSVFAMVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQDYVGFSIKIFASLLSPVAFGFGCEYFALFEEQGIGVQWDNLFESPVEEDGFNLTTAVSMMLFDTFLYGVMTWYIEAVFPGQYGIPRPWYFPCTKSYWFGEEIDEKSHPGSSQKGVSEICMEEEPTHLRLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSSIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLSSCRNSSSTVSCLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVSEARLVEDIGHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAETSDGTLPARRNRRAFGDKQSCLHPFTEDDAVDPNDSDIDPESRETDLLSGMDGKGSYQLKGWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLELQPWMYNEQYTFVSNDAPEDMGTQELLNALTKDPGFGTRCMEGNPIPDTPCLAGEEDWTISPVPQSIVDLFQNGNWTMKNPSPACQCSSDKIKKMLPVCPPGAGGLPPPQRKQKTADILQNLTGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGVSNSQALPPSHEVNDAIKQMKKLLKLTKDSSADRFLSSLGRFMAGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSQYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTNNKLNDINDILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEGVVFFLITVLIQYRFFIRPRPVKAKLPPLNDEDEDVRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRICIGIPPGECFGLLGVNGAGKSTTFKMLTGDTPVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYASNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKPVQEFFGLAFPGSVLKEKHRNMLQYQLPSSLSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNFAKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV
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. Thereby, participates in phospholipid transfer to apolipoproteins to form nascent high density lipoproteins/HDLs. Transports preferentially phosphatidylcholine over phosphatidylserine. May play a similar role in the efflux of intracellular cholesterol to apolipoproteins and the formation of nascent high density lipoproteins/HDLs. Translocates phospholipids from the outer face of the plasma membrane and forces it through its gateway and annulus into an elongated hydrophobic tunnel in its extracellular domain. {ECO:0000250|UniProtKB:O95477}.
uniprot
proteins
mass_dalton
253912
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Ser-2054 regulates phospholipid efflux. {ECO:0000250|UniProtKB:O95477}.; PTM: Palmitoylated by ZDHHC8. Palmitoylation is essential for localization to the plasma membrane. {ECO:0000250|UniProtKB:O95477}.
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCA family
uniprot
proteins
pubmed
11352567
uniprot
proteins
pubmed
12032171
uniprot
proteins
pubmed
12777468
uniprot
proteins
pubmed
17205124
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8088782
uniprot
proteins
sequence_length
2261
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95477}; Multi-pass membrane protein {ECO:0000255}. Endosome {ECO:0000250|UniProtKB:O95477}.
uniprot
proteins
transmembrane_region
TRANSMEM 22..42; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 640..660; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 683..703; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 716..736; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 745..765; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 777..797; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 827..847; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 941..961; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1351..1371; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1657..1677; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1703..1723; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1735..1755; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1768..1788; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1802..1822; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1852..1872; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins