ABCA3
entrez
21
canonical
uniprot
Q99758
canonical
ensembl
ENSG00000167972
resolver
ensp
ENSP00000301732
resolver
genesymbol
ABCA3
resolver
genesymbol_syn
ABC3
resolver
hgnc
HGNC:33
resolver
uniprot
B2RU09
resolver
uniprot
Q54A95
resolver
uniprot
Q6P5P9
resolver
uniprot
Q92473
resolver
uniprot_entry
ABCA3_HUMAN
resolver
uniprot_sec
B2RU09
resolver
uniprot_sec
Q54A95
resolver
uniprot_sec
Q6P5P9
resolver
uniprot_sec
Q92473
resolver
activity_regulation
ACTIVITY REGULATION: The ATP-dependent phosphatidylcholine transport is competitively inhibited by miltefosine. {ECO:0000269|PubMed:31473345}.
uniprot
proteins
amino_acid_sequence
MAVLRQLALLLWKNYTLQKRKVLVTVLELFLPLLFSGILIWLRLKIQSENVPNATIYPGQSIQELPLFFTFPPPGDTWELAYIPSHSDAAKTVTETVRRALVINMRVRGFPSEKDFEDYIRYDNCSSSVLAAVVFEHPFNHSKEPLPLAVKYHLRFSYTRRNYMWTQTGSFFLKETEGWHTTSLFPLFPNPGPREPTSPDGGEPGYIREGFLAVQHAVDRAIMEYHADAATRQLFQRLTVTIKRFPYPPFIADPFLVAIQYQLPLLLLLSFTYTALTIARAVVQEKERRLKEYMRMMGLSSWLHWSAWFLLFFLFLLIAASFMTLLFCVKVKPNVAVLSRSDPSLVLAFLLCFAISTISFSFMVSTFFSKANMAAAFGGFLYFFTYIPYFFVAPRYNWMTLSQKLCSCLLSNVAMAMGAQLIGKFEAKGMGIQWRDLLSPVNVDDDFCFGQVLGMLLLDSVLYGLVTWYMEAVFPGQFGVPQPWYFFIMPSYWCGKPRAVAGKEEEDSDPEKALRNEYFEAEPEDLVAGIKIKHLSKVFRVGNKDRAAVRDLNLNLYEGQITVLLGHNGAGKTTTLSMLTGLFPPTSGRAYISGYEISQDMVQIRKSLGLCPQHDILFDNLTVAEHLYFYAQLKGLSRQKCPEEVKQMLHIIGLEDKWNSRSRFLSGGMRRKLSIGIALIAGSKVLILDEPTSGMDAISRRAIWDLLQRQKSDRTIVLTTHFMDEADLLGDRIAIMAKGELQCCGSSLFLKQKYGAGYHMTLVKEPHCNPEDISQLVHHHVPNATLESSAGAELSFILPRESTHRFEGLFAKLEKKQKELGIASFGASITTMEEVFLRVGKLVDSSMDIQAIQLPALQYQHERRASDWAVDSNLCGAMDPSDGIGALIEEERTAVKLNTGLALHCQQFWAMFLKKAAYSWREWKMVAAQVLVPLTCVTLALLAINYSSELFDDPMLRLTLGEYGRTVVPFSVPGTSQLGQQLSEHLKDALQAEGQEPREVLGDLEEFLIFRASVEGGGFNERCLVAASFRDVGERTVVNALFNNQAYHSPATALAVVDNLLFKLLCGPHASIVVSNFPQPRSALQAAKDQFNEGRKGFDIALNLLFAMAFLASTFSILAVSERAVQAKHVQFVSGVHVASFWLSALLWDLISFLIPSLLLLVVFKAFDVRAFTRDGHMADTLLLLLLYGWAIIPLMYLMNFFFLGAATAYTRLTIFNILSGIATFLMVTIMRIPAVKLEELSKTLDHVFLVLPNHCLGMAVSSFYENYETRRYCTSSEVAAHYCKKYNIQYQENFYAWSAPGVGRFVASMAASGCAYLILLFLIETNLLQRLRGILCALRRRRTLTELYTRMPVLPEDQDVADERTRILAPSPDSLLHTPLIIKELSKVYEQRVPLLAVDRLSLAVQKGECFGLLGFNGAGKTTTFKMLTGEESLTSGDAFVGGHRISSDVGKVRQRIGYCPQFDALLDHMTGREMLVMYARLRGIPERHIGACVENTLRGLLLEPHANKLVRTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIIITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGYSLRAKVQSEGQQEALEEFKAFVDLTFPGSVLEDEHQGMVHYHLPGRDLSWAKVFGILEKAKEKYGVDDYSVSQISLEQVFLSFAHLQPPTAEEGR
uniprot
proteins
disease_involvement
DISEASE: Pulmonary surfactant metabolism dysfunction 3 (SMDP3) [MIM:610921]: A rare lung disorder due to impaired surfactant homeostasis. It is characterized by alveolar filling with floccular material that stains positive using the periodic acid-Schiff method and is derived from surfactant phospholipids and protein components. Excessive lipoproteins accumulation in the alveoli results in severe respiratory distress. {ECO:0000269|PubMed:15044640, ECO:0000269|PubMed:15976379, ECO:0000269|PubMed:16728712, ECO:0000269|PubMed:16959783, ECO:0000269|PubMed:17574245, ECO:0000269|PubMed:20863830, ECO:0000269|PubMed:25712598, ECO:0000269|PubMed:25817392, ECO:0000269|PubMed:27177387, ECO:0000269|PubMed:27352740, ECO:0000269|PubMed:28887056, ECO:0000269|PubMed:31473345}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
7.6.2.1
uniprot
proteins
ec_number
7.6.2.2
uniprot
proteins
function
