The domain within your query sequence starts at position 436 and ends at position 956; the E-value for the HCO3_cotransp domain shown below is 4.1e-231.

LQRTGRFCGGLIKDIKRKAPFFASDFYDALNIQALSAILFIYLATVTNAITFGGLLGDAT
DNMQGVLESFLGTAVSGAIFCLFAGQPLTILSSTGPVLVFERLLFNFSKDHNFDYLEFRL
WIGLWSAFMCLVLVATDASFLVQYFTRFTEEGFSSLISFIFIYDAFKKMIKLADYYPINS
DFKVGYNTHFSCACLPPDPVNLSVSNDTTLAPEDLPTISSTDMYHNVTFDWAYLSKKECV
KYGGKLVGNNCDFVPDITLMSFILFLGTYTSSMAMKKFKTSRYFPTTARKLISDFAIILS
ILIFCVIDALVGVDTPKLIVPSEFKPTSPNRGWFVPPFGGNPWWVCLAAAIPALLVTILI
FMDQQITAVIVNRKEHKLKKGAGYHLDLFWVAILMVVCSFMALPWYVAATVISIAHIDSL
KMETETSAPGEQPKFLGVREQRVTGTLVFILTGLSVFMAPILKFIPMPVLYGVFLYMGVA
SLNGVQFMDRLKLLLMPLKHQPDFIYLRHVPLRRVHLFTFL

HCO3_cotransp

 HCO3_cotransp
PFAM accession number:PF00955
Interpro abstract (IPR011531):

Bicarbonate (HCO 3 - ) 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 HCO 3 - transport modes. Anion exchanger proteins exchange HCO 3 - for Cl - in a reversible, electroneutral manner [ (PUBMED:2289848) ]. Na + /HCO 3 - co-transport proteins mediate the coupled movement of Na + and HCO 3 - across plasma membranes, often in an electrogenic manner [ (PUBMED:9261985) ]. Na - driven Cl - /HCO 3 - exchange and K + /HCO 3 - 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 HCO 3 - transporters that have been cloned to date (the anion exchangers and Na + /HCO 3 - co-transporters) reveals that they are homologous. This is not entirely unexpected, given that they both transport HCO 3 - and are inhibited by a class of pharmacological agents called disulphonic stilbenes [ (PUBMED:9235899) ]. 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.

This domain is found at the C terminus of many bicarbonate transport proteins. It is also found in some plant proteins responsible for boron transport [ (PUBMED:12447444) ]. In these proteins it covers almost the entire length of the sequence.

GO process:anion transport (GO:0006820)
GO component:integral component of membrane (GO:0016021)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry HCO3_cotransp