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Details on Person UniProt:Q99758 ABCA3

Class:Id	ReferenceGeneProduct:49416
_chainChangeLog	chain:1-1704 added on Fri February 6 2015;chain:175-1704 for 49416 added on Thu May 6 2021
_displayName	UniProt:Q99758 ABCA3
_timestamp	2025-05-21 21:34:43
chain	chain:1-1704 chain:175-1704
checksum	606735C504839D0D
comment	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).CATALYTIC ACTIVITY ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.CATALYTIC ACTIVITY a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ADP + phosphate + H(+)CATALYTIC ACTIVITY ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.CATALYTIC ACTIVITY 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine(in) + ATP + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine(out) + ADP + phosphate + H(+)CATALYTIC ACTIVITY cholesterol(in) + ATP + H2O = cholesterol(out) + ADP + phosphate + H(+)CATALYTIC ACTIVITY a 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)(in) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)(out) + ADP + phosphate + H(+)ACTIVITY REGULATION The ATP-dependent phosphatidylcholine transport is competitively inhibited by miltefosine.SUBUNIT Homooligomer; disulfide-linked.SUBCELLULAR LOCATION 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).ALTERNATIVE PRODUCTS Expressed in brain, pancreas, skeletal muscle and heart (PubMed:8706931). Highly expressed in the lung in an AT2-cell-specific manner (PubMed:11718719, PubMed:8706931). Weakly expressed in placenta, kidney and liver (PubMed:8706931). Also expressed in medullary thyroid carcinoma cells (MTC) and in C-cell carcinoma (PubMed:8706931).INDUCTION Up-regulated in Leishmania Viannia (L.V.) panamensis-infected macrophages exposed to miltefosine (PubMed:26903515). Down-regulated by L.V.panamensis infection (PubMed:26903515).DOMAIN Multifunctional polypeptide with two homologous halves, each containing a hydrophobic membrane-anchoring domain and an ATP binding cassette (ABC) domain.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).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.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the ABC transporter superfamily. ABCA family.ONLINE INFORMATION Database for mutations in ABC proteins
description	recommendedName: fullName evidence="26"Phospholipid-transporting ATPase ABCA3 ecNumber evidence="11 21 22"7.6.2.1 alternativeName: ABC-C transporter alternativeName: fullName evidence="26"ATP-binding cassette sub-family A member 3 alternativeName: ATP-binding cassette transporter 3 shortName: ATP-binding cassette 3 alternativeName: fullName evidence="26"Xenobiotic-transporting ATPase ABCA3 ecNumber evidence="27"7.6.2.2 component recommendedName: fullName evidence="28"150 Kda mature form /component
geneName	ABCA3 ABC3
identifier	Q99758
isSequenceChanged	FALSE
keyword	3D-structure Alternative splicing ATP-binding Cytoplasmic vesicle Disease variant Disulfide bond Endosome Glycoprotein Lipid transport Lysosome Membrane Nucleotide-binding Proteomics identification Reference proteome Repeat Translocase Transmembrane Transmembrane helix Transport
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9948485] Weiser, Joel, 2025-05-21
name	ABCA3
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:8994030] ENSEMBL:ENSG00000167972 ABCA3 [Homo sapiens]
secondaryIdentifier	ABCA3_HUMAN B2RU09 Q54A95 Q6P5P9 Q92473
sequenceLength	1704
species	[Species:48887] Homo sapiens
(isoformParent)	[ReferenceIsoform:8966411] UniProt:Q99758-1 ABCA3 [Homo sapiens] [ReferenceIsoform:8966412] UniProt:Q99758-2 ABCA3 [Homo sapiens]
(referenceEntity)	[EntityWithAccessionedSequence:1369005] ABCA3 [lamellar body membrane] [Homo sapiens] [EntityWithAccessionedSequence:5683658] ABCA3 L101P [lamellar body membrane] [Homo sapiens] [EntityWithAccessionedSequence:5683666] ABCA3 L326P [lamellar body membrane] [Homo sapiens] [EntityWithAccessionedSequence:5683671] ABCA3 L1553P [lamellar body membrane] [Homo sapiens] [EntityWithAccessionedSequence:5683691] ABCA3 W1142* [lamellar body membrane] [Homo sapiens] [EntityWithAccessionedSequence:5683697] ABCA3 D253H [lamellar body membrane] [Homo sapiens] [EntityWithAccessionedSequence:5683705] ABCA3 T1173R [lamellar body membrane] [Homo sapiens] [EntityWithAccessionedSequence:5688388] ABCA3 N568D [lamellar body membrane] [Homo sapiens] [EntityWithAccessionedSequence:5688389] ABCA3 E690K [lamellar body membrane] [Homo sapiens] [EntityWithAccessionedSequence:5688390] ABCA3 T1114M [lamellar body membrane] [Homo sapiens] List all 11 refering instances
(referenceSequence)	[ReplacedResidue:5683659] L-leucine 101 replaced with L-proline [ReplacedResidue:5683668] L-threonine 1173 replaced with L-arginine [ReplacedResidue:5683674] L-aspartic acid 253 replaced with L-histidine [ReplacedResidue:5683682] L-leucine 1553 replaced with L-proline [NonsenseMutation:5683690] Nonsense mutation at L-tryptophan 1142 [ReplacedResidue:5683695] L-leucine 326 replaced with L-proline [ReplacedResidue:5688381] L-glutamic acid 690 replaced with L-lysine [ReplacedResidue:5688382] L-threonine 1114 replaced with L-methionine [ReplacedResidue:5688384] L-glutamic acid 292 replaced with L-valine [ReplacedResidue:5688405] L-asparagine 568 replaced with L-aspartic acid
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No pathways have been reviewed or authored by UniProt:Q99758 ABCA3 (49416)