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TRPM3 Membrane Protein Introduction

Introduction of TRPM3

TRPM3, also known as MLSN2 and GON-2, belongs to transient receptor potential cation channel subfamily M. It is encoded by the TRPM3 gene, which is located at chromosome 9q21.13. TRPM3 is shown to be widely expressed in kidney, brain, ovary, and testis. In the nervous system, TRPM3 expression has been reported in both CNS and PNS, including DRG neurons and various nonneuronal tissues. The structure of TRPM3 is characterized by a homo-tetrameric channel with a distinct ~700 amino acid long TRPM-specific domain in the cytoplasmic N-terminus.

Basic Information of TRPM3
Protein Name Transient receptor potential cation channel subfamily M member 3
Gene Name TRPM3
Aliases GON-2, LTRPC3, MLSN2
Organism Homo sapiens (Human)
UniProt ID Q9HCF6
Transmembrane Times 7
Length (aa) 1732
Sequence MPEPWGTVYFLGIAQVFSFLFSWWNLEGVMNQADAPRPLNWTIRKLCHAAFLPSVRLLKAQKSWIERAFYKRECVHIIPSTKDPHRCCCGRLIGQHVGLTPSISVLQNEKNESRLSRNDIQSEKWSISKHTQLSPTDAFGTIEFQGGGHSNKAMYVRVSFDTKPDLLLHLMTKEWQLELPKLLISVHGGLQNFELQPKLKQVFGKGLIKAAMTTGAWIFTGGVNTGVIRHVGDALKDHASKSRGKICTIGIAPWGIVENQEDLIGRDVVRPYQTMSNPMSKLTVLNSMHSHFILADNGTTGKYGAEVKLRRQLEKHISLQKINTRCLPFFSLDSRLFYSFWGSCQLDSVGIGQGVPVVALIVEGGPNVISIVLEYLRDTPPVPVVVCDGSGRASDILAFGHKYSEEGGLINESLRDQLLVTIQKTFTYTRTQAQHLFIILMECMKKKELITVFRMGSEGHQDIDLAILTALLKGANASAPDQLSLALAWNRVDIARSQIFIYGQQWPVGSLEQAMLDALVLDRVDFVKLLIENGVSMHRFLTISRLEELYNTRHGPSNTLYHLVRDVKKGNLPPDYRISLIDIGLVIEYLMGGAYRCNYTRKRFRTLYHNLFGPKRPKALKLLGMEDDIPLRRGRKTTKKREEEVDIDLDDPEINHFPFPFHELMVWAVLMKRQKMALFFWQHGEEAMAKALVACKLCKAMAHEASENDMVDDISQELNHNSRDFGQLAVELLDQSYKQDEQLAMKLLTYELKNWSNATCLQLAVAAKHRDFIAHTCSQMLLTDMWMGRLRMRKNSGLKVILGILLPPSILSLEFKNKDDMPYMSQAQEIHLQEKEAEEPEKPTKEKEEEDMELTAMLGRNNGESSRKKDEEEVQSKHRLIPLGRKIYEFYNAPIVKFWFYTLAYIGYLMLFNYIVLVKMERWPSTQEWIVISYIFTLGIEKMREILMSEPGKLLQKVKVWLQEYWNVTDLIAILLFSVGMILRLQDQPFRSDGRVIYCVNIIYWYIRLLDIFGVNKYLGPYVMMIGKMMIDMMYFVIIMLVVLMSFGVARQAILFPNEEPSWKLAKNIFYMPYWMIYGEVFADQIDPPCGQNETREDGKIIQLPPCKTGAWIVPAIMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQLIMTFHERPVLPPPLIIFSHMTMIFQHLCCRWRKHESDPDERDYGLKLFITDDELKKVHDFEEQCIEEYFREKDDRFNSSNDERIRVTSERVENMSMRLEEVNEREHSMKASLQTVDIRLAQLEDLIGRMATALERLTGLERAESNKIRSRTSSDCTDAAYIVRQSSFNSQEGNTFKLQESIDPAGEETMSPTSPTLMPRMRSHSFYSVNMKDKGGIEKLESIFKERSLSLHRATSSHSVAKEPKAPAAPANTLAIVPDSRRPSSCIDIYVSAMDELHCDIDPLDNSVNILGLGEPSFSTPVPSTAPSSSAYATLAPTDRPPSRSIDFEDITSMDTRSFSSDYTHLPECQNPWDSEPPMYHTIERSKSSRYLATTPFLLEEAPIVKSHSFMFSPSRSYYANFGVPVKTAEYTSITDCIDTRCVNAPQAIADRAAFPGGLGDKVEDLTCCHPEREAELSHPSSDSEENEAKGRRATIAISSQEGDNSERTLSNNITVPKIERANSYSAEEPSAPYAHTRKSFSISDKLDRQRNTASLRNPFQRSKSSKPEGRGDSLSMRRLSRTSAFQSFESKHN

Function of TRPM3 Membrane Protein

TRPM3 is a nonselective cation channel with relatively high Ca²⁺ permeability and has a strong outwardly rectifying current-voltage relationship, playing crucial roles in cellular calcium ion signaling and homeostasis. The TRPM3 protein can regulate calcium entry, and the activity of this channel will be enhanced under the condition of calcium store depletion. On the other hand, neurosteroid pregnenolone sulfate is reported to activate TRPM3 in the pancreatic beta cell. And the activation may result in calcium influx and subsequent release of insulin, therefore, it is suggested that TRPM3 plays a role in the regulation of glucose homeostasis. Additionally, TRPM3 is involved in multiple other biological processes, such as sensory perception of temperature stimulus, detection of temperature stimulus, etc.

Schematic representation of the molecular mechanisms of TRPM3 modulation. Fig.1 Schematic representation of the molecular mechanisms of TRPM3 modulation. (Joris, 2018)

Application of TRPM3 Membrane Protein in Literature

  1. Przibilla J., et al. Ca²⁺-dependent regulation and binding of calmodulin to multiple sites of Transient Receptor Potential Melastatin 3 (TRPM3) ion channels. Cell Calcium. 2018, 73:40-52. PubMed ID: 29880196

    This article shows that TRPM3 cation channels are modulated by intracellular calcium ion and provides the basis for a mechanism of the calmodulin regulating TRPM3.

  2. Quallo T., et al. G protein βγ subunits inhibit TRPM3 ion channels in sensory neurons. Elife. 2017, 6. pii: e26138. PubMed ID: 28826490

    This article suggests that agonists of the Gi-coupled µ opioid, GABA-B and NPY receptors, can inhibit the activity of TRPM3 expressed in mouse dorsal root ganglion neurons.

  3. Siroky B.J., et al. Primary cilia regulate the osmotic stress response of renal epithelial cells through TRPM3. Am J Physiol Renal Physiol. 2017, 312(4):F791-F805. PubMed ID: 28122715

    This article demonstrates that TRPM3 is involved in the maximal osmotic response in renal epithelial cells and that the response requires the primary cilia and can be regulated by TRPV4 independent of cilia.

  4. Suzuki H., et al. Diclofenac, a nonsteroidal anti-inflammatory drug, is an antagonist of human TRPM3 isoforms. Pharmacol Res Perspect. 2016, 4(3):e00232. PubMed ID: 27433342

    This article demonstrates that diclofenac inhibits human TRPM3 without interacting with the channel pore.

  5. Rubil S. and Thiel G. Activation of gene transcription via CIM0216, a synthetic ligand of transient receptor potential melastatin-3 (TRPM3) channels. Channels (Austin). 2017, 11(1):79-83. PubMed ID: 27356187

    This article confirms that CIM0216 is less capable in activating TRPM3-mediated gene transcription, suggesting that pregnenolone sulfate is still the potent ligand of choice for affecting the gene expression pattern via TRPM3.

TRPM3 Preparation Options

In order to provide high-quality membrane protein preparation service, we have developed a versatile Magic™ membrane protein production platform. Our experienced scientists will do their best to help you find a perfect match in your required formats. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-TRPM3 antibody development services.


Creative Biolabs can offer high-quality membrane protein production service using a variety of strategies. Based on our leading-edge platform, we have successfully produced, purified, stabilized and characterized many challenging membrane protein targets for global customers. If you are interested in the service we can provide, please feel free to contact us for more information.

Reference

  1. Joris Vriens and Thomas Voets. (2018). Sensing the heat with TRPM3. Pflügers Archiv. 470(5): 799-807.

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