Abca3
entrez
302973
canonical
uniprot
A0A0G2K1Q8
canonical
ensembl
ENSRNOG00000050057
resolver
ensp
ENSRNOP00000071944
resolver
enst
ENSRNOT00000079700
resolver
genesymbol
Abca3
resolver
uniprot_entry
ABCA3_RAT
resolver
amino_acid_sequence
MVVLRQLRLLLWKNYTLKKRKVLVTVLELFLPLLFSGILIWLRLKIQSENVPNATVYPDQHIQELPLFFSFPPPGGSWELAYVPSHSDAARTITEAVRREFMIKMRVHGFSSEKDFEDYVRYDNHSSNVLAAVVFEHTFNHSKDPLPLAVRYHLRFSYTRRNYMWTQTGNLFLKETEGWHTASLFPLFPSPGPREPSSPDGGEPGYIREGFLAVQHAVDKAIMHYHANASAHQLFQKLTVITKRFPFPPYISDPFLIAIQYQLPLLLMLSFTYTSLTIIRAVVQEKEKKLKEYMRMMGLSSWLHWSAWFLMFLLFSLIVVSFMTLLFCVKVKKDIAVLSNSDPSLVLAFLLCFAISSISFSFMVSTFFSKANMAATVGGFLYFFTYTPYFFVAPRYNWMTLSQKLLSCLLSNVAMAMGAQLIGKFEAKGTGIQWCDLLNPVNVDDDFCFGQVLGMLLLDSVLYGLVTWYVEAVFPGQFGVPQPWYFFLMPSYWCGNPRTVVGKEEEGGDPEKAFRTEYFEAEPEDLAAGIKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSMLTGLFPPTSGHAYIRGYEISQDMVQIRKSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSVQKCPEEVKQMLHTLGLEDKRDSRSKFLSGGMKRKLAIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLKQKYGAGYHMTLVKEPHCNPEGISQLVHHHVPNAMLESHAGAELSFILPKESTHRFESLFAKLEKKQKELGIASFGASVTTMEEVFLRVGKLVDTSMDIQAIQLPALQYQHERRASDWALDSNLCGVMDPTNGIGALIEEEEVLVKLNTGLALHCQQFWAMFLKKAAYSWREWRMVAAQILVPVTCLTLALLAINYTSEIFDDPPLKLSLNEYGTTVVPFSVPGTSRLGQQLSEHLRDMLQAERQEPREVLGDLEEFLVFRASVEGGGFNERCLVATSFKDSGERTVVTALFNNQAYHSPATALAIVDNLLFKLLCGPRASIEISNYPQPRSTLQVAKDQFNEGRKGFDIALNLLIAMAFLASTFSILAVSERAVQAKHVQFVSGVHVATFWLSALLWDLISFLVPSLLLLVVFRAFDVHAFTRDGHMADLLLLLMLYGWAIIPLMYLLSFFFSAASTAYTRLTIFNILSGIATFIVVTIMRIPAVKLEELSRTLDHVFLVLPNHCLGMAVSNFYENYETRRYCTSSEVATHYCKKYNIQYQENFYAWSTPGIGKFVTSMAASGGIYLTLLFLIETNLLWRLRTFVCAFRRRWTLAELQNRTSVLPEDQDVADERSRVLVPSLDSMLDTPLIINELSKVYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGYCPQFDALLDHMTGREMLVMYARLRGIPERLIDACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGYSLQAKVRSEGKQEVLEEFKAFVDLTFPGSVLEDEHQDMVHYHLPGCDLSWAKVFGILEKAKEKYGVDDYSVSQISLEQVFLSFAHLQPPTTEDGR
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. Transports preferentially phosphatidylcholine containing short acyl chains. 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. {ECO:0000250|UniProtKB:Q99758}.
uniprot
proteins
mass_dalton
191767
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. Localization at intracellular vesicles is accompanied by processing of oligosaccharide from high mannose type to complex type. N-linked glycosylation at Asn-124 and Asn-140 is required for stability and efficient anterograde trafficking and prevents from proteasomal degradation. {ECO:0000250|UniProtKB:Q99758}.; 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:0000250|UniProtKB:Q99758}.
uniprot
proteins
pubmed
11940594
uniprot
proteins
pubmed
15057822
uniprot
proteins
sequence_length
1704
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:Q99758}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q99758}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q99758}. Late endosome membrane {ECO:0000250|UniProtKB:Q99758}. Lysosome membrane {ECO:0000250|UniProtKB:Q99758}. Note=Localized in the limiting membrane of lamellar bodies in lung alveolar type II cells. 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. Oligomers formation takes place in a post-endoplasmic reticulum compartment. {ECO:0000250|UniProtKB:Q99758}.
uniprot
proteins
transmembrane_region
TRANSMEM 22..42; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 251..271; /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 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 1310..1330; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins