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Phosphatidylcholine translocator ABCB4 (ATP-binding cassette sub-family B member 4) (Multidrug resistance protein 2) (Multidrug resistance protein 3) (EC 3.6.3.44) (P-glycoprotein 2) (P-glycoprotein 3)

 MDR3_MOUSE              Reviewed;        1276 AA.
P21440; B9EK77; Q6LCL9;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 2.
20-JUN-2018, entry version 151.
RecName: Full=Phosphatidylcholine translocator ABCB4 {ECO:0000305};
AltName: Full=ATP-binding cassette sub-family B member 4 {ECO:0000312|MGI:MGI:97569};
AltName: Full=Multidrug resistance protein 2 {ECO:0000303|PubMed:3405218};
AltName: Full=Multidrug resistance protein 3 {ECO:0000250|UniProtKB:P21439};
EC=3.6.3.44;
AltName: Full=P-glycoprotein 2 {ECO:0000250|UniProtKB:Q08201};
AltName: Full=P-glycoprotein 3 {ECO:0000250|UniProtKB:Q08201};
Name=Abcb4 {ECO:0000312|MGI:MGI:97569};
Synonyms=Mdr2 {ECO:0000303|PubMed:3405218}, Pgy-2,
Pgy2 {ECO:0000250|UniProtKB:Q08201};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3405218; DOI=10.1128/MCB.8.7.2770;
Gros P., Raymond M., Bell J., Housman D.;
"Cloning and characterization of a second member of the mouse mdr gene
family.";
Mol. Cell. Biol. 8:2770-2778(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
STRAIN=BALB/cJ;
Kirschner L.S., Horwitz S.B.;
"5'-end analysis of the murine mdr2 mRNA reveals complex and tissue-
specific processing.";
Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-92.
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=8759018; DOI=10.1093/nar/24.14.2829;
Kirschner L.S.;
"De novo generation of simple sequence during gene amplification.";
Nucleic Acids Res. 24:2829-2834(1996).
[6]
TISSUE SPECIFICITY.
PubMed=2471060; DOI=10.1128/MCB.9.3.1346;
Croop J.M., Raymond M., Haber D., Devault A., Arceci R.J., Gros P.,
Housman D.E.;
"The three mouse multidrug resistance (mdr) genes are expressed in a
tissue-specific manner in normal mouse tissues.";
Mol. Cell. Biol. 9:1346-1350(1989).
[7]
TISSUE SPECIFICITY.
PubMed=1969609; DOI=10.1128/MCB.10.4.1642;
Raymond M., Rose E., Housman D.E., Gros P.;
"Physical mapping, amplification, and overexpression of the mouse mdr
gene family in multidrug-resistant cells.";
Mol. Cell. Biol. 10:1642-1651(1990).
[8]
ABSENCE OF FUNCTION.
PubMed=1990275; DOI=10.1128/MCB.11.2.595;
Buschman E., Gros P.;
"Functional analysis of chimeric genes obtained by exchanging
homologous domains of the mouse mdr1 and mdr2 genes.";
Mol. Cell. Biol. 11:595-603(1991).
[9]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=1381362;
Buschman E., Arceci R.J., Croop J.M., Che M., Arias I.M.,
Housman D.E., Gros P.;
"mdr2 encodes P-glycoprotein expressed in the bile canalicular
membrane as determined by isoform-specific antibodies.";
J. Biol. Chem. 267:18093-18099(1992).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=8106172; DOI=10.1016/0092-8674(93)90380-9;
Smit J.J., Schinkel A.H., Oude Elferink R.P., Groen A.K., Wagenaar E.,
van Deemter L., Mol C.A., Ottenhoff R., van der Lugt N.M.,
van Roon M.A.;
"Homozygous disruption of the murine mdr2 P-glycoprotein gene leads to
a complete absence of phospholipid from bile and to liver disease.";
Cell 75:451-462(1993).
