ID   ABCA1_MOUSE             Reviewed;        2261 AA.
AC   P41233; B1AWZ8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 4.
DT   27-MAR-2024, entry version 209.
DE   RecName: Full=Phospholipid-transporting ATPase ABCA1 {ECO:0000250|UniProtKB:O95477};
DE            EC=7.6.2.1 {ECO:0000250|UniProtKB:O95477};
DE   AltName: Full=ATP-binding cassette sub-family A member 1;
DE   AltName: Full=ATP-binding cassette transporter 1;
DE            Short=ABC-1;
DE            Short=ATP-binding cassette 1;
GN   Name=Abca1 {ECO:0000312|MGI:MGI:99607}; Synonyms=Abc1;
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=DBA/2J; TISSUE=Macrophage;
RX   PubMed=8088782; DOI=10.1006/geno.1994.1237;
RA   Luciani M.-F., Denizot F., Savary S., Mattei M.-G., Chimini G.;
RT   "Cloning of two novel ABC transporters mapping on human chromosome 9.";
RL   Genomics 21:150-159(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=11352567; DOI=10.1006/geno.2000.6467;
RA   Qiu Y., Cavelier L., Chiu S., Yang X., Rubin E., Cheng J.-F.;
RT   "Human and mouse ABCA1 comparative sequencing and transgenesis studies
RT   revealing novel regulatory sequences.";
RL   Genomics 73:66-76(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INDUCTION BY LIPOPOLYSACCHARIDE.
RX   PubMed=12032171;
RA   Kaplan R., Gan X., Menke J.G., Wright S.D., Cai T.-Q.;
RT   "Bacterial lipopolysaccharide induces expression of ABCA1 but not ABCG1 via
RT   an LXR-independent pathway.";
RL   J. Lipid Res. 43:952-959(2002).
RN   [6]
RP   DOWN-REGULATION BY ENDOTOXIN.
RX   PubMed=12777468; DOI=10.1194/jlr.m300100-jlr200;
RA   Khovidhunkit W., Moser A.H., Shigenaga J.K., Grunfeld C., Feingold K.R.;
RT   "Endotoxin down-regulates ABCG5 and ABCG8 in mouse liver and ABCA1 and
RT   ABCG1 in J774 murine macrophages: differential role of LXR.";
RL   J. Lipid Res. 44:1728-1736(2003).
RN   [7]
RP   INTERACTION WITH MEGF10.
RX   PubMed=17205124; DOI=10.1371/journal.pone.0000120;
RA   Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V.,
RA   Zhou Z., Chimini G.;
RT   "Cooperation between engulfment receptors: the case of ABCA1 and MEGF10.";
RL   PLoS ONE 1:E120-E120(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1296, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-489.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1296, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Spleen, and Testis;
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).
CC   -!- FUNCTION: Catalyzes the translocation of specific phospholipids from
CC       the cytoplasmic to the extracellular/lumenal leaflet of membrane
CC       coupled to the hydrolysis of ATP. Thereby, participates in phospholipid
CC       transfer to apolipoproteins to form nascent high density
CC       lipoproteins/HDLs. Transports preferentially phosphatidylcholine over
CC       phosphatidylserine. May play a similar role in the efflux of
CC       intracellular cholesterol to apolipoproteins and the formation of
CC       nascent high density lipoproteins/HDLs. Translocates phospholipids from
CC       the outer face of the plasma membrane and forces it through its gateway
CC       and annulus into an elongated hydrophobic tunnel in its extracellular
CC       domain. {ECO:0000250|UniProtKB:O95477}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC         phospholipidSide 2.; EC=7.6.2.1;
CC         Evidence={ECO:0000250|UniProtKB:O95477};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a
CC         1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O95477};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38585;
CC         Evidence={ECO:0000250|UniProtKB:O95477};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O =
CC         a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) +
CC         phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57262, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:O95477};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38569;
CC         Evidence={ECO:0000250|UniProtKB:O95477};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a sphingomyelin(in) + ATP + H2O = a sphingomyelin(out) + ADP +
CC         H(+) + phosphate; Xref=Rhea:RHEA:38903, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:O95477};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38904;
CC         Evidence={ECO:0000250|UniProtKB:O95477};
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:O95477};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC         Evidence={ECO:0000250|UniProtKB:O95477};
CC   -!- ACTIVITY REGULATION: ATPase activity is decreased by cholesterol and
CC       ceramide. ATPase activity is stimulated by phosphatidylcholine and to a
CC       lesser degree by phosphatidylserine and sphingomyelin. Phospholipid
CC       translocase activity is highly reduced by berylium fluoride and
CC       aluminum flouride and reduced by N-ethylmaleimide.