FUNCTION: Catalyzes the ATP-dependent transport of phospholipids such as phosphatidylcholine and phosphoglycerol from the cytoplasm into the lumen side of lamellar bodies, in turn participates in the lamellar bodies biogenesis and homeostasis of pulmonary surfactant (PubMed:16959783, PubMed:17574245, PubMed:27177387, PubMed:28887056, PubMed:31473345). Transports preferentially phosphatidylcholine containing short acyl chains (PubMed:27177387). In addition plays a role as an efflux transporter of miltefosine across macrophage membranes and free cholesterol (FC) through intralumenal vesicles by removing FC from the cell as a component of surfactant and protects cells from free cholesterol toxicity (PubMed:25817392, PubMed:26903515, PubMed:27177387). {ECO:0000269|PubMed:16959783, ECO:0000269|PubMed:17574245, ECO:0000269|PubMed:25817392, ECO:0000269|PubMed:26903515, ECO:0000269|PubMed:27177387, ECO:0000269|PubMed:28887056, ECO:0000269|PubMed:31473345}.
uniprot
proteins
mass_dalton
191362
uniprot
proteins
mutagenesis
MUTAGEN 53; /note="N->Q: Does not affect N-glycosylation. Does not affect protein expression. Does not affect lamellar body membrane location."; /evidence="ECO:0000269|PubMed:24142515"; MUTAGEN 124; /note="N->Q: Loss of N-glycosylation. Reduces protein expression by 50%. Affects anterograde trafficking; when associated with Q-140. Reduces protein expression by 85%; when associated with Q-140. Does not affect lamellar body membrane location."; /evidence="ECO:0000269|PubMed:24142515"; MUTAGEN 140; /note="N->Q: Loss of N-glycosylation. Reduces protein expression by 50%. Affects anterograde trafficking; when associated with Q-124. Reduces protein expression by 85%; when associated with Q-140. Does not affect lamellar body membrane location."; /evidence="ECO:0000269|PubMed:24142515"; MUTAGEN 173..174; /note="LK->AA: Loss of proteolytic processing."; /evidence="ECO:0000269|PubMed:27031696"; MUTAGEN 693; /note="S->L: Does not affect protein oligomerization."; /evidence="ECO:0000269|PubMed:27352740"; MUTAGEN 945; /note="N->Q: Does not affect lamellar body membrane location. Does not affect protein expression. Does not affect proteolytic processing."; /evidence="ECO:0000269|PubMed:24142515"; MUTAGEN 1221; /note="G->A: Decreases ATP hydrolysis activity of 15% compared to the wild-type."; /evidence="ECO:0000269|PubMed:16959783"; MUTAGEN 1221; /note="G->T: Decreases ATP hydrolysis activity of 36% compared to the wild-type."; /evidence="ECO:0000269|PubMed:16959783"; MUTAGEN 1221; /note="G->V: Decreases ATP hydrolysis activity of 18% compared to the wild-type."; /evidence="ECO:0000269|PubMed:16959783"; MUTAGEN 1580; /note="L->A: Decreases ATP hydrolysis activity of 13% compared to the wild-type."; /evidence="ECO:0000269|PubMed:16959783"; MUTAGEN 1580; /note="L->F: Decreases ATP hydrolysis activity of 13% compared to the wild-type."; /evidence="ECO:0000269|PubMed:16959783"; MUTAGEN 1580; /note="L->V: Decreases ATP hydrolysis activity of 56% compared to the wild-type."; /evidence="ECO:0000269|PubMed:16959783
uniprot
proteins
post_translational_modification
PTM: N-glycosylated (PubMed:16959783, PubMed:24142515, PubMed:27177387). Localization at intracellular vesicles is accompanied by processing of oligosaccharide from high mannose type to complex type (PubMed:16959783, PubMed:27177387). N-linked glycosylation at Asn-124 and Asn-140 is required for stability and efficient anterograde trafficking and prevents from proteasomal degradation (PubMed:24142515). {ECO:0000269|PubMed:16959783, ECO:0000269|PubMed:24142515, ECO:0000269|PubMed:27177387}.; PTM: Proteolytically cleaved by CTSL and to a lower extent by CTSB within multivesicular bodies (MVB) and lamellar bodies (LB) leading to a mature form of 150 kDa. {ECO:0000269|PubMed:16959783, ECO:0000269|PubMed:20863830, ECO:0000269|PubMed:27031696, ECO:0000269|PubMed:27177387}.