[11]
FUNCTION, AND ENZYME REGULATION.
PubMed=7912658; DOI=10.1016/0092-8674(94)90446-4;
Ruetz S., Gros P.;
"Phosphatidylcholine translocase: a physiological role for the mdr2
gene.";
Cell 77:1071-1081(1994).
[12]
FUNCTION, AND ENZYME REGULATION.
PubMed=7592705; DOI=10.1074/jbc.270.43.25388;
Ruetz S., Gros P.;
"Enhancement of Mdr2-mediated phosphatidylcholine translocation by the
bile salt taurocholate. Implications for hepatic bile formation.";
J. Biol. Chem. 270:25388-25395(1995).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=7814632; DOI=10.1172/JCI117658;
Oude Elferink R.P., Ottenhoff R., van Wijland M., Smit J.J.,
Schinkel A.H., Groen A.K.;
"Regulation of biliary lipid secretion by mdr2 P-glycoprotein in the
mouse.";
J. Clin. Invest. 95:31-38(1995).
[14]
SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=8615769; DOI=10.1042/bj3140781;
Chianale J., Vollrath V., Wielandt A.M., Amigo L., Rigotti A.,
Nervi F., Gonzalez S., Andrade L., Pizarro M., Accatino L.;
"Fibrates induce mdr2 gene expression and biliary phospholipid
secretion in the mouse.";
Biochem. J. 314:781-786(1996).
[15]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8725158;
Oude Elferink R.P., Ottenhoff R., van Wijland M., Frijters C.M.,
van Nieuwkerk C., Groen A.K.;
"Uncoupling of biliary phospholipid and cholesterol secretion in mice
with reduced expression of mdr2 P-glycoprotein.";
J. Lipid Res. 37:1065-1075(1996).
[16]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9366571; DOI=10.1172/JCI119799;
Crawford A.R., Smith A.J., Hatch V.C., Oude Elferink R.P., Borst P.,
Crawford J.M.;
"Hepatic secretion of phospholipid vesicles in the mouse critically
depends on mdr2 or MDR3 P-glycoprotein expression. Visualization by
electron microscopy.";
J. Clin. Invest. 100:2562-2567(1997).
[17]
INDUCTION.
PubMed=12381268; DOI=10.1042/BJ20020981;
Kok T., Bloks V.W., Wolters H., Havinga R., Jansen P.L., Staels B.,
Kuipers F.;
"Peroxisome proliferator-activated receptor alpha (PPARalpha)-mediated
regulation of multidrug resistance 2 (Mdr2) expression and function in
mice.";
Biochem. J. 369:539-547(2003).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[19]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21820390; DOI=10.1053/j.gastro.2011.07.042;
Groen A., Romero M.R., Kunne C., Hoosdally S.J., Dixon P.H.,
Wooding C., Williamson C., Seppen J., Van den Oever K., Mok K.S.,
Paulusma C.C., Linton K.J., Oude Elferink R.P.;
"Complementary functions of the flippase ATP8B1 and the floppase ABCB4
in maintaining canalicular membrane integrity.";
Gastroenterology 141:1927-1937(2011).
[20]
SUBCELLULAR LOCATION.
PubMed=23468132; DOI=10.1194/jlr.M032425;
Morita S.Y., Tsuda T., Horikami M., Teraoka R., Kitagawa S.,
Terada T.;
"Bile salt-stimulated phospholipid efflux mediated by ABCB4 localized
in nonraft membranes.";
J. Lipid Res. 54:1221-1230(2013).
-!- FUNCTION: Energy-dependent phospholipid efflux translocator that
acts as a positive regulator of biliary lipid secretion. Functions
as a floppase that translocates specifically phosphatidylcholine
(PC) from the inner to the outer leaflet of the canalicular
membrane bilayer into the canaliculi between hepatocytes.
Translocation of PC makes the biliary phospholipids available for
extraction into the canaliculi lumen by bile salt mixed micelles
and therefore protects the biliary tree from the detergent
activity of bile salts (PubMed:8106172, PubMed:7912658,
PubMed:7592705, PubMed:7814632, PubMed:8725158, PubMed:9366571).
Plays a role in the recruitment of phosphatidylcholine (PC),
phosphatidylethanolamine (PE) and sphingomyelin (SM) molecules to
nonraft membranes and to further enrichment of SM and cholesterol
in raft membranes in hepatocytes (By similarity). Required for
proper phospholipid bile formation (PubMed:8106172). Indirectly
involved in cholesterol efflux activity from hepatocytes into the
canalicular lumen in the presence of bile salts in an ATP-
dependent manner (PubMed:7814632, PubMed:8725158). May promote
biliary phospholipid secretion as canaliculi-containing vesicles
from the canalicular plasma membrane (PubMed:9366571). In
cooperation with ATP8B1, functions to protect hepatocytes from the
deleterious detergent activity of bile salts (PubMed:21820390).
Does not confer multidrug resistance (PubMed:1990275).
{ECO:0000250|UniProtKB:P21439, ECO:0000269|PubMed:1990275,
ECO:0000269|PubMed:21820390, ECO:0000269|PubMed:7592705,
ECO:0000269|PubMed:7814632, ECO:0000269|PubMed:7912658,
ECO:0000269|PubMed:8106172, ECO:0000269|PubMed:8725158,
ECO:0000269|PubMed:9366571}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + xenobiotic(In) = ADP + phosphate
+ xenobiotic(Out).
-!- ENZYME REGULATION: Translocation activity is inhibited by the
ATPase inhibitor vanadate and the calcium channel blocker
verapamil (PubMed:7912658). Translocation activity is enhanced by
the addition of the bile salt taurocholate (PubMed:7592705).
{ECO:0000269|PubMed:7592705, ECO:0000269|PubMed:7912658}.
-!- SUBUNIT: May interact with RACK1. Interacts with HAX1.
{ECO:0000250|UniProtKB:P21439, ECO:0000250|UniProtKB:Q08201}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23468132,
ECO:0000269|PubMed:8106172, ECO:0000269|PubMed:8615769}; Multi-
pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Apical cell membrane {ECO:0000269|PubMed:1381362}; Multi-pass
membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. Membrane
raft {ECO:0000250|UniProtKB:P21439}. Cytoplasm
{ECO:0000250|UniProtKB:P21439}. Cytoplasmic vesicle, clathrin-
coated vesicle {ECO:0000250|UniProtKB:Q08201}. Note=Transported
from the Golgi to the apical bile canalicular membrane in a RACK1-
dependent manner. Redistributed into pseudocanaliculi formed
between cells in a bezafibrate- or PPARA-dependent manner (By
similarity). Localized at the apical canalicular membrane of the
epithelial cells lining the lumen of the bile canaliculi and
biliary ductules (PubMed:1381362, PubMed:8106172, PubMed:8615769).
Localized preferentially in lipid nonraft domains of canalicular
plasma membranes (PubMed:23468132). {ECO:0000250|UniProtKB:P21439,
ECO:0000269|PubMed:1381362, ECO:0000269|PubMed:23468132,
ECO:0000269|PubMed:8106172, ECO:0000269|PubMed:8615769}.
-!- TISSUE SPECIFICITY: Expressed in the liver (PubMed:1381362,
PubMed:8615769) (at protein level). Expressed in adrenal, liver,
muscle, spleen and heart (PubMed:2471060). Expressed in multidrug-
resistant cell lines (PubMed:1969609).
{ECO:0000269|PubMed:1381362, ECO:0000269|PubMed:1969609,
ECO:0000269|PubMed:2471060, ECO:0000269|PubMed:8615769}.
-!- INDUCTION: Up-regulated by compounds that cause peroxisome
proliferation, such as ciprofibrate and clofibrate (at protein
level) (PubMed:8615769). Up-regulated by compounds that cause
peroxisome proliferation, such as fenofibrate, ciprofibrate,
clofibrate, bezafibrate and gemfibrozil (PubMed:8615769,
PubMed:12381268). {ECO:0000269|PubMed:12381268,
ECO:0000269|PubMed:8615769}.
-!- PTM: Phosphorylated. Phosphorylation is required for PC efflux
activity. Phosphorylation occurs on serine and threonine residues
in a protein kinase A- or C-dependent manner. May be
phosphorylated on Thr-41 and Ser-46.
{ECO:0000250|UniProtKB:P21439}.
-!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P21439}.
-!- DISRUPTION PHENOTYPE: Mice show severe necrotic damage of
hepatocytes, strong portal inflammation, proliferation and
destruction of the canalicular and small bile ductular tracts
(PubMed:8106172). Display almost complete reduction of biliary
phospholipid secretion, although bile salt secretion is normal
(PubMed:8106172, PubMed:7814632, PubMed:8725158, PubMed:9366571).
Show also reduced cholesterol secretion (PubMed:8106172,
PubMed:9366571). Knockout mice lacking both ABCB4 and ATP8B1 show
lower hepatic damage compared with the single ABCB4 knockout mice
(PubMed:21820390). Display equivalent reduction of biliary
phosphatidylcholine (PC) secretion as the single ABCB4 knockout
mice (PubMed:21820390). Biliary cholesterol secretion is higher
compared to the single ABCB4 knockout mice (PubMed:21820390). Bile
salt secretion is normal in both single ABCB4 knockout mice and
double ABCB4 and ATP8B1 knockout mice (PubMed:21820390). Biliary
excretion of canalicular ectoenzymes, aminopeptidase N and
alkaline phosphatase is strongly reduced compared to single ATP8B1
knockout mice (PubMed:21820390). {ECO:0000269|PubMed:21820390,
ECO:0000269|PubMed:7814632, ECO:0000269|PubMed:8106172,
ECO:0000269|PubMed:8725158, ECO:0000269|PubMed:9366571}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB
family. Multidrug resistance exporter (TC 3.A.1.201) subfamily.
{ECO:0000305}.
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EMBL; J03398; AAA39516.1; -; mRNA.
EMBL; CH466600; EDL14681.1; -; Genomic_DNA.
EMBL; BC150687; AAI50688.1; -; mRNA.
EMBL; M74151; AAA39515.1; -; Genomic_DNA.
EMBL; U46839; AAC52722.1; -; Genomic_DNA.
CCDS; CCDS19086.1; -.
PIR; A30409; DVMS2.
RefSeq; NP_032856.2; NM_008830.2.
UniGene; Mm.297825; -.
ProteinModelPortal; P21440; -.
SMR; P21440; -.
STRING; 10090.ENSMUSP00000003717; -.
SwissLipids; SLP:000000362; -.
iPTMnet; P21440; -.
PhosphoSitePlus; P21440; -.
MaxQB; P21440; -.
PaxDb; P21440; -.
PeptideAtlas; P21440; -.
PRIDE; P21440; -.
Ensembl; ENSMUST00000003717; ENSMUSP00000003717; ENSMUSG00000042476.
GeneID; 18670; -.
KEGG; mmu:18670; -.
UCSC; uc008wkr.2; mouse.
CTD; 5244; -.
MGI; MGI:97569; Abcb4.
eggNOG; KOG0055; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00530000062896; -.
HOVERGEN; HBG080809; -.
InParanoid; P21440; -.
KO; K05659; -.
OMA; FAVQWKL; -.
OrthoDB; EOG091G0HVA; -.
TreeFam; TF105193; -.
Reactome; R-MMU-382556; ABC-family proteins mediated transport.
PRO; PR:P21440; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000042476; -.
ExpressionAtlas; P21440; baseline and differential.
Genevisible; P21440; MM.
GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0046581; C:intercellular canaliculus; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; ISS:UniProtKB.
GO; GO:0008525; F:phosphatidylcholine transporter activity; ISS:UniProtKB.
GO; GO:0090554; F:phosphatidylcholine-translocating ATPase activity; ISS:UniProtKB.
GO; GO:0032782; P:bile acid secretion; IMP:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0033231; P:carbohydrate export; IEA:Ensembl.
GO; GO:0071475; P:cellular hyperosmotic salinity response; IEA:Ensembl.
GO; GO:0071312; P:cellular response to alkaloid; IEA:Ensembl.
GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl.
GO; GO:1903413; P:cellular response to bile acid; ISS:UniProtKB.
GO; GO:1905231; P:cellular response to borneol; IEA:Ensembl.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
GO; GO:0071217; P:cellular response to external biotic stimulus; IEA:Ensembl.
GO; GO:1905232; P:cellular response to L-glutamate; IEA:Ensembl.
GO; GO:0036146; P:cellular response to mycotoxin; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0043215; P:daunorubicin transport; IEA:Ensembl.
GO; GO:0046618; P:drug export; IEA:Ensembl.
GO; GO:1990962; P:drug transport across blood-brain barrier; IEA:Ensembl.
GO; GO:0060856; P:establishment of blood-brain barrier; IEA:Ensembl.
GO; GO:1990963; P:establishment of blood-retinal barrier; IEA:Ensembl.
GO; GO:0009914; P:hormone transport; IEA:Ensembl.
GO; GO:0050892; P:intestinal absorption; IEA:Ensembl.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
GO; GO:0035633; P:maintenance of permeability of blood-brain barrier; IEA:Ensembl.
GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
GO; GO:0045332; P:phospholipid translocation; ISO:MGI.
GO; GO:0001890; P:placenta development; IEA:Ensembl.
GO; GO:0032376; P:positive regulation of cholesterol transport; ISS:UniProtKB.
GO; GO:0061092; P:positive regulation of phospholipid translocation; ISS:UniProtKB.
GO; GO:2001140; P:positive regulation of phospholipid transport; ISS:UniProtKB.
GO; GO:2001025; P:positive regulation of response to drug; IEA:Ensembl.
GO; GO:1904478; P:regulation of intestinal absorption; IEA:Ensembl.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:1905233; P:response to codeine; IEA:Ensembl.
GO; GO:1905237; P:response to cyclosporin A; IEA:Ensembl.
GO; GO:1901557; P:response to fenofibrate; IDA:UniProtKB.
GO; GO:0033762; P:response to glucagon; IEA:Ensembl.
GO; GO:1903416; P:response to glycoside; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
GO; GO:1905235; P:response to quercetin; IEA:Ensembl.
GO; GO:0097068; P:response to thyroxine; IEA:Ensembl.
GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR030275; MDR3.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24221:SF241; PTHR24221:SF241; 2.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Glycoprotein; Hydrolase; Lipid transport;
Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1276 Phosphatidylcholine translocator ABCB4.
/FTId=PRO_0000093337.
TOPO_DOM 1 47 Cytoplasmic. {ECO:0000250}.
TRANSMEM 48 70 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 71 115 Extracellular. {ECO:0000250}.
TRANSMEM 116 136 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 137 185 Cytoplasmic. {ECO:0000250}.
TRANSMEM 186 207 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 208 212 Extracellular. {ECO:0000250}.
TRANSMEM 213 235 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 236 293 Cytoplasmic. {ECO:0000250}.
TRANSMEM 294 315 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 316 329 Extracellular. {ECO:0000250}.
TRANSMEM 330 351 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 352 708 Cytoplasmic. {ECO:0000250}.
TRANSMEM 709 729 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 730 752 Extracellular. {ECO:0000250}.
TRANSMEM 753 773 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 774 828 Cytoplasmic. {ECO:0000250}.
TRANSMEM 829 849 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 850 850 Extracellular. {ECO:0000250}.
TRANSMEM 851 870 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 871 930 Cytoplasmic. {ECO:0000250}.
TRANSMEM 931 953 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 954 969 Extracellular. {ECO:0000250}.
TRANSMEM 970 991 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 992 1276 Cytoplasmic. {ECO:0000250}.
DOMAIN 54 356 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 391 627 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 708 996 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1031 1269 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 426 433 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1066 1073 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 622 646 Interaction with HAX1. {ECO:0000250}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 257 257 L -> P (in Ref. 1; AAA39516).
{ECO:0000305}.
CONFLICT 828 828 R -> K (in Ref. 1; AAA39516).
{ECO:0000305}.
SEQUENCE 1276 AA; 140377 MW; 30BC72EDDFA4388C CRC64;
MDLEAARNGT ARRLDGDFEL GSISNQGREK KKKVNLIGLL TLFRYSDWQD KLFMFLGTLM
AIAHGSGLPL MMIVFGEMTD KFVDNTGNFS LPVNFSLSML NPGRILEEEM TRYAYYYSGL
GGGVLVAAYI QVSFWTLAAG RQIKKIRQKF FHAILRQEMG WFDIKGTTEL NTRLTDDVSK
ISEGIGDKVG MFFQAIATFF AGFIVGFIRG WKLTLVIMAI SPILGLSTAV WAKILSTFSD
KELAAYAKAG AVAEEALGAI RTVIAFGGQN KELERYQKHL ENAKKIGIKK AISANISMGI
AFLLIYASYA LAFWYGSTLV ISKEYTIGNA MTVFFSILIG AFSVGQAAPC IDAFANARGA
AYVIFDIIDN NPKIDSFSER GHKPDNIKGN LEFSDVHFSY PSRANIKILK GLNLKVKSGQ
TVALVGNSGC GKSTTVQLLQ RLYDPTEGKI SIDGQDIRNF NVRCLREIIG VVSQEPVLFS
TTIAENIRYG RGNVTMDEIE KAVKEANAYD FIMKLPQKFD TLVGDRGAQL SGGQKQRIAI
ARALVRNPKI LLLDEATSAL DTESEAEVQA ALDKAREGRT TIVIAHRLST IRNADVIAGF
EDGVIVEQGS HSELMKKEGI YFRLVNMQTA GSQILSEEFE VELSDEKAAG DVAPNGWKAR
IFRNSTKKSL KSPHQNRLDE ETNELDANVP PVSFLKVLKL NKTEWPYFVV GTVCAIANGA
LQPAFSIILS EMIAIFGPGD DAVKQQKCNM FSLVFLGLGV LSFFTFFLQG FTFGKAGEIL
TTRLRSMAFK AMLRQDMSWF DDHKNSTGAL STRLATDAAQ VQGATGTRLA LIAQNTANLG
TGIIISFIYG WQLTLLLLSV VPFIAVAGIV EMKMLAGNAK RDKKEMEAAG KIATEAIENI
RTVVSLTQER KFESMYVEKL HGPYRNSVRK AHIYGITFSI SQAFMYFSYA GCFRFGSYLI
VNGHMRFKDV ILVFSAIVLG AVALGHASSF APDYAKAKLS AAYLFSLFER QPLIDSYSGE
GLWPDKFEGS VTFNEVVFNY PTRANVPVLQ GLSLEVKKGQ TLALVGSSGC GKSTVVQLLE
RFYDPMAGSV LLDGQEAKKL NVQWLRAQLG IVSQEPILFD CSIAENIAYG DNSRVVPHDE
IVRAAKEANI HPFIETLPQK YNTRVGDKGT QLSGGQKQRI AIARALIRQP RVLLLDEATS
ALDTESEKVV QEALDKAREG RTCIVIAHRL STIQNADLIV VIENGKVKEH GTHQQLLAQK
GIYFSMVNIQ AGTQNL


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