ABCA1
entrez
19
canonical
uniprot
O95477
canonical
ensembl
ENSG00000165029
resolver
ensp
ENSP00000363868
resolver
enst
ENST00000374736
resolver
genesymbol
ABCA1
resolver
genesymbol_syn
ABC1
resolver
genesymbol_syn
CERP
resolver
hgnc
HGNC:29
resolver
uniprot
B2RUU2
resolver
uniprot
B7XCW9
resolver
uniprot
Q5VX33
resolver
uniprot
Q96S56
resolver
uniprot
Q96T85
resolver
uniprot
Q9NQV4
resolver
uniprot
Q9UN06
resolver
uniprot
Q9UN07
resolver
uniprot
Q9UN08
resolver
uniprot
Q9UN09
resolver
uniprot_entry
ABCA1_HUMAN
resolver
uniprot_entry
B2RUU2_HUMAN
resolver
uniprot_entry
B7XCW9_HUMAN
resolver
uniprot_sec
Q5VX33
resolver
uniprot_sec
Q96S56
resolver
uniprot_sec
Q96T85
resolver
uniprot_sec
Q9NQV4
resolver
uniprot_sec
Q9UN06
resolver
uniprot_sec
Q9UN07
resolver
uniprot_sec
Q9UN08
resolver
uniprot_sec
Q9UN09
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:0000269|PubMed:24097981}.
uniprot
proteins
amino_acid_sequence
MACWPQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVARLFSDARRLLLYSQKDTSMKDMRKVLRTLQQIKKSSSNLKLQDFLVDNETFSGFLYHNLSLPKSTVDKMLRADVILHKVFLQGYQLHLTSLCNGSKSEEMIQLGDQEVSELCGLPREKLAAAERVLRSNMDILKPILRTLNSTSPFPSKELAEATKTLLHSLGTLAQELFSMRSWSDMRQEVMFLTNVNSSSSSTQIYQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDAETFYDNSTTPYCNDLMKNLESSPLSRIIWKALKPLLVGKILYTPDTPATRQVMAEVNKTFQELAVFHDLEGMWEELSPKIWTFMENSQEMDLVRMLLDSRDNDHFWEQQLDGLDWTAQDIVAFLAKHPEDVQSSNGSVYTWREAFNETNQAIRTISRFMECVNLNKLEPIATEVWLINKSMELLDERKFWAGIVFTGITPGSIELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVVEQAIIRVLTGTEKKTGVYMQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNSILWFSWFISSLIPLLVSAGLLVVILKLGNLLPYSDPSVVFVFLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQDYVGFTLKIFASLLSPVAFGFGCEYFALFEEQGIGVQWDNLFESPVEEDGFNLTTSVSMMLFDTFLYGVMTWYIEAVFPGQYGIPRPWYFPCTKSYWFGEESDEKSHPGSNQKRISEICMEEEPTHLKLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLSSCRNSSSTVSYLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVSEARLVEDIGHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAETSDGTLPARRNRRAFGDKQSCLRPFTEDDAADPNDSDIDPESRETDLLSGMDGKGSYQVKGWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLELQPWMYNEQYTFVSNDAPEDTGTLELLNALTKDPGFGTRCMEGNPIPDTPCQAGEEEWTTAPVPQTIMDLFQNGNWTMQNPSPACQCSSDKIKKMLPVCPPGAGGLPPPQRKQNTADILQDLTGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGVSNTQALPPSQEVNDAIKQMKKHLKLAKDSSADRFLNSLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSHYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTDNKLNNINDILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEGVVFFLITVLIQYRFFIRPRPVNAKLSPLNDEDEDVRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKPVQDFFGLAFPGSVLKEKHRNMLQYQLPSSLSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNFAKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV
uniprot
proteins
disease_involvement
DISEASE: Tangier disease (TGD) [MIM:205400]: An autosomal recessive disorder characterized by near absence of plasma high density lipoproteins, low serum HDL cholesterol, and massive tissue deposition of cholesterol esters. Clinical features include large yellow-orange tonsils, hepatomegaly, splenomegaly, enlarged lymph nodes, and often sensory polyneuropathy. {ECO:0000269|PubMed:10431236, ECO:0000269|PubMed:10431237, ECO:0000269|PubMed:10706591, ECO:0000269|PubMed:10938021, ECO:0000269|PubMed:11086027, ECO:0000269|PubMed:11257260, ECO:0000269|PubMed:11476961, ECO:0000269|PubMed:11476965, ECO:0000269|PubMed:11785958, ECO:0000269|PubMed:12111371, ECO:0000269|PubMed:12111381, ECO:0000269|PubMed:12407001, ECO:0000269|PubMed:14576201, ECO:0000269|PubMed:14754908, ECO:0000269|PubMed:15019541, ECO:0000269|PubMed:15158913, ECO:0000269|PubMed:15262183, ECO:0000269|PubMed:15297675, ECO:0000269|PubMed:15520867, ECO:0000269|PubMed:18776170, ECO:0000269|PubMed:24097981}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Hypoalphalipoproteinemia, primary, 1 (FHA1) [MIM:604091]: An autosomal dominant disorder characterized by decreased plasma high density lipoproteins, moderately low HDL cholesterol, a reduction in cellular cholesterol efflux, and susceptibility to premature coronary artery disease. {ECO:0000269|PubMed:10431236, ECO:0000269|PubMed:10533863, ECO:0000269|PubMed:11086027, ECO:0000269|PubMed:11785958, ECO:0000269|PubMed:12009425, ECO:0000269|PubMed:12204794, ECO:0000269|PubMed:15722566, ECO:0000269|PubMed:19556522, ECO:0000269|PubMed:24097981}. 