ABCA7_MOUSE
ID ABCA7_MOUSE Reviewed; 2159 AA.
AC Q91V24; Q9JL36;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ATP-binding cassette sub-family A member 7;
GN Name=Abca7;
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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=DBA/2J; TISSUE=Lymphoma;
RX PubMed=11435699; DOI=10.1159/000056914;
RA Broccardo C., Osorio J., Luciani M.-F., Schriml L.M., Prades C.,
RA Shulenin S., Arnould I., Naudin L., Lafargue C., Rosier M., Jordan B.,
RA Mattei M.-G., Dean M., Denefle P., Chimini G.;
RT "Comparative analysis of the promoter structure and genomic organization of
RT the human and mouse ABCA7 gene encoding a novel ABCA transporter.";
RL Cytogenet. Cell Genet. 92:264-270(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1920-2159.
RC STRAIN=C57BL/6J;
RX PubMed=10708515; DOI=10.1006/geno.1999.6102;
RA Schriml L.M., Dean M.;
RT "Identification of 18 mouse ABC genes and characterization of the ABC
RT superfamily in Mus musculus.";
RL Genomics 64:24-31(2000).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12917409; DOI=10.1074/jbc.m307831200;
RA Wang N., Lan D., Gerbod-Giannone M., Linsel-Nitschke P., Jehle A.W.,
RA Chen W., Martinez L.O., Tall A.R.;
RT "ATP-binding cassette transporter A7 (ABCA7) binds apolipoprotein A-I and
RT mediates cellular phospholipid but not cholesterol efflux.";
RL J. Biol. Chem. 278:42906-42912(2003).
RN [4]
RP INDUCTION.
RX PubMed=16445568; DOI=10.1111/j.1440-1681.2005.04301.x;
RA Wakaumi M., Ishibashi K., Ando H., Kasanuki H., Tsuruoka S.;
RT "Acute digoxin loading reduces ABCA8A mRNA expression in the mouse liver.";
RL Clin. Exp. Pharmacol. Physiol. 32:1034-1041(2005).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15550377; DOI=10.1074/jbc.m412602200;
RA Kim W.S., Fitzgerald M.L., Kang K., Okuhira K., Bell S.A., Manning J.J.,
RA Koehn S.L., Lu N., Moore K.J., Freeman M.W.;
RT "Abca7 null mice retain normal macrophage phosphatidylcholine and
RT cholesterol efflux activity despite alterations in adipose mass and serum
RT cholesterol levels.";
RL J. Biol. Chem. 280:3989-3995(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16908670; DOI=10.1083/jcb.200601030;
RA Jehle A.W., Gardai S.J., Li S., Linsel-Nitschke P., Morimoto K.,
RA Janssen W.J., Vandivier R.W., Wang N., Greenberg S., Dale B.M., Qin C.,
RA Henson P.M., Tall A.R.;
RT "ATP-binding cassette transporter A7 enhances phagocytosis of apoptotic
RT cells and associated ERK signaling in macrophages.";
RL J. Cell Biol. 174:547-556(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20495215; DOI=10.1194/jlr.m006049;
RA Tanaka N., Abe-Dohmae S., Iwamoto N., Fitzgerald M.L., Yokoyama S.;
RT "Helical apolipoproteins of high-density lipoprotein enhance phagocytosis
RT by stabilizing ATP-binding cassette transporter A7.";
RL J. Lipid Res. 51:2591-2599(2010).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=26260791; DOI=10.1074/jbc.m115.655076;
RA Satoh K., Abe-Dohmae S., Yokoyama S., St George-Hyslop P., Fraser P.E.;
RT "ATP-binding cassette transporter A7 (ABCA7) loss of function alters
RT Alzheimer amyloid processing.";
RL J. Biol. Chem. 290:24152-24165(2015).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=27472885; DOI=10.3233/jad-160456;
RA Fu Y., Hsiao J.H., Paxinos G., Halliday G.M., Kim W.S.;
RT "ABCA7 Mediates Phagocytic Clearance of Amyloid-beta in the Brain.";
RL J. Alzheimers Dis. 54:569-584(2016).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27030769; DOI=10.1523/jneurosci.3757-15.2016;
RA Sakae N., Liu C.C., Shinohara M., Frisch-Daiello J., Ma L., Yamazaki Y.,
RA Tachibana M., Younkin L., Kurti A., Carrasquillo M.M., Zou F., Sevlever D.,
RA Bisceglio G., Gan M., Fol R., Knight P., Wang M., Han X., Fryer J.D.,
RA Fitzgerald M.L., Ohyagi Y., Younkin S.G., Bu G., Kanekiyo T.;
RT "ABCA7 Deficiency Accelerates Amyloid-beta Generation and Alzheimer's
RT Neuronal Pathology.";
RL J. Neurosci. 36:3848-3859(2016).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28091533; DOI=10.1038/srep40273;
RA Nowyhed H.N., Chandra S., Kiosses W., Marcovecchio P., Andary F., Zhao M.,
RA Fitzgerald M.L., Kronenberg M., Hedrick C.C.;
RT "ATP Binding Cassette Transporter ABCA7 Regulates NKT Cell Development and
RT Function by Controlling CD1d Expression and Lipid Raft Content.";
RL Sci. Rep. 7:40273-40273(2017).
CC -!- FUNCTION: Probable ATP-binding cassette (ABC) transporter that plays a
CC role in lipid homeostasis and macrophage-mediated phagocytosis
CC (PubMed:12917409, PubMed:15550377, PubMed:16908670, PubMed:27472885,
CC PubMed:27030769, PubMed:20495215). Binds APOA1 and may function in
CC apolipoprotein-mediated phospholipid efflux from cells
CC (PubMed:12917409). May also mediate cholesterol efflux (By similarity).
CC May regulate cellular ceramide homeostasis during keratinocyte
CC differentiation (By similarity). Involved in lipid raft organization
CC and CD1D localization on thymocytes and antigen-presenting cells, which
CC plays an important role in natural killer T-cell development and
CC activation (PubMed:28091533). Plays a role in phagocytosis of apoptotic
CC cells by macrophages (PubMed:16908670). Macrophage phagocytosis is
CC stimulated by APOA1 or APOA2, probably by stabilization of ABCA7
CC (PubMed:20495215). Also involved in phagocytic clearance of amyloid-
CC beta by microglia cells and macrophages (PubMed:27472885). Further
CC limits amyloid-beta production by playing a role in the regulation of
CC amyloid-beta A4 precursor protein (APP) endocytosis and/or processing
CC (PubMed:26260791, PubMed:27030769). {ECO:0000250|UniProtKB:Q8IZY2,
CC ECO:0000269|PubMed:12917409, ECO:0000269|PubMed:15550377,
CC ECO:0000269|PubMed:16908670, ECO:0000269|PubMed:20495215,
CC ECO:0000269|PubMed:26260791, ECO:0000269|PubMed:27030769,
CC ECO:0000269|PubMed:27472885, ECO:0000269|PubMed:28091533}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12917409,
CC ECO:0000269|PubMed:20495215, ECO:0000269|PubMed:26260791}; Multi-pass
CC membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:16908670}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:16908670};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:27472885}. Cell projection, ruffle membrane
CC {ECO:0000269|PubMed:16908670}. Cell projection, phagocytic cup
CC {ECO:0000269|PubMed:16908670}. Note=Localizes to cell membrane ruffles
CC and phagocytic cups of macrophages stimulated with C1q or apoptotic
CC cells. Localizes to the cytoplasm of resting macrophages, probably in
CC Golgi and endosomes (PubMed:16908670). Localizes to the apical brush
CC border of cells in the proximal tubules of kidney (Probable).
CC {ECO:0000269|PubMed:16908670, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in brain,
CC lung, adrenal gland, spleen and hematopoietic tissues (at protein
CC level) (PubMed:12917409, PubMed:15550377, PubMed:27472885). In the
CC brain, expressed in cortex, cerebellum, hippocampus, olfactory bulb,
CC neurons, astrocytes and microglia (at protein level) (PubMed:26260791).
CC Also expressed in adipocytes and macrophages (at protein level)
CC (PubMed:15550377, PubMed:27472885). Expressed in thymocytes (at protein
CC level) (PubMed:28091533). Highly expressed in spleen and hematopoietic
CC tissues (PubMed:11435699). Expressed in brain, lung, macrophages,
CC microglia, oligodendrocytes and neurons (PubMed:27472885).
CC {ECO:0000269|PubMed:11435699, ECO:0000269|PubMed:12917409,
CC ECO:0000269|PubMed:15550377, ECO:0000269|PubMed:26260791,
CC ECO:0000269|PubMed:27472885, ECO:0000269|PubMed:28091533}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed during embryogenesis
CC (PubMed:11435699). Expressed in newborn mice with increasing expression
CC from 4 to 24 weeks of age (PubMed:26260791).
CC {ECO:0000269|PubMed:11435699, ECO:0000269|PubMed:26260791}.
CC -!- INDUCTION: Up-regulated during differentiation from monocytes to
CC macrophages (PubMed:27472885). Down-regulated by digoxin.
CC {ECO:0000269|PubMed:16445568, ECO:0000269|PubMed:27472885}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20495215}.
CC -!- DISRUPTION PHENOTYPE: According to one study, knockout mice are not
CC viable and heterozygous knockout mice display impaired phagocytosis of
CC apoptotic cells (PubMed:16908670). However, another study shows that
CC knockout mice are viable and females have less visceral fat and lower
CC total serum and high density lipoprotein cholesterol level
CC (PubMed:15550377). Knockout mice exhibit altered lipid profile in mouse
CC brains, compromised spatial memory and increased BACE1 activity
CC (PubMed:27030769). Display an increase in amyloid-beta protein 42
CC (Abeta42) from 4 to 24 weeks of age, whereas amyloid-beta protein 40
CC (Abeta40) is increased at 4 weeks and decreased at 24 weeks of age
CC (PubMed:26260791). Increased endocytotic uptake of APP into endosomes
CC in primary microglia cells (PubMed:26260791). Reduced phagocytic uptake
CC of Abeta42 and Abeta40 by microglia cells and phagocytes
CC (PubMed:27472885). Decreased macrophage phagocytosis in the peritoneal
CC cavity (PubMed:20495215). Decreased surface CD1D expression on double
CC positive thymocytes, on antigen-presenting thymocytes, on peripheral
CC antigen-presenting cells in the spleen and on peritoneal macrophages
CC (PubMed:28091533). Increased accumulation of CD1D to late endosomes
CC (PubMed:28091533). Impaired natural killer T (NKT) cell development
CC with a 2-fold decrease in frequencies and total numbers of NKT cells in
CC the thymus and a reduction of peripheral NKT cells in spleen and liver
CC (PubMed:28091533). Reduced proliferation during early stages of NKT
CC development and reduced expression of Egr2 in NKT cells
CC (PubMed:28091533). Decreased number of plasma membrane lipid rafts on
CC thymocytes and a reduction of CAV1 and CD1D clusters in macrophages
CC (PubMed:28091533). RNAi-mediated knockdown reduces phagocytosis of
CC apoptotic cells by macrophages (PubMed:16908670).
CC {ECO:0000269|PubMed:15550377, ECO:0000269|PubMed:16908670,
CC ECO:0000269|PubMed:20495215, ECO:0000269|PubMed:26260791,
CC ECO:0000269|PubMed:27030769, ECO:0000269|PubMed:27472885,
CC ECO:0000269|PubMed:28091533}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
CC -!- CAUTION: There are conflicting results concerning the role of ABCA7 in
CC lipid transport. ABCA7 was described to play a role in apolipoprotein-
CC mediated phospholipid and cholesterol efflux when expressed in HEK293
CC cells (PubMed:12917409, PubMed:27472885). However, another report shows
CC that ABCA7 deficiency does not influence cholesterol and phospholipid
CC efflux in mouse primary macrophages, but leads to lower serum HDL
CC cholesterol levels and a reduction in fat mass in female mice
CC (PubMed:15550377). {ECO:0000269|PubMed:12917409,
CC ECO:0000269|PubMed:15550377, ECO:0000269|PubMed:27472885}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF31434.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF287141; AAK56862.1; -; mRNA.
DR EMBL; AF287142; AAK56863.1; -; Genomic_DNA.
DR EMBL; AF213395; AAF31434.1; ALT_FRAME; mRNA.
DR CCDS; CCDS24004.1; -.
DR RefSeq; NP_038878.1; NM_013850.1.
DR RefSeq; XP_017169446.1; XM_017313957.1.
DR AlphaFoldDB; Q91V24; -.
DR SMR; Q91V24; -.
DR IntAct; Q91V24; 1.
DR STRING; 10090.ENSMUSP00000128121; -.
DR GlyConnect; 2142; 4 N-Linked glycans (2 sites).
DR GlyGen; Q91V24; 3 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q91V24; -.
DR PhosphoSitePlus; Q91V24; -.
DR SwissPalm; Q91V24; -.
DR EPD; Q91V24; -.
DR MaxQB; Q91V24; -.
DR PaxDb; Q91V24; -.
DR PRIDE; Q91V24; -.
DR ProteomicsDB; 285900; -.
DR Antibodypedia; 22516; 181 antibodies from 31 providers.
DR DNASU; 27403; -.
DR Ensembl; ENSMUST00000043866; ENSMUSP00000043090; ENSMUSG00000035722.
DR Ensembl; ENSMUST00000132517; ENSMUSP00000115111; ENSMUSG00000035722.
DR GeneID; 27403; -.
DR KEGG; mmu:27403; -.
DR UCSC; uc007gba.1; mouse.
DR CTD; 10347; -.
DR MGI; MGI:1351646; Abca7.
DR VEuPathDB; HostDB:ENSMUSG00000035722; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000161439; -.
DR HOGENOM; CLU_000604_19_0_1; -.
DR InParanoid; Q91V24; -.
DR Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
DR BioGRID-ORCS; 27403; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Abca7; mouse.
DR PRO; PR:Q91V24; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q91V24; protein.
DR Bgee; ENSMUSG00000035722; Expressed in granulocyte and 191 other tissues.
DR ExpressionAtlas; Q91V24; baseline and differential.
DR Genevisible; Q91V24; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097386; C:glial cell projection; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0016020; C:membrane; ISO:MGI.
DR GO; GO:0001891; C:phagocytic cup; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0005886; C:plasma membrane; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0032587; C:ruffle membrane; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0034188; F:apolipoprotein A-I receptor activity; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0140328; F:floppase activity; ISO:MGI.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0090554; F:phosphatidylcholine floppase activity; ISO:MGI.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; ISO:MGI.
DR GO; GO:0005548; F:phospholipid transporter activity; IDA:MGI.
DR GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; IMP:UniProtKB.
DR GO; GO:0034205; P:amyloid-beta formation; IMP:UniProtKB.
DR GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0033344; P:cholesterol efflux; IMP:UniProtKB.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0007613; P:memory; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0045806; P:negative regulation of endocytosis; IMP:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:ARUK-UCL.
DR GO; GO:1903898; P:negative regulation of PERK-mediated unfolded protein response; IMP:ARUK-UCL.
DR GO; GO:0018149; P:peptide cross-linking; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0033700; P:phospholipid efflux; IDA:MGI.
DR GO; GO:0045332; P:phospholipid translocation; ISO:MGI.
DR GO; GO:0044857; P:plasma membrane raft organization; IMP:UniProtKB.
DR GO; GO:1900223; P:positive regulation of amyloid-beta clearance; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:UniProtKB.
DR GO; GO:1902995; P:positive regulation of phospholipid efflux; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IMP:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IDA:Alzheimers_University_of_Toronto.
DR GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; ISO:MGI.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:ARUK-UCL.
DR GO; GO:0008542; P:visual learning; IMP:ARUK-UCL.
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; IPR030369; ABCA7.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR PANTHER; PTHR19229:SF49; PTHR19229:SF49; 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; Cell membrane; Cell projection; Cytoplasm; Disulfide bond;
KW Endosome; Glycoprotein; Golgi apparatus; Lipid transport; Membrane;
KW Nucleotide-binding; Phagocytosis; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..2159
FT /note="ATP-binding cassette sub-family A member 7"
FT /id="PRO_0000250675"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..546
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 678..698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 732..752
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 846..866
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1246..1266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1267..1551
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1552..1572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1598..1618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1635..1655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1663..1683
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1743..1763
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 804..1035
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1807..2039
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1042..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2118..2159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2118..2150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 838..845
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1841..1848
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..222
FT /evidence="ECO:0000250"
FT DISULFID 1359..1373
FT /evidence="ECO:0000250"
FT CONFLICT 1944
FT /note="N -> D (in Ref. 2; AAF31434)"
FT /evidence="ECO:0000305"
FT CONFLICT 2004
FT /note="A -> R (in Ref. 2; AAF31434)"
FT /evidence="ECO:0000305"
FT CONFLICT 2069
FT /note="L -> M (in Ref. 2; AAF31434)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2159 AA; 236884 MW; CD2BE3FE0D8B822B CRC64;
MALGTQLMLL LWKNYTYRRR QPIQLLVELL WPLFLFFILV AVRHSHPPLE HHECHFPNKP
LPSAGTVPWL QGLVCNVNNS CFQHPTPGEK PGVLSNFKDS LISRLLADTR TVLGGHSIQD
MLDALGKLIP VLRAVGGGAR PQESDQPTSQ GSVTKLLEKI LQRASLDPVL GQAQDSMRKF
SDAIRDLAQE LLTLPSLMEL RALLRRPRGS AGSLELVSEA LCSTKGPSSP GGLSLNWYEA
NQLNEFMGPE VAPALPDNSL SPACSEFVGT LDDHPVSRLL WRRLKPLILG KILFAPDTNF
TRKLMAQVNQ TFEELALLRD LHELWGVLGP QIFNFMNDST NVAMLQRLLD VGGTGQRQQT
PRAQKKLEAI KDFLDPSRGG YSWREAHADM GRLAGILGQM MECVSLDKLE AVPSEEALVS
RALELLGERR LWAGIVFLSP EHPLDPSELS SPALSPGHLR FKIRMDIDDV TRTNKIRDKF
WDPGPSADPF MDLRYVWGGF VYLQDLLEQA AVRVLGGGNS RTGLYLQQMP HPCYVDDVFL
RVLSRSLPLF LTLAWIYSVA LTVKAVVREK ETRLRETMRA MGLSRAVLWL GWFLSCLGPF
LVSAALLVLV LKLGNILPYS HPVVIFLFLA AFAVATVAQS FLLSAFFSRA NLAAACGGLA
YFALYLPYVL CVAWRERLHL GGLLAASLLS PVAFGFGCES LALLEEQGDG AQWHNLGTGP
AEDVFSLAQV SAFLLLDAVI YGLALWYLEA VCPGQYGIPE PWNFPFRRSY WCGPGPPKSS
VLAPAPQDPK VLVEEPPLGL VPGVSIRGLK KHFRGCPQPA LQGLNLDFYE GHITAFLGHN
GAGKTTTLSI LSGLFPPSSG SASILGHDVQ TNMAAIRPHL GICPQYNVLF DMLTVEEHVW
FYGRLKGVSA AAMGPERERL IRDVGLTLKR DTQTRHLSGG MQRKLSVAIA FVGGSRVVIM
DEPTAGVDPA SRRGIWELLL KYREGRTLIL STHHLDEAEL LGDRVAMVAG GSLCCCGSPL
FLRRHLGCGY YLTLVKSSQS LVTHDAKGDS EDPRREKKSD GNGRTSDTAF TRGTSDKSNQ
APAPGAVPIT PSTARILELV QQHVPGAQLV EDLPHELLLV LPYAGALDGS FAMVFQELDQ
QLELLGLTGY GISDTNLEEI FLKVVEDAHR EGGDSRPQLH LRTCTPQPPT GPEASVLENG
ELAPQGLAPN AAQVQGWTLT CQQLRALLHK RFLLARRSRR GLFAQVVLPA LFVGLALFFS
LIVPPFGQYP PLQLSPAMYG PQVSFFSEDA PGDPNRMKLL EALLGEAGLQ EPSMQDKDAR
GSECTHSLAC YFTVPEVPPD VASILASGNW TPESPSPACQ CSQPGARRLL PDCPAGAGGP
PPPQAVAGLG EVVQNLTGRN VSDFLVKTYP SLVRRGLKTK KWVDEVRYGG FSLGGRDPDL
PTGHEVVRTL AEIRALLSPQ PGNALDRILN NLTQWALGLD ARNSLKIWFN NKGWHAMVAF
VNRANNGLLH ALLPSGPVRH AHSITTLNHP LNLTKEQLSE ATLIASSVDV LVSICVVFAM
SFVPASFTLV LIEERITRAK HLQLVSGLPQ TLYWLGNFLW DMCNYLVAVC IVVFIFLAFQ
QRAYVAPENL PALLLLLLLY GWSITPLMYP ASFFFSVPST AYVVLTCINL FIGINSSMAT
FVLELLSDQN LQEVSRILKQ VFLIFPHFCL GRGLIDMVRN QAMADAFERL GDKQFQSPLR
WDIIGKNLLA MMAQGPLFLL ITLLLQHRNR LLPQSKPRLL PPLGEEDEDV AQERERVTKG
ATQGDVLVLR DLTKVYRGQR NPAVDRLCLG IPPGECFGLL GVNGAGKTST FRMVTGDTLP
SSGEAVLAGH NVAQERSAAH RSMGYCPQSD AIFDLLTGRE HLELFARLRG VPEAQVAQTA
LSGLVRLGLP SYADRPAGTY SGGNKRKLAT ALALVGDPAV VFLDEPTTGM DPSARRFLWN
SLLSVVREGR SVVLTSHSME ECEALCTRLA IMVNGRFRCL GSSQHLKGRF GAGHTLTLRV
PPDQPEPAIA FIRITFPGAE LREVHGSRLR FQLPPGGRCT LTRVFRELAA QGRAHGVEDF
SVSQTTLEEV FLYFSKDQGE EEESSRQEAE EEEVSKPGRQ HPKRVSRFLE DPSSVETMI
