Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR004323 is a Divalent ion tolerance protein, CutA.
<p>The CutA family of proteins which exhibit ion tolerance are found in a large variety of species [[cite:PUB00014093]]. In E.Coli, two operons on the cutA locus contain genes that encode three proteins, CutA1, CutA2 and CutA3. CutA1 proteins are found in the cytoplasm while CutA2 (50kDa) and CutA3 (24kDa) are located in the inner membrane. Although the role of E. Coli CutA1 is not clear, studies on E. coli cutA locus describe some mutations that lead to an increase in copper sensitivity, thus suggesting a role in ion tolerance [[cite:PUB00007507]].</p> <p>To date, the structure of CutA proteins from several species have been solved [[cite:PUB00022783], [cite:PUB00028855]]. The crystal structures of the E.Coli and rat CutA1 proteins show both these proteins to be trimeric in the crystal as well as in solution[[cite:PUB00014093]].Trimerisation seems to supported by the formation of β sheets between the subunit. This trimeric structure suggests the protein may be involved in signal transduction due to architectural similarities with PII signal transducer proteins [[cite:PUB00014093]]. Recent studies propose that mammalian CutA1 in the neuronal cell membrane acts as an anchor for acetylcholinesterase (AChE)1 [[cite:PUB00056052]].</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Biological process | Response to metal ion | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a metal ion stimulus. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: protein CutA, chloroplastic-like isoform X2 [Cicer arietinum] gi|502133020|ref|XP_004501622.1| | 15 | ||
| – | PREDICTED: protein CutA, chloroplastic-like isoform X2 [Cicer arietinum] gi|502133020|ref|XP_004501622.1| | 16 | ||
| – | Divalent-cation tolerance protein CutA; TAIR: AT2G33740.2 Nitrogen regulatory PII-like, alpha/beta; Swiss-Prot: sp|P93009|CUTA_ARATH Protein CutA, chloroplastic; TrEMBL-Plants: tr|G7J568|G7J568_MEDTR Divalent cation tolerance protein, CutA1 family protein; Found in the gene: LotjaGi1g1v0348600 | 16 | ||
| – | Divalent-cation tolerance protein CutA; TAIR: AT2G33740.2 Nitrogen regulatory PII-like, alpha/beta; Swiss-Prot: sp|P93009|CUTA_ARATH Protein CutA, chloroplastic; TrEMBL-Plants: tr|I3SA72|I3SA72_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0348600 | 8 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| SSF54913 | SUPERFAMILY | 1 | 25.00 |