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

 MDR3_CRIGR              Reviewed;        1281 AA.
P23174;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 1.
05-DEC-2018, entry version 111.
RecName: Full=Phosphatidylcholine translocator ABCB4;
AltName: Full=ATP-binding cassette sub-family B member 4;
AltName: Full=Multidrug resistance protein 3 {ECO:0000250|UniProtKB:P21439};
EC=7.6.2.2;
AltName: Full=P-glycoprotein 3 {ECO:0000250|UniProtKB:Q08201};
Name=ABCB4; Synonyms=PGP3 {ECO:0000250|UniProtKB:Q08201}, PGY3;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1685679; DOI=10.3109/10425179109039677;
Endicott J.A., Sarangi F., Ling V.;
"Complete cDNA sequences encoding the Chinese hamster P-glycoprotein
gene family.";
DNA Seq. 2:89-101(1991).
-!- 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 of 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. 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. Required for proper
phospholipid bile formation. Indirectly involved in cholesterol
efflux activity from hepatocytes into the canalicular lumen in the
presence of bile salts in an ATP-dependent manner. May promote
biliary phospholipid secretion as canaliculi-containing vesicles
from the canalicular plasma membrane. In cooperation with ATP8B1,
functions to protect hepatocytes from the deleterious detergent
activity of bile salts. Does not confer multidrug resistance.
{ECO:0000250|UniProtKB:P21439, ECO:0000250|UniProtKB:P21440}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H(2)O + xenobiotic(Side 1) = ADP + phosphate +
xenobiotic(Side 2).; EC=7.6.2.2;
-!- ACTIVITY REGULATION: Translocation activity is inhibited by the
ATPase inhibitor vanadate and the calcium channel blocker
verapamil. Translocation activity is enhanced by the addition of
the bile salt taurocholate. {ECO:0000250|UniProtKB:P21439}.
-!- SUBUNIT: Interacts with HAX1. May interact with RACK1.
{ECO:0000250|UniProtKB:P21439, ECO:0000250|UniProtKB:Q08201}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P21439}; Multi-pass membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00441}. Apical cell membrane
{ECO:0000250|UniProtKB:P21439}; 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=Localized at
the apical canalicular membrane of the epithelial cells lining the
lumen of the bile canaliculi and biliary ductules. Localized
preferentially in lipid nonraft domains of canalicular plasma
membranes. 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. {ECO:0000250|UniProtKB:P21439,
ECO:0000250|UniProtKB:P21440}.
-!- 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-44 and Ser-49.
{ECO:0000250|UniProtKB:P21439}.
-!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P21439}.
-!- 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; M60042; AAA68885.1; -; mRNA.
PIR; I48120; I48120.
PIR; I48123; I48123.
RefSeq; NP_001230916.1; NM_001243987.1.
ProteinModelPortal; P23174; -.
SMR; P23174; -.
PRIDE; P23174; -.
GeneID; 100682535; -.
KEGG; cge:100682535; -.
CTD; 5244; -.
HOVERGEN; HBG080809; -.
KO; K05659; -.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISS: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; ISS:UniProtKB.
GO; GO:1903413; P:cellular response to bile acid; ISS:UniProtKB.
GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
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:1901557; P:response to fenofibrate; ISS:UniProtKB.
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.
InterPro; IPR039421; Type_I_exporter.
PANTHER; PTHR24221; PTHR24221; 1.
PANTHER; PTHR24221:SF241; PTHR24221:SF241; 1.
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; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
2: Evidence at transcript level;
ATP-binding; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
Glycoprotein; Lipid transport; Membrane; Nucleotide-binding;
Phosphoprotein; Repeat; Translocase; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 1281 Phosphatidylcholine translocator ABCB4.
/FTId=PRO_0000093341.
TOPO_DOM 1 50 Cytoplasmic. {ECO:0000250}.
TRANSMEM 51 73 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 74 118 Extracellular. {ECO:0000250}.
TRANSMEM 119 139 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 140 188 Cytoplasmic. {ECO:0000250}.
TRANSMEM 189 210 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 211 217 Extracellular. {ECO:0000250}.
TRANSMEM 218 238 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 239 296 Cytoplasmic. {ECO:0000250}.
