ABCA3_MOUSE
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 03-AUG-2022, entry version 148.
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 cleveage 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 STRING; 10090.ENSMUSP00000045285; -.
DR GlyConnect; 2141; 1 N-Linked glycan (1 site).
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; Q8R420; -.
DR PeptideAtlas; Q8R420; -.
DR PRIDE; Q8R420; -.
DR ProteomicsDB; 285951; -.
DR Antibodypedia; 1409; 78 antibodies from 19 providers.
DR DNASU; 27410; -.
DR Ensembl; ENSMUST00000039013; ENSMUSP00000045285; ENSMUSG00000024130.
DR Ensembl; ENSMUST00000079594; ENSMUSP00000078544; ENSMUSG00000024130.
DR GeneID; 27410; -.
DR KEGG; mmu:27410; -.
DR UCSC; uc008avm.2; mouse.
DR CTD; 21; -.
DR MGI; MGI:1351617; Abca3.
DR VEuPathDB; HostDB:ENSMUSG00000024130; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000155289; -.
DR InParanoid; Q8R420; -.
DR OMA; MAIANTW; -.
DR OrthoDB; 131191at2759; -.
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; 2 hits in 72 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 253 other tissues.
DR ExpressionAtlas; Q8R420; baseline and differential.
DR Genevisible; Q8R420; MM.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
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; PTHR19229; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
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