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: Catalyzes the translocation of specific phospholipids from the cytoplasmic to the extracellular/lumenal leaflet of membrane coupled to the hydrolysis of ATP (PubMed:24097981, PubMed:35974019). Thereby, participates in phospholipid transfer to apolipoproteins to form nascent high density lipoproteins/HDLs (PubMed:14754908). Transports preferentially phosphatidylcholine over phosphatidylserine (PubMed:24097981). May play a similar role in the efflux of intracellular cholesterol to apolipoproteins and the formation of nascent high density lipoproteins/HDLs (PubMed:10533863, PubMed:14754908, PubMed:24097981, PubMed:35974019). 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 (PubMed:35974019). {ECO:0000269|PubMed:10533863, ECO:0000269|PubMed:14754908, ECO:0000269|PubMed:24097981, ECO:0000269|PubMed:35974019}.
uniprot
proteins
mass_dalton
254302
uniprot
proteins
mutagenesis
MUTAGEN 3; /note="C->S: Mild decrease of palmitoylation. Loss of localization to plasma membrane. Decreased cholesterol efflux. Decreased phospholipid efflux. Decreased palmitoylation; when associated with S-23, S-1110 and S-1111."; /evidence="ECO:0000269|PubMed:19556522"; MUTAGEN 23; /note="C->S: Mild decrease of palmitoylation. Loss of localization to plasma membrane. Decreased palmitoylation; when associated with S-3, S-1110 and S-1111."; /evidence="ECO:0000269|PubMed:19556522"; MUTAGEN 74; /note="I->C: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with C-371."; /evidence="ECO:0000269|PubMed:35974019"; MUTAGEN 74; /note="I->K: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with E-371."; /evidence="ECO:0000269|PubMed:35974019"; MUTAGEN 100; /note="S->C: Highly decreased protein abundance. Highly decreased ATPase activity. Highly decreased phospholipid translocase activity."; /evidence="ECO:0000269|PubMed:24097981"; MUTAGEN 304; /note="V->C: No effect on phospholipid and cholesterol efflux or localization to cell membrane; when associated with C-308."; /evidence="ECO:0000269|PubMed:35974019"; MUTAGEN 308; /note="V->C: No effect on phospholipid and cholesterol efflux or localization to cell membrane; when associated with C-304."; /evidence="ECO:0000269|PubMed:35974019"; MUTAGEN 371; /note="I->C: No effect on phospholipid and cholesterol efflux or localization to cell membrane. 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with C-74 or C-375."; /evidence="ECO:0000269|PubMed:35974019"; MUTAGEN 371; /note="I->E: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-74."; /evidence="ECO:0000269|PubMed:35974019"; MUTAGEN 375; /note="L->C: 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with C-371."; /evidence="ECO:0000269|PubMed:35974019"; MUTAGEN 568; /note="K->A: 60-65% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane."; /evidence="ECO:0000269|PubMed:35974019"; MUTAGEN 573; /note="Y->F: No effect on phospholipid and cholesterol efflux and on localization to cell membrane."; /evidence="ECO:0000269|PubMed:35974019"; MUTAGEN 581; /note="D->K: 80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-584 and K-585."; /evidence="ECO:0000269|PubMed:35974019"; MUTAGEN 583; /note="F->K: 90-95% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with E-590."; /evidence="ECO:0000269|PubMed:35974019"; MUTAGEN 584; /note="E->K: 80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-581 and K-585."; /evidence="ECO:0000269|PubMed:35974019"; MUTAGEN 585; /note="D->K: 80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-581 and K-584."; /evidence="ECO:0000269|PubMed:35974019"; MUTAGEN 590; /note="W->E: 90-95% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-583."; /evidence="ECO:0000269|PubMed:35974019"; MUTAGEN 593; /note="F->L: Moderately decreased protein abundance. Highly decreased ATPase activity. Highly decreased phospholipid translocase activity."; /evidence="ECO:0000269|PubMed:24097981"; MUTAGEN 939; /note="K->M: Inhibits ATPase activity; when associated with M-1952. Decreases translocase activity; when associated with M-1952. Does not affect protein subcellular localization in plasma membrane and endosome; when associated with M-1952."; /evidence="ECO:0000269|PubMed:24097981"; MUTAGEN 1110; /note="C->S: Decreased palmitoylation; when associated with S-3, S-23 and S-1111."; /evidence="ECO:0000269|PubMed:19556522"; MUTAGEN 1111; /note="C->S: Decreased palmitoylation; when associated with S-3, S-23 and S-1110."; /evidence="ECO:0000269|PubMed:19556522"; MUTAGEN 1512; /note="T->M: Moderately decreased protein abundance. Does not affect ATPase activity. Moderately decreased phospholipid translocase activity."; /evidence="ECO:0000269|PubMed:24097981"; MUTAGEN 1952; /note="K->M: Inhibits ATPase activity; when associated with M-939. Decreases translocase activity; when associated with M-939. Does not affect protein subcellular localization in plasma membrane and endosome; when associated with M-939."; /evidence="ECO:0000269|PubMed:24097981
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Ser-2054 regulates phospholipid efflux. {ECO:0000269|PubMed:12196520}.; PTM: Palmitoylated by ZDHHC8 (PubMed:19556522). Palmitoylation is essential for localization to the plasma membrane (PubMed:19556522). {ECO:0000269|PubMed:19556522}.
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCA family
uniprot
proteins
pubmed
10092505
uniprot
proteins
pubmed
10431236
uniprot
proteins
pubmed
10431237
uniprot
proteins
pubmed
10431238
uniprot
proteins
pubmed
10533863
uniprot
proteins
pubmed
10706591
uniprot
proteins
pubmed
10884428
uniprot
proteins
pubmed
10938021
uniprot
proteins
pubmed
11086027
uniprot
proteins
pubmed
11238261
uniprot
proteins
pubmed
11257260
uniprot
proteins
pubmed
11257261
uniprot
proteins
pubmed
11279031
uniprot
proteins
pubmed
11352567
uniprot
proteins
pubmed
11476961
uniprot
proteins
pubmed
11476965
uniprot
proteins
pubmed
11785958
uniprot
proteins
pubmed
12009425
uniprot
proteins
pubmed
12032171
uniprot
proteins
pubmed
12111371
uniprot
proteins
pubmed
12111381
uniprot
proteins
pubmed
12196520
uniprot
proteins
pubmed
12204794
uniprot
proteins
pubmed
12407001
uniprot
proteins
pubmed
12624133
uniprot
proteins
pubmed
12709788
uniprot
proteins
pubmed
12763760
uniprot
proteins
pubmed
12966036
uniprot
proteins
pubmed
14576201
uniprot
proteins
pubmed
14754908
uniprot
proteins
pubmed
15019541
uniprot
proteins
pubmed
15158913
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15262183
uniprot
proteins
pubmed
15297675
uniprot
proteins
pubmed
15520867
uniprot
proteins
pubmed
15722566
uniprot
proteins
pubmed
15790791
uniprot
proteins
pubmed
16226177
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17205124
uniprot
proteins
pubmed
18354102
uniprot
proteins
pubmed
18776170
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19258317
uniprot
proteins
pubmed
19556522
uniprot
proteins
pubmed
23931754
uniprot
proteins
pubmed
24097981
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27535533
uniprot
proteins
pubmed
28882873
uniprot
proteins
pubmed
35974019
uniprot
proteins
sequence_length
2261
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19258317, ECO:0000269|PubMed:19556522, ECO:0000269|PubMed:24097981, ECO:0000269|PubMed:35974019}; Multi-pass membrane protein {ECO:0000255}. Endosome {ECO:0000269|PubMed:24097981}.
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 1041..1057; /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