TRANSMEM 297 318 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 319 332 Extracellular. {ECO:0000250}.
TRANSMEM 333 354 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 355 713 Cytoplasmic. {ECO:0000250}.
TRANSMEM 714 734 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 735 757 Extracellular. {ECO:0000250}.
TRANSMEM 758 778 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 779 833 Cytoplasmic. {ECO:0000250}.
TRANSMEM 834 854 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 855 855 Extracellular. {ECO:0000250}.
TRANSMEM 856 875 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 876 937 Cytoplasmic. {ECO:0000250}.
TRANSMEM 938 958 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 959 974 Extracellular. {ECO:0000250}.
TRANSMEM 975 996 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 997 1281 Cytoplasmic. {ECO:0000250}.
DOMAIN 57 359 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 394 630 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 713 1001 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1036 1274 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 429 436 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1071 1078 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 625 649 Interaction with HAX1. {ECO:0000250}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000250|UniProtKB:P21440}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 1281 AA; 140866 MW; 2203EF61EBB29602 CRC64;
MDLEAARNGT ARRPGTVEGD FELGSISNQG RNKKKKVNLI GPLTLFRYSD WQDKLFMLLG
TIMAIAHGSG LPLMMIVFGE MTDKFVNNAG NFSLPVNFSL SMINPGRILE EEMTRYAYYY
SGLGGGVLVA AYIQVSFWTL AAGRQIKKIR QNFFHAILRQ EMGWFDIKGT TELNTRLTDD
ISKISEGIGD KVGMFFQAVA TFFAGFIVGF IRGWKLTLVI MAISPILGLS AAVWAKILST
FSDKELAAYA KAGAVAEEAL GAIRTVIAFG GQNKELERYQ KHLENAKKIG IKKAISANIS
MGIAFLLIYA SYALAFWYGS TLVISKEYTI GNAMTVFFSI LIGAFSVGQA APCIDAFANA
RGAAYVIFDI IDNNPKIDSF SERGHKPDSI KGNLDFSDVH FSYPSRANIK ILKGLNLKVQ
SGQTVALVGN SGCGKTTTLQ LLQRLYDPTE GTISIDGQDI RNFNVRYLRE IIGVVSQEPV
LFSTTIAENI RYGRGNVTME EIKKAVKEAN AYEFIMKLPQ KFDTLVGERG AQLSGGQKQR
IAIARALVRN PKILLLDEAT SALDTESEAE VQAALDKARE GRTTIVIAHR LSTVRNADVI
AGFEDGVIVE QGSHSELMQK EGVYFKLVNM QTSGSQILSQ EFEVELSEEK AADGMTPNGW
KSHIFRNSTK KSLKSSRAHH HRLDVDADEL DANVPPVSFL KVLKLNKTEW PYFVVGTVCA
IVNGALQPAI SIILSEMIAI FGPGDDAVKQ QKCNLFSLVF LGLGVLSFFT FFLQGFTFGK
AGEILTTRLR SMAFKAMLRQ DMSWFDDYKN STGALSTRLA TDRAQVQGAT GTRLALIAQN
TANLGTGIII SFIYGWQLTL LLLSVVPFIA VSGIVEMKML AGNAKRDKKA LEAAGKIATE
AIENIRTVVS LTQERKFESM YVEKLHEPYR NSVQMAHIYG ITFSISQAFM YFSYAGCFRF
GAYLIVNGHM RFRDVILVFS AIVFGAVALG HASSFAPDYA KAKLSAAHLF SLFERQPLID
SYSGEGLWPD KFEGSVTFNE VVFNYPTRAN MPVLQGLSLE VKKGQTLALV GSSGCGKSTV
VQLLERFYDP MAGTVLLDGQ EAKKLNIQWL RAQLGIVSQE PVLFDCSIAE NIAYGDNSRV
VSQDEIVRAA KAANIHPFIE TLPQKYKTRV GDKGTQLSGG QKQRLAIRRA LIRQPRVLLL
DEATSALDTE SEKVVQEALD KAREGRTCIV IAHRLSTIQN ADLIVVIQNG KVKEHGTHQQ
LLAQKGIYFS MVNIQAGAQN S


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