Protein: Solute carrier organic anion transporter family member 2B1 (Organic anion transporter B) (OATP-B) (Organic anion transporter polypeptide-related protein 2) (OATP-RP2) (OATPRP2) (Organic anion transporting polypeptide 2B1) (OATP2B1) (Solute carrier family 21 member 9) (O94956)
Organism: Homo sapiens (Human)
Function: Mediates the Na(+)-independent transport of steroid sulfate conjugates and other specific organic anions. Responsible for the transport of estrone 3-sulfate (E1S) through the basal membrane of syncytiotrophoblast, highlighting a potential role in the placental absorption of fetal-derived sulfated steroids including the steroid hormone precursor dehydroepiandrosterone sulfate (DHEA-S). Also facilitates the uptake of sulfated steroids at the basal/sinusoidal membrane of hepatocytes, therefore accounting for the major part of organic anions clearance of liver. Mediates the intestinal uptake of sulfated steroids. Mediates the uptake of the neurosteroids DHEA-S and pregnenolone sulfate (PregS) into the endothelial cells of the blood-brain barrier as the first step to enter the brain. Also plays a role in the reuptake of neuropeptides such as substance P/TAC1 and vasoactive intestinal peptide/VIP released from retinal neurons. May act as a heme transporter that promotes cellular iron availability via heme oxygenase/HMOX2 and independently of TFRC. Also transports heme by-product coproporphyrin III (CPIII), and may be involved in their hepatic disposition. Mediates the uptake of other substrates such as prostaglandins D2 (PGD2), E1 (PGE1) and E2 (PGE2), taurocholate, L-thyroxine, leukotriene C4 and thromboxane B2. May contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (Probable). Shows a pH-sensitive substrate specificity which may be ascribed to the protonation state of the binding site and leads to a stimulation of substrate transport in an acidic microenvironment. The exact transport mechanism has not been yet deciphered but most likely involves an anion exchange, coupling the cellular uptake of organic substrate with the efflux of an anionic compound. Hydrogencarbonate/HCO3(-) acts as a probable counteranion that exchanges for organic anions. Cytoplasmic glutamate may also act as counteranion in the placenta. An inwardly directed proton gradient has also been proposed as the driving force of E1S uptake with a (H(+):E1S) stoichiometry of (1:1).
Subcellular location: Cell membrane {ECO:0000269|PubMed:25132355}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000269|PubMed:11159893, ECO:0000269|PubMed:11932330, ECO:0000269|PubMed:12409283, ECO:0000269|PubMed:35307651}; Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:28408210}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:12724351, ECO:0000269|PubMed:28408210}; Multi-pass membrane protein {ECO:0000305}. Note=Expressed at the basal membrane of hepatocytes, syncytiotrophoblast and Sertoli cells (PubMed:11159893, PubMed:11932330, PubMed:12409283, PubMed:35307651). Localized to the basolateral membrane of enterocytes (PubMed:28408210). Also found at the apical membrane of enterocytes (PubMed:12724351, PubMed:28408210). {ECO:0000269|PubMed:11159893, ECO:0000269|PubMed:11932330, ECO:0000269|PubMed:12409283, ECO:0000269|PubMed:12724351, ECO:0000269|PubMed:28408210, ECO:0000269|PubMed:35307651}.
Interaction partners:
- Broad substrate specificity ATP-binding cassette transporter ABCG2
- Organic anion transporter 3
- Solute carrier family 22 member 7
- Multidrug and toxin extrusion protein 1
- Hepatic sodium/bile acid cotransporter
- ATP-binding cassette sub-family C member 3
- ATP-binding cassette sub-family C member 2
- ATP-binding cassette sub-family C member 4
- Organic anion transporter 7
- Solute carrier family 22 member 1
Sequence:
MGPRIGPAGEVPQVPDKETKATMGTENTPGGKASPDPQDVRPSVFHNIKLFVLCHSLLQLAQLMISGYLKSSISTVEKRFGLSSQTSGLLASFNEVGNTALIVFVSYFGSRVHRPRMIGYGAILVALAGLLMTLPHFISEPYRYDNTSPEDMPQDFKASLCLPTTSAPASAPSNGNCSSYTETQHLSVVGIMFVAQTLLGVGGVPIQPFGISYIDDFAHNSNSPLYLGILFAVTMMGPGLAFGLGSLMLRLYVDINQMPEGGISLTIKDPRWVGAWWLGFLIAAGAVALAAIPYFFFPKEMPKEKRELQFRRKVLAVTDSPARKGKDSPSKQSPGESTKKQDGLVQIAPNLTVIQFIKVFPRVLLQTLRHPIFLLVVLSQVCLSSMAAGMATFLPKFLERQFSITASYANLLIGCLSFPSVIVGIVVGGVLVKRLHLGPVGCGALCLLGMLLCLFFSLPLFFIGCSSHQIAGITHQTSAHPGLELSPSCMEACSCPLDGFNPVCDPSTRVEYITPCHAGCSSWVVQDALDNSQVFYTNCSCVVEGNPVLAGSCDSTCSHLVVPFLLLVSLGSALACLTHTPSFMLILRGVKKEDKTLAVGIQFMFLRILAWMPSPVIHGSAIDTTCVHWALSCGRRAVCRYYNNDLLRNRFIGLQFFFKTGSVICFALVLAVLRQQDKEARTKESRSSPAVEQQLLVSGPGKKPEDSRV