ID   ABCA3_MOUSE             Reviewed;        1704 AA.
AC   Q8R420; Q3U3L4;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 3.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Phospholipid-transporting ATPase ABCA3 {ECO:0000305};
DE            EC=7.6.2.1 {ECO:0000269|PubMed:17142808};
DE   AltName: Full=ATP-binding cassette sub-family A member 3 {ECO:0000305};
DE   AltName: Full=Xenobiotic-transporting ATPase ABCA3 {ECO:0000250|UniProtKB:Q99758};
DE            EC=7.6.2.2 {ECO:0000250|UniProtKB:Q99758};
DE   Contains:
DE     RecName: Full=150 Kda mature form {ECO:0000250|UniProtKB:Q99758};
GN   Name=Abca3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv;
RA   Gray J.M., Zhao M., Fisher A.B., Shuman H.;
RT   "Mus musculus ABCA3 cDNA.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 117-197, AND SUBCELLULAR LOCATION.
RX   PubMed=11940594; DOI=10.1074/jbc.m201812200;
RA   Mulugeta S., Gray J.M., Notarfrancesco K.L., Gonzales L.W., Koval M.,
RA   Feinstein S.I., Ballard P.L., Fisher A.B., Shuman H.;
RT   "Identification of LBM180, a lamellar body limiting membrane protein of
RT   alveolar type II cells, as the ABC transporter protein ABCA3.";
RL   J. Biol. Chem. 277:22147-22155(2002).
RN   [4]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17577581; DOI=10.1016/j.bbrc.2007.05.219;
RA   Hammel M., Michel G., Hoefer C., Klaften M., Mueller-Hoecker J.,
RA   de Angelis M.H., Holzinger A.;
RT   "Targeted inactivation of the murine Abca3 gene leads to respiratory
RT   failure in newborns with defective lamellar bodies.";
RL   Biochem. Biophys. Res. Commun. 359:947-951(2007).
RN   [5]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17540762; DOI=10.1074/jbc.m703927200;
RA   Cheong N., Zhang H., Madesh M., Zhao M., Yu K., Dodia C., Fisher A.B.,
RA   Savani R.C., Shuman H.;
RT   "ABCA3 is critical for lamellar body biogenesis in vivo.";
RL   J. Biol. Chem. 282:23811-23817(2007).
RN   [6]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17267394; DOI=10.1074/jbc.m611767200;
RA   Ban N., Matsumura Y., Sakai H., Takanezawa Y., Sasaki M., Arai H.,
RA   Inagaki N.;
RT   "ABCA3 as a lipid transporter in pulmonary surfactant biogenesis.";
RL   J. Biol. Chem. 282:9628-9634(2007).
RN   [7]
RP   DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX   PubMed=17142808; DOI=10.1194/jlr.m600449-jlr200;
RA   Fitzgerald M.L., Xavier R., Haley K.J., Welti R., Goss J.L., Brown C.E.,
RA   Zhuang D.Z., Bell S.A., Lu N., McKee M., Seed B., Freeman M.W.;
RT   "ABCA3 inactivation in mice causes respiratory failure, loss of pulmonary
RT   surfactant, and depletion of lung phosphatidylglycerol.";
RL   J. Lipid Res. 48:621-632(2007).
RN   [8]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=20190032; DOI=10.1152/ajplung.00409.2009;
RA   Besnard V., Matsuzaki Y., Clark J., Xu Y., Wert S.E., Ikegami M.,
RA   Stahlman M.T., Weaver T.E., Hunt A.N., Postle A.D., Whitsett J.A.;
RT   "Conditional deletion of Abca3 in alveolar type II cells alters surfactant
RT   homeostasis in newborn and adult mice.";
RL   Am. J. Physiol. 298:L646-L659(2010).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [10]
RP   MUTAGENESIS OF GLU-292, AND FUNCTION.
RX   PubMed=28034695; DOI=10.1016/j.aanat.2016.11.015;
RA   Beers M.F., Knudsen L., Tomer Y., Maronn J., Zhao M., Ochs M., Mulugeta S.;
RT   "Aberrant lung remodeling in a mouse model of surfactant dysregulation
RT   induced by modulation of the Abca3 gene.";
RL   Ann. Anat. 210:135-146(2017).
