B2RX12 · MRP3_MOUSE
- ProteinATP-binding cassette sub-family C member 3
- GeneAbcc3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1523 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
ATP-dependent transporter of the ATP-binding cassette (ABC) family that binds and hydrolyzes ATP to enable active transport of various substrates including many drugs, toxicants and endogenous compound across cell membranes. Transports glucuronide conjugates such as bilirubin diglucuronide, estradiol-17-beta-o-glucuronide and GSH conjugates such as leukotriene C4 (LTC4) (By similarity).
Transports also various bile salts (taurocholate, glycocholate, taurochenodeoxycholate-3-sulfate, taurolithocholate- 3-sulfate) (By similarity).
Does not contribute substantially to bile salt physiology but provides an alternative route for the export of bile acids and glucuronides from cholestatic hepatocytes (PubMed:15814571, PubMed:16225954).
May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (By similarity).
Transports also various bile salts (taurocholate, glycocholate, taurochenodeoxycholate-3-sulfate, taurolithocholate- 3-sulfate) (By similarity).
Does not contribute substantially to bile salt physiology but provides an alternative route for the export of bile acids and glucuronides from cholestatic hepatocytes (PubMed:15814571, PubMed:16225954).
May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (By similarity).
Catalytic activity
- an S-substituted glutathione(in) + ATP + H2O = ADP + an S-substituted glutathione(out) + H+ + phosphateThis reaction proceeds in the forward direction.
- 17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
- ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP + dehydroepiandrosterone 3-sulfate(out) + H+ + phosphateThis reaction proceeds in the forward direction.
- ATP + H2O + leukotriene C4(in) = ADP + H+ + leukotriene C4(out) + phosphateThis reaction proceeds in the forward direction.
- ATP + H2O + taurocholate(in) = ADP + H+ + phosphate + taurocholate(out)This reaction proceeds in the forward direction.
- ATP + glycocholate(in) + H2O = ADP + glycocholate(out) + H+ + phosphateThis reaction proceeds in the forward direction.
- ATP + H2O + taurolithocholate 3-sulfate(in) = ADP + H+ + phosphate + taurolithocholate 3-sulfate(out)
- ATP + H2O + taurochenodeoxycholate 3-sulfate(in) = ADP + H+ + phosphate + taurochenodeoxycholate 3-sulfate(out)This reaction proceeds in the forward direction.
- (4Z,15Z)-bilirubin IXalpha C8-beta-D-glucuronoside(in) + ATP + H2O = (4Z,15Z)-bilirubin IXalpha C8-beta-D-glucuronoside(out) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
- (4Z,15Z)-bilirubin IXalpha C8,C12-beta-D-bisglucuronoside(in) + ATP + H2O = (4Z,15Z)-bilirubin IXalpha C8,C12-beta-D-bisglucuronoside(out) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | basolateral plasma membrane | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | ABC-type bile acid transporter activity | |
Molecular Function | ABC-type glutathione S-conjugate transporter activity | |
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 | glucuronoside transmembrane transporter activity | |
Molecular Function | icosanoid transmembrane transporter activity | |
Biological Process | bile acid and bile salt transport | |
Biological Process | canalicular bile acid transport | |
Biological Process | leukotriene transport | |
Biological Process | monoatomic anion transmembrane transport | |
Biological Process | transmembrane transport | |
Biological Process | xenobiotic transmembrane transport |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-binding cassette sub-family C member 3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionB2RX12
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Basolateral cell membrane ; Multi-pass membrane protein
Basal cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-35 | Extracellular | ||||
Sequence: MDRLCGSGELGSKFWDSNLSIYTNTPDLTPCFQNS | ||||||
Transmembrane | 36-56 | Helical; Name=1 | ||||