CC       {ECO:0000250|UniProtKB:O95477}.
CC   -!- SUBUNIT: Interacts with MEGF10 (PubMed:17205124). May interact with
CC       APOE1; functionally associated with APOE1 in the biogenesis of HDLs (By
CC       similarity). Interacts with ABCA8; this interaction potentiates
CC       cholesterol efflux (By similarity). Interacts with ABCA12 and NR1H2;
CC       this interaction is required for ABCA1 localization to the cell surface
CC       and is necessary for its normal activity and stability (By similarity).
CC       {ECO:0000250|UniProtKB:O95477, ECO:0000269|PubMed:17205124}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95477};
CC       Multi-pass membrane protein {ECO:0000255}. Endosome
CC       {ECO:0000250|UniProtKB:O95477}.
CC   -!- TISSUE SPECIFICITY: Widely expressed in adult tissues. Highest levels
CC       are found in pregnant uterus and uterus.
CC   -!- INDUCTION: Down-regulated by endotoxins (LPS) or cytokines (TNF and IL-
CC       1) in J774 macrophages. The down-regulation by endotoxin in macrophages
CC       is not likely to be mediated by the liver X receptor/retinoic X
CC       receptor (LXR/RXR). {ECO:0000269|PubMed:12032171}.
CC   -!- DOMAIN: Multifunctional polypeptide with two homologous halves, each
CC       containing a hydrophobic membrane-anchoring domain and an ATP binding
CC       cassette (ABC) domain.
CC   -!- PTM: Phosphorylation on Ser-2054 regulates phospholipid efflux.
CC       {ECO:0000250|UniProtKB:O95477}.
CC   -!- PTM: Palmitoylated by ZDHHC8. Palmitoylation is essential for
CC       localization to the plasma membrane. {ECO:0000250|UniProtKB:O95477}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG39073.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA53530.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X75926; CAA53530.1; ALT_INIT; mRNA.
DR   EMBL; AF287263; AAG39073.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL772397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL807243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466565; EDL02285.1; -; Genomic_DNA.
DR   CCDS; CCDS18187.1; -.
DR   PIR; A54774; A54774.
DR   RefSeq; NP_038482.3; NM_013454.3.
DR   AlphaFoldDB; P41233; -.
DR   SMR; P41233; -.
DR   BioGRID; 197900; 1.
DR   CORUM; P41233; -.
DR   IntAct; P41233; 2.
DR   STRING; 10090.ENSMUSP00000030010; -.
DR   BindingDB; P41233; -.
DR   ChEMBL; CHEMBL1641361; -.
DR   TCDB; 3.A.1.211.1; the atp-binding cassette (abc) superfamily.
DR   GlyConnect; 2139; 2 N-Linked glycans (1 site).
DR   GlyCosmos; P41233; 22 sites, 2 glycans.
DR   GlyGen; P41233; 22 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; P41233; -.
DR   PhosphoSitePlus; P41233; -.
DR   SwissPalm; P41233; -.
DR   jPOST; P41233; -.
DR   MaxQB; P41233; -.
DR   PaxDb; 10090-ENSMUSP00000030010; -.
DR   PeptideAtlas; P41233; -.
DR   ProteomicsDB; 285949; -.
DR   Antibodypedia; 14760; 654 antibodies from 38 providers.
DR   DNASU; 11303; -.
DR   Ensembl; ENSMUST00000030010.4; ENSMUSP00000030010.4; ENSMUSG00000015243.5.
