Bicarbonate transporter protein
| HCO3- transporter family | |||||||||
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a low energy structure for the final cytoplasmic loop of band 3, nmr, minimized average structure
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| Identifiers | |||||||||
| Symbol | HCO3_cotransp | ||||||||
| Pfam | PF00955 | ||||||||
| Pfam clan | CL0062 | ||||||||
| InterPro | IPR011531 | ||||||||
| PROSITE | PDOC00192 | ||||||||
| SCOP | 1btr | ||||||||
| SUPERFAMILY | 1btr | ||||||||
| TCDB | 2.A.31 | ||||||||
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| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
| Band 3 cytoplasmic domain | |||||||||
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crystal structure of the cytoplasmic domain of human erythrocyte band-3 protein
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| Identifiers | |||||||||
| Symbol | Band_3_cyto | ||||||||
| Pfam | PF07565 | ||||||||
| Pfam clan | CL0340 | ||||||||
| InterPro | IPR013769 | ||||||||
| SCOP | 1hyn | ||||||||
| SUPERFAMILY | 1hyn | ||||||||
| TCDB | 2.A.31 | ||||||||
| OPM superfamily | 336 | ||||||||
| OPM protein | 1btq | ||||||||
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| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
In molecular biology, bicarbonate transporter proteins are proteins which transport bicarbonate. Bicarbonate (HCO3−) transport mechanisms are the principal regulators of pH in animal cells. Such transport also plays a vital role in acid-base movements in the stomach, pancreas, intestine, kidney, reproductive organs and the central nervous system. Functional studies have suggested four different HCO3− transport modes. Anion exchanger proteins exchange HCO3− for Cl− in a reversible, electroneutral manner. Na+/HCO3−co-transport proteins mediate the coupled movement of Na+ and HCO3− across plasma membranes, often in an electrogenic manner. Na+ driven Cl−/HCO3− exchange and K+/HCO3− exchange activities have also been detected in certain cell types, although the molecular identities of the proteins responsible remain to be determined.
Sequence analysis of the two families of HCO3−transporters that have been cloned to date (the anion exchangers and Na+/HCO3− co-transporters) reveals that they are homologous. This is not entirely unexpected, given that they both transport HCO3− and are inhibited by a class of pharmacological agents called disulphonic stilbenes. They share around ~25-30% sequence identity, which is distributed along their entire sequence length, and have similar predicted membrane topologies, suggesting they have ~10 transmembrane (TM) domains.
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