Sequence: LLAWVPCIYLWAALPCYLFYL | ||||||
Topological domain | 57-75 | Cytoplasmic | ||||
Sequence: RHHQLGYIVLSWLSRLKTA | ||||||
Transmembrane | 76-96 | Helical; Name=2 | ||||
Sequence: LGVLLWCVSWVDLFYSFHGLI | ||||||
Topological domain | 97-102 | Extracellular | ||||
Sequence: HGSSPA | ||||||
Transmembrane | 103-123 | Helical; Name=3 | ||||
Sequence: PVFFVTPLVVGITMLLATLLI | ||||||
Topological domain | 124-129 | Cytoplasmic | ||||
Sequence: QYERLR | ||||||
Transmembrane | 130-150 | Helical; Name=4 | ||||
Sequence: GVQSSGVLIIFWLLCVICAII | ||||||
Topological domain | 151-170 | Extracellular | ||||
Sequence: PFRSKILSALAEGKILDPFR | ||||||
Transmembrane | 171-191 | Helical; Name=5 | ||||
Sequence: FTTFYIYFALVFCALILSCFK | ||||||
Topological domain | 192-301 | Cytoplasmic | ||||
Sequence: EKPPLFSPENLDTNPCPEASAGFFSRLSFWWFTRLAILGYRRPLEDRDLWSLSEEDCSHKVVQRLLEAWQKQQNQASRSQTATAEPKIPGEDAVLLKPRPKSKQPSFLRA | ||||||
Transmembrane | 302-324 | Helical; Name=6 | ||||
Sequence: LVRTFTSSLLMSACFNLIQNLLG | ||||||
Topological domain | 325-345 | Extracellular | ||||
Sequence: FVNPQLLSILIRFISDPTAPT | ||||||
Transmembrane | 346-366 | Helical; Name=7 | ||||
Sequence: WWGFLLAGLMFLSSTMQTLIL | ||||||
Topological domain | 367-419 | Cytoplasmic | ||||
Sequence: HQYYHCIFVMALRLRTAIIGVIYRKALVITNSVKRESTVGEMVNLMSVDAQRF | ||||||
Transmembrane | 420-440 | Helical; Name=8 | ||||
Sequence: MDVSPFINLLWSAPLQVILAI | ||||||
Topological domain | 441 | Extracellular | ||||
Sequence: Y | ||||||
Transmembrane | 442-462 | Helical; Name=9 | ||||
Sequence: FLWQILGPSALAGVAVIVLLI | ||||||
Topological domain | 463-535 | Cytoplasmic | ||||
Sequence: PLNGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAIST | ||||||
Transmembrane | 536-556 | Helical; Name=10 | ||||
Sequence: FIWICTPFLVTLITLGVYVYV | ||||||
Topological domain | 557-567 | Extracellular | ||||
Sequence: DESNVLDAEKA | ||||||
Transmembrane | 568-588 | Helical; Name=11 | ||||
Sequence: FVSLSLFNILKIPLNMLPQLI | ||||||
Topological domain | 589-967 | Cytoplasmic | ||||
Sequence: SGLTQASVSLKRIQDFLNQNELDPQCVERKTISPGYAITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLRNYAPDEDQEDHEAALQNANEEVLLLEDTLSTHTDLTDNEPAIYEVRKQFMREMSSLSSEGEVQNRTMPKKHTNSLEKEALVTKTKETGALIKEEIAETGNVKLSVYWDYAKSMGLCTT | ||||||
Transmembrane | 968-988 | Helical; Name=12 | ||||
Sequence: LSICLLYGGQSAAAIGANVWL | ||||||
Topological domain | 989-1013 | Extracellular | ||||
Sequence: SAWSNDAEEHGQQNKTSVRLGVYAA | ||||||
Transmembrane | 1014-1034 | Helical; Name=13 | ||||
Sequence: LGILQGLLVMLSAFTMVVGAI | ||||||
Topological domain | 1035-1071 | Cytoplasmic | ||||
Sequence: QAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKD | ||||||
Transmembrane | 1072-1092 | Helical; Name=14 | ||||
Sequence: IYVIDEVLAPTILMLLNSFFT | ||||||
Topological domain | 1093-1096 | Extracellular | ||||
Sequence: SIST | ||||||
Transmembrane | 1097-1117 | Helical; Name=15 | ||||
Sequence: IMVIVASTPLFMVVVLPLAVL | ||||||
Topological domain | 1118-1191 | Cytoplasmic | ||||
Sequence: YGFVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWL | ||||||
Transmembrane | 1192-1212 | Helical; Name=16 | ||||
Sequence: GVHVEFVGNCVVLFAALFAVI | ||||||
Topological domain | 1213-1219 | Extracellular | ||||
Sequence: GRNSLNP | ||||||
Transmembrane | 1220-1240 | Helical; Name=17 | ||||
Sequence: GLVGLSVSYALQVTMALNWMI | ||||||
Topological domain | 1241-1523 | Cytoplasmic | ||||
Sequence: RMISDLESNIIAVERVKEYSKTKTEAPWVVESNRAPEGWPTRGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAKDAGLA |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Deficient mice do not exhibit any overt phenotype under normal conditions. However when challenged with cholestasis induced by bile duct ligation, increased levels of hepatic bile salts and lower serum levels of bilirubin glucuronide are observed, suggesting that Abcc3 provides an alternative route for removal from the liver of these substrates under cholestatic conditions.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 89 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_0000356238 | 1-1523 | ATP-binding cassette sub-family C member 3 | |||
Sequence: MDRLCGSGELGSKFWDSNLSIYTNTPDLTPCFQNSLLAWVPCIYLWAALPCYLFYLRHHQLGYIVLSWLSRLKTALGVLLWCVSWVDLFYSFHGLIHGSSPAPVFFVTPLVVGITMLLATLLIQYERLRGVQSSGVLIIFWLLCVICAIIPFRSKILSALAEGKILDPFRFTTFYIYFALVFCALILSCFKEKPPLFSPENLDTNPCPEASAGFFSRLSFWWFTRLAILGYRRPLEDRDLWSLSEEDCSHKVVQRLLEAWQKQQNQASRSQTATAEPKIPGEDAVLLKPRPKSKQPSFLRALVRTFTSSLLMSACFNLIQNLLGFVNPQLLSILIRFISDPTAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYRKALVITNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTLITLGVYVYVDESNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRIQDFLNQNELDPQCVERKTISPGYAITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLRNYAPDEDQEDHEAALQNANEEVLLLEDTLSTHTDLTDNEPAIYEVRKQFMREMSSLSSEGEVQNRTMPKKHTNSLEKEALVTKTKETGALIKEEIAETGNVKLSVYWDYAKSMGLCTTLSICLLYGGQSAAAIGANVWLSAWSNDAEEHGQQNKTSVRLGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLGVHVEFVGNCVVLFAALFAVIGRNSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYSKTKTEAPWVVESNRAPEGWPTRGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAKDAGLA | ||||||
Glycosylation | 18 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 903 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 906 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 1002 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected throughout the gastrointestinal tract, liver, lung, pancreas, bladder, gall bladder and at low levels in the adrenal gland.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 310-593 | ABC transmembrane type-1 1 | ||||
Sequence: LLMSACFNLIQNLLGFVNPQLLSILIRFISDPTAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYRKALVITNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTLITLGVYVYVDESNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQ | ||||||
Domain | 626-850 | ABC transporter 1 | ||||
Sequence: ITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLRN | ||||||
Region | 903-923 | Disordered | ||||
Sequence: SSLSSEGEVQNRTMPKKHTNS | ||||||
Domain | 967-1248 | ABC transmembrane type-1 2 | ||||
Sequence: TLSICLLYGGQSAAAIGANVWLSAWSNDAEEHGQQNKTSVRLGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLGVHVEFVGNCVVLFAALFAVIGRNSLNPGLVGLSVSYALQVTMALNWMIRMISDLES | ||||||
Domain | 1287-1519 | ABC transporter 2 | ||||
Sequence: FRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAKD |
Sequence similarities
Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
B2RX12-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,523
- Mass (Da)169,223
- Last updated2021-02-10 v2
- ChecksumF25A63BDE6123AC1
B2RX12-2
- Name2
- Differences from canonical
- 862-862: Missing
B2RX12-3
- Name3
- Differences from canonical
- 803-827: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0R4J015 | A0A0R4J015_MOUSE | Abcc3 | 1522 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 81 | in Ref. 2; AAQ10530/AAQ10531 | ||||
Sequence: W → R | ||||||
Sequence conflict | 247 | in Ref. 3; BAE33375 | ||||
Sequence: D → N | ||||||
Sequence conflict | 269 | in Ref. 1; AAX39010/AAX33774, 2; AAQ10530/AAQ10531, 3; BAE33375 and 5; AAH48825/AAI50789 | ||||
Sequence: R → G | ||||||
Sequence conflict | 742 | in Ref. 3; BAE33375 | ||||
Sequence: E → G | ||||||
Alternative sequence | VSP_036011 | 803-827 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_036012 | 862 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY841885 EMBL· GenBank· DDBJ | AAX39010.1 EMBL· GenBank· DDBJ | mRNA | ||
AY795569 EMBL· GenBank· DDBJ | AAX33774.1 EMBL· GenBank· DDBJ | mRNA | ||
AF534127 EMBL· GenBank· DDBJ | AAQ10530.1 EMBL· GenBank· DDBJ | mRNA | ||
AF534128 EMBL· GenBank· DDBJ | AAQ10531.1 EMBL· GenBank· DDBJ | mRNA | ||
AK149551 EMBL· GenBank· DDBJ | BAE28953.1 EMBL· GenBank· DDBJ | mRNA | ||
AK155664 EMBL· GenBank· DDBJ | BAE33375.1 EMBL· GenBank· DDBJ | mRNA | ||
AL645965 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC048825 EMBL· GenBank· DDBJ | AAH48825.1 EMBL· GenBank· DDBJ | mRNA | ||
BC150788 EMBL· GenBank· DDBJ | AAI50789.1 EMBL· GenBank· DDBJ | mRNA |