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCA family
uniprot
proteins
pubmed
11718719
uniprot
proteins
pubmed
15044640
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
15976379
uniprot
proteins
pubmed
16728712
uniprot
proteins
pubmed
16959783
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17574245
uniprot
proteins
pubmed
20863830
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
24142515
uniprot
proteins
pubmed
25712598
uniprot
proteins
pubmed
25817392
uniprot
proteins
pubmed
26903515
uniprot
proteins
pubmed
27031696
uniprot
proteins
pubmed
27177387
uniprot
proteins
pubmed
27352740
uniprot
proteins
pubmed
28887056
uniprot
proteins
pubmed
31473345
uniprot
proteins
pubmed
8706931
uniprot
proteins
pubmed
9027511
uniprot
proteins
sequence_length
1704
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endosome, multivesicular body membrane {ECO:0000269|PubMed:16959783, ECO:0000269|PubMed:20863830, ECO:0000269|PubMed:27177387}; Multi-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:16959783, ECO:0000269|PubMed:17574245, ECO:0000269|PubMed:20863830, ECO:0000269|PubMed:22673903, ECO:0000269|PubMed:27177387, ECO:0000269|PubMed:31473345}. Late endosome membrane {ECO:0000269|PubMed:27177387}. Lysosome membrane {ECO:0000269|PubMed:16959783, ECO:0000269|PubMed:17574245, ECO:0000269|PubMed:20863830, ECO:0000269|PubMed:24142515}. Note=Localized in the limiting membrane of lamellar bodies in lung alveolar type II cells (PubMed:11718719, PubMed:16959783, PubMed:22673903, PubMed:24142515, PubMed:27177387). Trafficks via the Golgi, sorting vesicles (SVs) and late endosome/multivesicular body network directly to the outer membrane of lamellar bodies in AT2 lung epithelial cells or to lysosomes and lysosomal-related organelles (LROs) in other cells where undergoes proteolytic cleavage and oligosaccharide processing from high mannose type to complex type (PubMed:16959783, PubMed:20863830, PubMed:24142515, PubMed:27177387). Oligomers formation takes place in a post-endoplasmic reticulum compartment (PubMed:27352740). {ECO:0000269|PubMed:11718719, ECO:0000269|PubMed:16959783, ECO:0000269|PubMed:20863830, ECO:0000269|PubMed:22673903, ECO:0000269|PubMed:24142515, ECO:0000269|PubMed:27177387, ECO:0000269|PubMed:27352740}.
uniprot
proteins
transmembrane_region
TRANSMEM 22..42; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 261..283; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 307..327; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 344..364; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 373..393; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 405..425; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 447..467; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 925..945; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1100..1120; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1144..1164; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1183..1203; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1213..1233; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1245..1265; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1306..1326; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins