P06795 · MDR1B_MOUSE
- ProteinATP-dependent translocase ABCB1
- GeneAbcb1b
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1276 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Translocates drugs and phospholipids across the membrane. Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins. Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells.
Miscellaneous
In mouse the MDR gene family includes three or more related but distinct cellular genes.
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ADP + H+ + phosphate
- a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H+ + phosphate
- a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ATP + H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ADP + H+ + phosphate
- a sphingomyelin(in) + ATP + H2O = a sphingomyelin(out) + ADP + H+ + phosphate
Activity regulation
Translocase activity is inhibited by verapamil and is sensitive to energy depletion. C1orf115 regulates drug efflux through modulation of ABCB1 localization and activity.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | external side of apical plasma membrane | |
Cellular Component | Golgi membrane | |
Cellular Component | intercellular canaliculus | |
Cellular Component | mitochondrion | |
Cellular Component | plasma membrane | |
Molecular Function | ABC-type xenobiotic transporter activity | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATPase-coupled transmembrane transporter activity | |
Molecular Function | floppase activity | |
Molecular Function | phosphatidylcholine floppase activity | |
Molecular Function | xenobiotic transmembrane transporter activity | |
Biological Process | ceramide translocation | |
Biological Process | establishment of endothelial blood-brain barrier | |
Biological Process | phospholipid translocation | |
Biological Process | response to xenobiotic stimulus | |
Biological Process | Sertoli cell barrier remodeling |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent translocase ABCB1
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP06795
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: ABCB1 localization is influenced by C1orf115 expression levels (plasma membrane versus cytoplasm).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-43 | Cytoplasmic | ||||
Sequence: MEFEENLKGRADKNFSKMGKKSKKEKKEKKPAVGVFGMFRYAD | ||||||
Transmembrane | 44-66 | Helical | ||||
Sequence: WLDKLCMILGTLAAIIHGTLLPL | ||||||
Topological domain | 67-115 | Extracellular | ||||
Sequence: LMLVFGNMTDSFTKAEASILPSITNQSGPNSTLIISNSSLEEEMAIYAY | ||||||
Transmembrane | 116-136 | Helical | ||||
Sequence: YYTGIGAGVLIVAYIQVSLWC | ||||||
Topological domain | 137-185 | Cytoplasmic | ||||
Sequence: LAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGI | ||||||
Transmembrane | 186-207 | Helical | ||||
Sequence: GDKIGMFFQSITTFLAGFIIGF | ||||||
Topological domain | 208-214 | Extracellular | ||||
Sequence: ISGWKLT | ||||||
Transmembrane | 215-235 | Helical | ||||
Sequence: LVILAVSPLIGLSSALWAKVL | ||||||
Topological domain | 236-293 | Cytoplasmic | ||||
Sequence: TSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAIT | ||||||
Transmembrane | 294-315 | Helical | ||||
Sequence: ASISIGIAYLLVYASYALAFWY | ||||||
Topological domain | 316-329 | Extracellular | ||||
Sequence: GTSLVLSNEYSIGE | ||||||
Transmembrane | 330-351 | Helical | ||||
Sequence: VLTVFFSILLGTFSIGHLAPNI | ||||||
Topological domain | 352-709 | Cytoplasmic | ||||
Sequence: EAFANARGAAFEIFKIIDNEPSIDSFSTKGYKPDSIMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTRGNEIEPGNNAYGSQSDTDASELTSEESKSPLIRRSIYRSVHRKQDQERRLSMKEAVDEDVPLVSFWRILNLNLSEWPYL | ||||||
Transmembrane | 710-730 | Helical | ||||
Sequence: LVGVLCAVINGCIQPVFAIVF | ||||||
Topological domain | 731-754 | Extracellular | ||||
Sequence: SRIVGVFSRDDDHETKRQNCNLFS | ||||||