CC   -!- FUNCTION: Catalyzes the ATP-dependent transport of phospholipids such
CC       as phosphatidylcholine and phosphoglycerol from the cytoplasm into the
CC       lumen side of lamellar bodies, in turn participates in the lamellar
CC       bodies biogenesis and homeostasis of pulmonary surfactant
CC       (PubMed:17577581, PubMed:17540762, PubMed:17267394, PubMed:17142808,
CC       PubMed:20190032, PubMed:28034695). Transports preferentially
CC       phosphatidylcholine containing short acyl chains (PubMed:17142808). In
CC       addition plays a role as an efflux transporter of miltefosine across
CC       macrophage membranes and free cholesterol (FC) through intralumenal
CC       vesicles by removing FC from the cell as a component of surfactant and
CC       protects cells from free cholesterol toxicity (By similarity).
CC       {ECO:0000250|UniProtKB:Q99758, ECO:0000269|PubMed:17142808,
CC       ECO:0000269|PubMed:17267394, ECO:0000269|PubMed:17540762,
CC       ECO:0000269|PubMed:17577581, ECO:0000269|PubMed:20190032,
CC       ECO:0000269|PubMed:28034695}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)(in) + ATP +
CC         H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)(out) + ADP +
CC         H(+) + phosphate; Xref=Rhea:RHEA:66344, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:64716, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:17142808};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66345;
CC         Evidence={ECO:0000269|PubMed:17142808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ATP + H2O = a
CC         1,2-diacyl-sn-glycero-3-phosphocholine(out) + ADP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:66272, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17142808};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66273;
CC         Evidence={ECO:0000269|PubMed:17142808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC         phospholipidSide 2.; EC=7.6.2.1;
CC         Evidence={ECO:0000269|PubMed:17142808};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC         xenobioticSide 2.; EC=7.6.2.2;
CC         Evidence={ECO:0000250|UniProtKB:Q99758};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine(in) + ATP + H2O
CC         = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine(out) + ADP + H(+) +
CC         phosphate; Xref=Rhea:RHEA:66340, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:72999, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q99758};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66341;
CC         Evidence={ECO:0000250|UniProtKB:Q99758};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) +
CC         phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q99758};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC         Evidence={ECO:0000250|UniProtKB:Q99758};
CC   -!- SUBUNIT: Homooligomer; disulfide-linked.
CC       {ECO:0000250|UniProtKB:Q99758}.
CC   -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC       {ECO:0000250|UniProtKB:Q99758}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q99758}. Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:Q99758}. Late endosome membrane
CC       {ECO:0000250|UniProtKB:Q99758}. Lysosome membrane
CC       {ECO:0000250|UniProtKB:Q99758}. Note=Localized in the limiting membrane
CC       of lamellar bodies in lung alveolar type II cells (PubMed:11940594).
CC       Trafficks via the Golgi, sorting vesicles (SVs) and late
CC       endosome/multivesicular body network directly to the outer membrane of
CC       lamellar bodies in AT2 lung epithelial cells or to lysosomes and
CC       lysosomal-related organelles (LROs) in other cells where undergoes
CC       proteolytic cleavage and oligosaccharide processing from high mannose
CC       type to complex type. Oligomers formation takes place in a post-
CC       endoplasmic reticulum compartment (By similarity).
CC       {ECO:0000250|UniProtKB:Q99758, ECO:0000269|PubMed:11940594}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the lung and moderately
CC       expressed in the kidney, adipose, macrophage, and spleen.
CC       {ECO:0000269|PubMed:17142808}.
CC   -!- DOMAIN: Multifunctional polypeptide with two homologous halves, each
CC       containing a hydrophobic membrane-anchoring domain and an ATP binding
CC       cassette (ABC) domain. {ECO:0000250}.
CC   -!- PTM: N-glycosylated. Localization at intracellular vesicles is
CC       accompanied by processing of oligosaccharide from high mannose type to
CC       complex type. N-linked glycosylation at Asn-124 and Asn-140 is required
CC       for stability and efficient anterograde trafficking and prevents from
CC       proteasomal degradation. {ECO:0000250|UniProtKB:Q99758}.
CC   -!- PTM: Proteolytically cleaved by CTSL and to a lower extent by CTSB
CC       within multivesicular bodies (MVB) and lamellar bodies (LB) leading to
CC       a mature form of 150 kDa. {ECO:0000250|UniProtKB:Q99758}.
CC   -!- DISRUPTION PHENOTYPE: Homozygous knockout mice for ABCA3 are die within
CC       one hour after birth (PubMed:17577581, PubMed:17540762,
CC       PubMed:17267394). Mice develop respiratory failure immediately after
CC       birth with clinical signs such as gasping, cyanosis, failure to achieve
CC       inflation of the lung as visible through the skin and reduced motor
CC       activity and (PubMed:17577581, PubMed:17142808, PubMed:17267394).
CC       Conditional knockout mice in which ABCA3 is deleted in alveolar type II
CC       cells die shortly after birth from respiratory distress related to
CC       surfactant deficiency but approximately 30% of these mice survive after
CC       birth and develop emphysema in the absence of significant pulmonary
CC       inflammation (PubMed:20190032). {ECO:0000269|PubMed:17142808,
CC       ECO:0000269|PubMed:17267394, ECO:0000269|PubMed:17540762,
CC       ECO:0000269|PubMed:17577581, ECO:0000269|PubMed:20190032}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC       {ECO:0000305}.
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DR   EMBL; AY083616; AAL99380.1; -; mRNA.
DR   EMBL; AK154698; BAE32771.1; -; mRNA.
DR   CCDS; CCDS37486.1; -.
DR   RefSeq; NP_001034670.1; NM_001039581.2.
DR   RefSeq; NP_038883.2; NM_013855.3.
DR   RefSeq; XP_006524433.1; XM_006524370.2.
DR   AlphaFoldDB; Q8R420; -.
DR   SMR; Q8R420; -.
DR   BioGRID; 205216; 1.
DR   STRING; 10090.ENSMUSP00000045285; -.
DR   GlyConnect; 2141; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q8R420; 7 sites, 1 glycan.
DR   GlyGen; Q8R420; 7 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q8R420; -.
DR   PhosphoSitePlus; Q8R420; -.
DR   SwissPalm; Q8R420; -.
DR   EPD; Q8R420; -.
DR   MaxQB; Q8R420; -.
DR   PaxDb; 10090-ENSMUSP00000045285; -.
DR   PeptideAtlas; Q8R420; -.
DR   ProteomicsDB; 285951; -.
DR   Pumba; Q8R420; -.
DR   Antibodypedia; 1409; 99 antibodies from 19 providers.
DR   DNASU; 27410; -.
DR   Ensembl; ENSMUST00000039013.15; ENSMUSP00000045285.9; ENSMUSG00000024130.17.
DR   Ensembl; ENSMUST00000079594.12; ENSMUSP00000078544.6; ENSMUSG00000024130.17.
DR   GeneID; 27410; -.
DR   KEGG; mmu:27410; -.
DR   UCSC; uc008avm.2; mouse.
DR   AGR; MGI:1351617; -.
DR   CTD; 21; -.
DR   MGI; MGI:1351617; Abca3.
DR   VEuPathDB; HostDB:ENSMUSG00000024130; -.
DR   eggNOG; KOG0059; Eukaryota.
DR   GeneTree; ENSGT00940000155289; -.
DR   InParanoid; Q8R420; -.
DR   OMA; VCPQDDA; -.
DR   OrthoDB; 6951at2759; -.
DR   PhylomeDB; Q8R420; -.
DR   TreeFam; TF105191; -.
DR   Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
DR   Reactome; R-MMU-5683826; Surfactant metabolism.
DR   BioGRID-ORCS; 27410; 3 hits in 77 CRISPR screens.
DR   ChiTaRS; Abca3; mouse.
DR   PRO; PR:Q8R420; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q8R420; Protein.
DR   Bgee; ENSMUSG00000024130; Expressed in left lung lobe and 255 other cell types or tissues.
DR   ExpressionAtlas; Q8R420; baseline and differential.
DR   GO; GO:0097208; C:alveolar lamellar body; ISO:MGI.
DR   GO; GO:0097233; C:alveolar lamellar body membrane; IDA:UniProtKB.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0042599; C:lamellar body; ISO:MGI.
DR   GO; GO:0097232; C:lamellar body membrane; ISO:MGI.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR   GO; GO:0140345; F:phosphatidylcholine flippase activity; ISS:UniProtKB.
DR   GO; GO:0120019; F:phosphatidylcholine transfer activity; ISS:UniProtKB.
DR   GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR   GO; GO:0030324; P:lung development; IMP:UniProtKB.
DR   GO; GO:0070925; P:organelle assembly; IMP:UniProtKB.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IMP:UniProtKB.
DR   GO; GO:0046471; P:phosphatidylglycerol metabolic process; IMP:UniProtKB.
DR   GO; GO:0055091; P:phospholipid homeostasis; IMP:UniProtKB.
DR   GO; GO:0015914; P:phospholipid transport; ISS:UniProtKB.
DR   GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB.
DR   GO; GO:1902995; P:positive regulation of phospholipid efflux; ISS:UniProtKB.
DR   GO; GO:2001140; P:positive regulation of phospholipid transport; ISS:UniProtKB.
DR   GO; GO:0032464; P:positive regulation of protein homooligomerization; ISO:MGI.
DR   GO; GO:0046890; P:regulation of lipid biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0032368; P:regulation of lipid transport; IMP:UniProtKB.
DR   GO; GO:0150172; P:regulation of phosphatidylcholine metabolic process; ISS:UniProtKB.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0043129; P:surfactant homeostasis; IMP:UniProtKB.
DR   GO; GO:0046618; P:xenobiotic export from cell; ISS:UniProtKB.
DR   GO; GO:0006855; P:xenobiotic transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0042908; P:xenobiotic transport; ISS:UniProtKB.
DR   CDD; cd03263; ABC_subfamily_A; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC2_TM.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR026082; ABCA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR   PANTHER; PTHR19229:SF98; PHOSPHOLIPID-TRANSPORTING ATPASE ABCA3; 1.
DR   Pfam; PF12698; ABC2_membrane_3; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   Genevisible; Q8R420; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasmic vesicle; Disulfide bond; Endosome; Glycoprotein;
KW   Lipid transport; Lysosome; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1704
FT                   /note="Phospholipid-transporting ATPase ABCA3"
FT                   /id="PRO_0000093294"
FT   CHAIN           175..1704
FT                   /note="150 Kda mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q99758"
FT                   /id="PRO_0000452298"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        925..945
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1100..1120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1144..1164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1183..1203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1213..1233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1245..1265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1310..1330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          530..763
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          1381..1614
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         566..573
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1416..1423
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   SITE            174..175
FT                   /note="Cleavage; by CTSL"
FT                   /evidence="ECO:0000250|UniProtKB:Q99758"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        620
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         292
FT                   /note="E->V: Knockin new born mice are healthy and survive
FT                   into adulthood without overt signs of respiratory distress.
FT                   Knockin mice show a severe lung phenotype that begins with
FT                   alveolar inflammatory cell infiltration at the early stage
FT                   of the mouse life followed by aberrant lung remodeling with
FT                   characteristics of diffuse parenchymal lung disease
FT                   (DPLD)- and emphysema-like alveolar disruption in older
FT                   mice."
FT                   /evidence="ECO:0000269|PubMed:28034695"
FT   CONFLICT        217
FT                   /note="A -> T (in Ref. 1; AAL99380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        446
FT                   /note="N -> D (in Ref. 1; AAL99380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        589
FT                   /note="H -> R (in Ref. 1; AAL99380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        693
FT                   /note="S -> P (in Ref. 1; AAL99380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        939
FT                   /note="L -> Q (in Ref. 1; AAL99380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1069
FT                   /note="Q -> W (in Ref. 1; AAL99380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1143
FT                   /note="F -> L (in Ref. 1; AAL99380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1185
FT                   /note="L -> P (in Ref. 1; AAL99380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1232
FT                   /note="R -> C (in Ref. 1; AAL99380)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1704 AA;  191971 MW;  6741132D2CA30897 CRC64;
     MAVLRQLTLL LWKNYTLKKR KVLVTVLELF LPLLFSGILI WLRLKIQSEN VPNATVYPDQ
     SIQELPLFFS FPPPGGTWEL AYVPSHSDAA RTITETVKRE FMIKMRVHGF SSEKDFEDYI
     RYDNHSSSVL AAVVFEHSFN HSQDPLPLAV KYHLRFSYTR RNYMWTQTGN IFLKETEGWH
     TTSLFPLFPS PGPREPSSPD GGEPGYIREG FLAMQHAVDK AIMRYHANTS AQQLFQKLMV
     ITKRFPFPPY ISDPFLIAIQ YQLPLLLMLS FTYTSLTIIR AVVQEKEKKL KEYMRMMGLN
     SWLHWSAWFL MFFLFFLIVV SFMTLLFCVK VKKDIAVLSN SDPSLVLAFL LCFAISSISF
     SFMVSTFFSK ANIAAAVGGF LYFFTYTPYF FVAPRYNWMT LSQKLLSCLL SNVAMAMGAQ
     LIGKFEAKGT GIQWRDLLNP VNVDDNFCFG QVLGMLLLDS ALYGLVTWYV EAVFPGQFGV
     PQPWHFFLMP SYWCGNPRTV VGKEEEGSDP EKALRNEYFE AEPEDLVAGI KIKHLSKVFQ
     VGNKDKMGIR DLTLNLYEGQ ITVLLGHNGA GKTTTMSLLT GLFPPTSGHA YIHGYEISQD
     MAQIRKSLGL CPQHDVLFDN LTVAEHLYFY AQLKGLSLQK CPEEVKQMLH ILSLEDKRDL
     RSKFLSGGMK RKLSIGIALI AGSKVLMLDE PTSGMDAVSR RAIWDLLQQQ KSDRTVLLTT
     HFMDEADLLG DRIAILAKGE LQCCGSSLFL KQKYGAGYHM TLVKEPHCNP EGISQLVHHH
     VPNAMLESHA GAELSFILPK ESTHRFESLF AKLEKKQKEL GIASFGASVT TMEEVFLRVG
     KLVDTSMDIQ AIQLPALQYQ HERRASDWAL DSNLCGVMDP TNGIGALIEE EEVLVKLNTG
     LALHCQQFWA MFLKKAAYSW REWKMVAAQV LVPLTCLTLA LLAIHYTSEI FDDPLLKLSL
     NEYGRTVVPF SVPGTSRLAQ QLSENLRDML QAERQEPREV LGDLEEFLVF RASVEGGGFN
     ERCLVATSFK DRGELTVVTA LFNNQAYHSP ATALAIVDNL LFKLLCGPQA SIEISNYPQP
     RNTLQVAKDH FNEGRKGFDI ALNLLIAMAF LASTFSILAV SERAVQAKHV QFVSGVHVAT
     FWFSALLWDL ISFLVPSLLL LVVFQAFNVH AFTRDGHMAD LLLLLMLYGW AIIPLMYLMS
     FFFSAASTAY TRLTIFNILS GIATFIMVTI MRIPAVKLEE LSRTLDHVFL VLPNHCLGMA
     VSNFYENYET RRYCTSSELA AHYCKKYNIQ YQESFYAWST PGVGKFVTSM AASGGIYLTL
     LFLIETNLLW RLRTFICAFR RRWTLAELQN RTSVLPEDQD VAEERSRILV PSLDSMLDTP
     LIINELSKVY DQRAPLLAVD RISLAVQKGE CFGLLGFNGA GKTTTFKMLT GEETITSGDA
     FVGGYSISSD IGKVRQRMGY CPQFDALLDH MTGREMLVMY ARLRGIPERL INACVENTLR
     GLLLEPHANK LVKTYSGGNK RKLSTGIALI GEPAVIFLDE PSTGMDPVAR RLLWDTVARA
     RESGKAIVIT SHSMEECEAL CTRLAIMVQG QFKCLGSPQH LKSKFGSGYS LQAKVRSEGK
     QDALEEFKAF VDLTFPGSIL EDEHQDMVHY HLPGCDLSWA KVFGILEKAK EKYGVDDYSV
     SQISLEQVFL SFAHLQPPTT EDGR
//