Summary: HCO3- transporter family
This is the Wikipedia entry entitled "Bicarbonate transporter proteins". More...
Does Pfam agree with the content of the Wikipedia entry ?
Editing Wikipedia articles
Before you edit for the first time
You should take a few minutes to view the following pages:
How your contribution will be recorded
HCO3- transporter family Provide feedback
External database links
|MIM:||112050 130600 112010|
This tab holds annotation information from the InterPro database.
InterPro entry IPR011531
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 [PUBMED:2289848]. Na+/HCO3 - co-transport proteins mediate the coupled movement of Na+ and HCO3 - across plasma membranes, often in an electrogenic manner [PUBMED:9261985]. 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 [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.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||integral to membrane (GO:0016021)|
|Biological process||anion transport (GO:0006820)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
- the Pfam graphic itself.
Loading domain graphics...
This large superfamily contains a variety of transporters including amino acid permeases that according to TCDB belong to the APC (Amino acid-Polyamine-organoCation) superfamily.
The clan contains the following 18 members:AA_permease AA_permease_2 AA_permease_C Aa_trans BenE Branch_AA_trans CstA HCO3_cotransp K_trans Na_Ala_symp Nramp Spore_permease SSF Sulfate_tra_GLY Sulfate_transp Transp_cyt_pur Trp_Tyr_perm Xan_ur_permease
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
- Pfam viewer
- an HTML-based viewer that uses DAS to retrieve alignment fragments on request
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
Format an alignment
If you find these logos useful in your own work, please consider citing the following article:
Note: You can also download the data file for the tree.
Curation and family details
|Seed source:||Pfam-B_1004 (release 3.0)|
|Author:||Croning MDR, Finn RD, Bateman A|
|Number in seed:||18|
|Number in full:||2233|
|Average length of the domain:||300.50 aa|
|Average identity of full alignment:||27 %|
|Average coverage of the sequence by the domain:||52.48 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
Weight segments by...
Change the size of the sunburst
selected sequences to HMM
a FASTA-format file
- 0 sequences
- 0 species
How the sunburst is generated
Colouring and labels
Anomalies in the taxonomy tree
Missing taxonomic levels
Unmapped species names
Too many species/sequences
The tree shows the occurrence of this domain across different species. More...
You can use the tree controls to manipulate how the interactive tree is displayed:
- show/hide the summary boxes
- highlight species that are represented in the seed alignment
- expand/collapse the tree or expand it to a given depth
- select a sub-tree or a set of species within the tree and view them graphically or as an alignment
- save a plain text representation of the tree
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the HCO3_cotransp domain has been found. There are 7 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
Loading structure mapping...