Transmembrane | 755-775 | Helical | ||||
Sequence: LFFLVMGLISFVTYFFQGFTF | ||||||
Topological domain | 776-830 | Cytoplasmic | ||||
Sequence: GKAGEILTKRVRYMVFKSMLRQDISWFDDHKNSTGSLTTRLASDASSVKGAMGAR | ||||||
Transmembrane | 831-851 | Helical | ||||
Sequence: LAVVTQNVANLGTGVILSLVY | ||||||
Topological domain | 852 | Extracellular | ||||
Sequence: G | ||||||
Transmembrane | 853-872 | Helical | ||||
Sequence: WQLTLLLVVIIPLIVLGGII | ||||||
Topological domain | 873-932 | Cytoplasmic | ||||
Sequence: EMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKK | ||||||
Transmembrane | 933-955 | Helical | ||||
Sequence: AHVFGITFSFTQAMMYFSYAACF | ||||||
Topological domain | 956-971 | Extracellular | ||||
Sequence: RFGAYLVAQQLMTFEN | ||||||
Transmembrane | 972-993 | Helical | ||||
Sequence: VMLVFSAVVFGAMAAGNTSSFA | ||||||
Topological domain | 994-1276 | Cytoplasmic | ||||
Sequence: PDYAKAKVSASHIIRIIEKTPEIDSYSTEGLKPTLLEGNVKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQAGAKRS |
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 69 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000093334 | 1-1276 | ATP-dependent translocase ABCB1 | |||
Sequence: MEFEENLKGRADKNFSKMGKKSKKEKKEKKPAVGVFGMFRYADWLDKLCMILGTLAAIIHGTLLPLLMLVFGNMTDSFTKAEASILPSITNQSGPNSTLIISNSSLEEEMAIYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANARGAAFEIFKIIDNEPSIDSFSTKGYKPDSIMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTRGNEIEPGNNAYGSQSDTDASELTSEESKSPLIRRSIYRSVHRKQDQERRLSMKEAVDEDVPLVSFWRILNLNLSEWPYLLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTSSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLKPTLLEGNVKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQAGAKRS | ||||||
Glycosylation | 73 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 91 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 96 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 103 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 641 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 659 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Several phosphorylated serine residues are present in the linker domain.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Basic and acidic residues | ||||
Sequence: MEFEENLKGRADKNFSKMGKK | ||||||
Region | 1-26 | Disordered | ||||
Sequence: MEFEENLKGRADKNFSKMGKKSKKEK | ||||||
Domain | 50-356 | ABC transmembrane type-1 1 | ||||
Sequence: MILGTLAAIIHGTLLPLLMLVFGNMTDSFTKAEASILPSITNQSGPNSTLIISNSSLEEEMAIYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFAN | ||||||
Domain | 391-627 | ABC transporter 1 | ||||
Sequence: LEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMT | ||||||
Compositional bias | 633-650 | Polar residues | ||||
Sequence: EIEPGNNAYGSQSDTDAS | ||||||
Region | 633-659 | Disordered | ||||
Sequence: EIEPGNNAYGSQSDTDASELTSEESKS | ||||||
Domain | 709-998 | ABC transmembrane type-1 2 | ||||
Sequence: LLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTSSFAPDYAK | ||||||
Domain | 1033-1271 | ABC transporter 2 | ||||
Sequence: VKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQA |
Sequence similarities
Belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,276
- Mass (Da)140,994
- Last updated1988-01-01 v1
- Checksum1804D0F011B0FF4E
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2JGL4 | A0A0G2JGL4_MOUSE | Abcb1b | 106 | ||
A0A0G2JF49 | A0A0G2JF49_MOUSE | Abcb1b | 205 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Basic and acidic residues | ||||
Sequence: MEFEENLKGRADKNFSKMGKK | ||||||
Compositional bias | 633-650 | Polar residues | ||||
Sequence: EIEPGNNAYGSQSDTDAS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M14757 EMBL· GenBank· DDBJ | AAA79005.1 EMBL· GenBank· DDBJ | mRNA | ||
M60348 EMBL· GenBank· DDBJ | AAA39513.1 EMBL· GenBank· DDBJ | Genomic DNA |