Abcb4
entrez
24891
canonical
uniprot
Q08201
canonical
genesymbol
Abcb4
resolver
genesymbol_syn
Mdr2
resolver
genesymbol_syn
Pgp3
resolver
genesymbol_syn
Pgy2
resolver
uniprot
Q78E07
resolver
uniprot_entry
MDR3_RAT
resolver
uniprot_sec
Q78E07
resolver
activity_regulation
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}.
uniprot
proteins
amino_acid_sequence
MDLEAARNGTARRLDGDFELGSISNQSREKKKKVNLIGPLTLFRYSDWQDKLFMLLGTAMAIAHGSGLPLMMIVFGEMTDKFVDNAGNFSLPVNFSLSMLNPGRILEEEMTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFPNARGAAYVIFDIIDNNPKIDSFSERGHKPDSIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQTSGSQILSEEFEVELSDEKAAGGVAPNGWKARIFRNSTKKSLKSSRAHQNRLDVETNELDANVPPVSFLKVLRLNKTEWPYFVVGTLCAIANGALQPAFSIILSEMIAIFGPGDDTVKQQKCNMFSLVFLGLGVHSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQPLIDSYSREGMWPDKFEGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQAGTQNL
uniprot
proteins
ec_number
7.6.2.1
uniprot
proteins
function
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}.
uniprot
proteins
mass_dalton
140655
uniprot
proteins
post_translational_modification
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}.
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCB family
uniprot
proteins
protein_family
Multidrug resistance exporter (TC 3.A.1.201) subfamily
uniprot
proteins
pubmed
10067174
uniprot
proteins
pubmed
1348630
uniprot
proteins
pubmed
15159385
uniprot
proteins
pubmed
7948020
uniprot
proteins
pubmed
8103593
uniprot
proteins
sequence_length
1278
uniprot
proteins
subcellular_location
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:0000269|PubMed:15159385}. 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}.
uniprot
proteins
transmembrane_region
TRANSMEM 48..70; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 116..136; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 186..207; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 215..235; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 294..315; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 330..351; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 711..731; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 755..775; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 831..851; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 853..872; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 933..955; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 972..993; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441
uniprot
proteins