DR   GeneID; 11303; -.
DR   KEGG; mmu:11303; -.
DR   UCSC; uc008swu.1; mouse.
DR   AGR; MGI:99607; -.
DR   CTD; 19; -.
DR   MGI; MGI:99607; Abca1.
DR   VEuPathDB; HostDB:ENSMUSG00000015243; -.
DR   eggNOG; KOG0059; Eukaryota.
DR   GeneTree; ENSGT00940000154658; -.
DR   HOGENOM; CLU_000604_19_0_1; -.
DR   InParanoid; P41233; -.
DR   OMA; FMWNVIA; -.
DR   OrthoDB; 6951at2759; -.
DR   PhylomeDB; P41233; -.
DR   TreeFam; TF105191; -.
DR   Reactome; R-MMU-8963896; HDL assembly.
DR   Reactome; R-MMU-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR   BioGRID-ORCS; 11303; 5 hits in 79 CRISPR screens.
DR   ChiTaRS; Abca1; mouse.
DR   PRO; PR:P41233; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; P41233; Protein.
DR   Bgee; ENSMUSG00000015243; Expressed in stroma of bone marrow and 256 other cell types or tissues.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:MGI.
DR   GO; GO:0097708; C:intracellular vesicle; ISO:MGI.
DR   GO; GO:0045121; C:membrane raft; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0045335; C:phagocytic vesicle; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0034186; F:apolipoprotein A-I binding; ISO:MGI.
DR   GO; GO:0034188; F:apolipoprotein A-I receptor activity; ISO:MGI.
DR   GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; ISO:MGI.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0120020; F:cholesterol transfer activity; IDA:MGI.
DR   GO; GO:0140328; F:floppase activity; ISS:UniProtKB.
DR   GO; GO:0008035; F:high-density lipoprotein particle binding; ISO:MGI.
DR   GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR   GO; GO:0090554; F:phosphatidylcholine floppase activity; ISS:UniProtKB.
DR   GO; GO:0090556; F:phosphatidylserine floppase activity; ISO:MGI.
DR   GO; GO:0005548; F:phospholipid transporter activity; IDA:MGI.
DR   GO; GO:0008320; F:protein transmembrane transporter activity; IMP:ARUK-UCL.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR   GO; GO:0046623; F:sphingolipid floppase activity; ISO:MGI.
DR   GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0071397; P:cellular response to cholesterol; IEA:Ensembl.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; IEA:Ensembl.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0033344; P:cholesterol efflux; IDA:MGI.
DR   GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
DR   GO; GO:0008203; P:cholesterol metabolic process; IDA:MGI.
DR   GO; GO:0030301; P:cholesterol transport; ISO:MGI.
DR   GO; GO:0016197; P:endosomal transport; ISO:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR   GO; GO:0140115; P:export across plasma membrane; IMP:ARUK-UCL.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0034380; P:high-density lipoprotein particle assembly; ISO:MGI.
DR   GO; GO:0032367; P:intracellular cholesterol transport; ISO:MGI.
DR   GO; GO:0042158; P:lipoprotein biosynthetic process; IMP:MGI.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IMP:MGI.
DR   GO; GO:0007040; P:lysosome organization; ISO:MGI.
DR   GO; GO:0002790; P:peptide secretion; IMP:MGI.
DR   GO; GO:0006911; P:phagocytosis, engulfment; IMP:MGI.
DR   GO; GO:0033700; P:phospholipid efflux; IDA:MGI.
DR   GO; GO:0055091; P:phospholipid homeostasis; ISO:MGI.
DR   GO; GO:0045332; P:phospholipid translocation; IMP:MGI.
DR   GO; GO:0015914; P:phospholipid transport; ISO:MGI.
DR   GO; GO:0060155; P:platelet dense granule organization; ISO:MGI.
DR   GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:BHF-UCL.
DR   GO; GO:0090108; P:positive regulation of high-density lipoprotein particle assembly; IMP:UniProtKB.
DR   GO; GO:0009306; P:protein secretion; IMP:ARUK-UCL.
DR   GO; GO:0071806; P:protein transmembrane transport; IMP:ARUK-UCL.
DR   GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISO:MGI.
DR   GO; GO:0034616; P:response to laminar fluid shear stress; ISO:MGI.
DR   GO; GO:0033552; P:response to vitamin B3; IEA:Ensembl.
DR   GO; GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL.
DR   GO; GO:0023061; P:signal release; IMP:ARUK-UCL.
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:SF34; PHOSPHOLIPID-TRANSPORTING ATPASE ABCA1; 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; P41233; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Disulfide bond; Endosome; Glycoprotein;
KW   Lipoprotein; Membrane; Nucleotide-binding; Palmitate; Phosphoprotein;
KW   Reference proteome; Repeat; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..2261
FT                   /note="Phospholipid-transporting ATPase ABCA1"
FT                   /id="PRO_0000093289"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..639
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        640..660
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        683..703
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        716..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        745..765
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        777..797
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        827..847
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        941..961
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1351..1371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1372..1656
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        1657..1677
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1703..1723
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1735..1755
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1768..1788
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1802..1822
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1852..1872
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          899..1131
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          1912..2144
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          69..80
FT                   /note="Annulus domain 1"
FT                   /evidence="ECO:0000250|UniProtKB:O95477"
FT   REGION          368..379
FT                   /note="Annulus domain 2"
FT                   /evidence="ECO:0000250|UniProtKB:O95477"
FT   REGION          564..594
FT                   /note="Gateway domain"
FT                   /evidence="ECO:0000250|UniProtKB:O95477"
FT   REGION          1285..1310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1285..1308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         933..940
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         1946..1953
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   MOD_RES         1042
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:O95477"
FT   MOD_RES         1296
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         2054
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:O95477"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           23
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           1110
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           1111
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        244
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        337
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        400
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        478
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        489
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        521
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        820
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1453
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1499
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1504
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1637
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2044
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        75..309
FT                   /evidence="ECO:0000250"
FT   DISULFID        1463..1477
FT                   /evidence="ECO:0000250"
FT   CONFLICT        1567..1568
FT                   /note="Missing (in Ref. 2; AAG39073)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1568
FT                   /note="S -> T (in Ref. 1; CAA53530)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2024
FT                   /note="V -> F (in Ref. 1; CAA53530)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2024
FT                   /note="Missing (in Ref. 2; AAG39073)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2261 AA;  253912 MW;  E041DA4FA73C2660 CRC64;
     MACWPQLRLL LWKNLTFRRR QTCQLLLEVA WPLFIFLILI SVRLSYPPYE QHECHFPNKA
     MPSAGTLPWV QGIICNANNP CFRYPTPGEA PGVVGNFNKS IVSRLFSDAQ RLLLYSQRDT
     SIKDMHKVLR MLRQIKHPNS NLKLQDFLVD NETFSGFLQH NLSLPRSTVD SLLQANVGLQ
     KVFLQGYQLH LASLCNGSKL EEIIQLGDAE VSALCGLPRK KLDAAERVLR YNMDILKPVV
     TKLNSTSHLP TQHLAEATTV LLDSLGGLAQ ELFSTKSWSD MRQEVMFLTN VNSSSSSTQI
     YQAVSRIVCG HPEGGGLKIK SLNWYEDNNY KALFGGNNTE EDVDTFYDNS TTPYCNDLMK
     NLESSPLSRI IWKALKPLLV GKILYTPDTP ATRQVMAEVN KTFQELAVFH DLEGMWEELS
     PQIWTFMENS QEMDLVRTLL DSRGNDQFWE QKLDGLDWTA QDIMAFLAKN PEDVQSPNGS
     VYTWREAFNE TNQAIQTISR FMECVNLNKL EPIPTEVRLI NKSMELLDER KFWAGIVFTG
     ITPDSVELPH HVKYKIRMDI DNVERTNKIK DGYWDPGPRA DPFEDMRYVW GGFAYLQDVV
     EQAIIRVLTG SEKKTGVYVQ QMPYPCYVDD IFLRVMSRSM PLFMTLAWIY SVAVIIKSIV
     YEKEARLKET MRIMGLDNGI LWFSWFVSSL IPLLVSAGLL VVILKLGNLL PYSDPSVVFV
     FLSVFAMVTI LQCFLISTLF SRANLAAACG GIIYFTLYLP YVLCVAWQDY VGFSIKIFAS
     LLSPVAFGFG CEYFALFEEQ GIGVQWDNLF ESPVEEDGFN LTTAVSMMLF DTFLYGVMTW
     YIEAVFPGQY GIPRPWYFPC TKSYWFGEEI DEKSHPGSSQ KGVSEICMEE EPTHLRLGVS
     IQNLVKVYRD GMKVAVDGLA LNFYEGQITS FLGHNGAGKT TTMSILTGLF PPTSGTAYIL
     GKDIRSEMSS IRQNLGVCPQ HNVLFDMLTV EEHIWFYARL KGLSEKHVKA EMEQMALDVG
     LPPSKLKSKT SQLSGGMQRK LSVALAFVGG SKVVILDEPT AGVDPYSRRG IWELLLKYRQ
     GRTIILSTHH MDEADILGDR IAIISHGKLC CVGSSLFLKN QLGTGYYLTL VKKDVESSLS
     SCRNSSSTVS CLKKEDSVSQ SSSDAGLGSD HESDTLTIDV SAISNLIRKH VSEARLVEDI
     GHELTYVLPY EAAKEGAFVE LFHEIDDRLS DLGISSYGIS ETTLEEIFLK VAEESGVDAE
     TSDGTLPARR NRRAFGDKQS CLHPFTEDDA VDPNDSDIDP ESRETDLLSG MDGKGSYQLK
     GWKLTQQQFV ALLWKRLLIA RRSRKGFFAQ IVLPAVFVCI ALVFSLIVPP FGKYPSLELQ
     PWMYNEQYTF VSNDAPEDMG TQELLNALTK DPGFGTRCME GNPIPDTPCL AGEEDWTISP
     VPQSIVDLFQ NGNWTMKNPS PACQCSSDKI KKMLPVCPPG AGGLPPPQRK QKTADILQNL
     TGRNISDYLV KTYVQIIAKS LKNKIWVNEF RYGGFSLGVS NSQALPPSHE VNDAIKQMKK
     LLKLTKDSSA DRFLSSLGRF MAGLDTKNNV KVWFNNKGWH AISSFLNVIN NAILRANLQK
     GENPSQYGIT AFNHPLNLTK QQLSEVALMT TSVDVLVSIC VIFAMSFVPA SFVVFLIQER
     VSKAKHLQFI SGVKPVIYWL SNFVWDMCNY VVPATLVIII FICFQQKSYV SSTNLPVLAL
     LLLLYGWSIT PLMYPASFVF KIPSTAYVVL TSVNLFIGIN GSVATFVLEL FTNNKLNDIN
     DILKSVFLIF PHFCLGRGLI DMVKNQAMAD ALERFGENRF VSPLSWDLVG RNLFAMAVEG
     VVFFLITVLI QYRFFIRPRP VKAKLPPLND EDEDVRRERQ RILDGGGQND ILEIKELTKI
     YRRKRKPAVD RICIGIPPGE CFGLLGVNGA GKSTTFKMLT GDTPVTRGDA FLNKNSILSN
     IHEVHQNMGY CPQFDAITEL LTGREHVEFF ALLRGVPEKE VGKVGEWAIR KLGLVKYGEK
     YASNYSGGNK RKLSTAMALI GGPPVVFLDE PTTGMDPKAR RFLWNCALSI VKEGRSVVLT
     SHSMEECEAL CTRMAIMVNG RFRCLGSVQH LKNRFGDGYT IVVRIAGSNP DLKPVQEFFG
     LAFPGSVLKE KHRNMLQYQL PSSLSSLARI FSILSQSKKR LHIEDYSVSQ TTLDQVFVNF
     AKDQSDDDHL KDLSLHKNQT VVDVAVLTSF LQDEKVKESY V
//