TRPM7

TRPM7
Identifiers
Aliases	TRPM7, ALSPDC, CHAK, CHAK1, LTRPC7, LTrpC-7, TRP-PLIK, transient receptor potential cation channel subfamily M member 7
External IDs	OMIM: 605692 MGI: 1929996 HomoloGene: 9774 GeneCards: TRPM7
Gene location (Human)
Chr.	Chromosome 15 (human)[1]
End	50,686,797 bp[1]
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)[2]
End	126,876,230 bp[2]
Gene ontology
Molecular function	• transferase activity; • nucleotide binding; • myosin binding; • metal ion binding; • kinase activity; • protein serine/threonine kinase activity; • ion channel activity; • actin binding; • ATP binding; • calcium channel activity;
Cellular component	• integral component of membrane; • membrane; • ruffle; • cell membrane;
Biological process	• cellular magnesium ion homeostasis; • calcium-dependent cell-matrix adhesion; • programmed cell death; • phosphorylation; • actomyosin structure organization; • cation transport; • ion transport; • protein tetramerization; • protein phosphorylation; • calcium ion transmembrane transport; • autophosphorylation; • GO:0060554, GO:0060555 necroptosis; • calcium ion transport; • transmembrane transport;
	Sources:Amigo / QuickGO
Orthologs
	54822
	58800
	ENSG00000092439
	ENSMUSG00000027365
	Q96QT4
	Q923J1
	NM_001301212; NM_017672
	NM_001164325; NM_021450
	NP_001288141; NP_060142
	NP_001157797; NP_067425
	Wikidata
View/Edit Human	View/Edit Mouse

Transient receptor potential cation channel, subfamily M, member 7, also known as TRPM7, is a human gene encoding a protein of the same name.

Function

TRPs, mammalian homologs of the Drosophila transient receptor potential (trp) protein, are ion channels that are thought to mediate capacitative calcium entry into the cell. TRP-PLIK is a protein that is both an ion channel and a kinase. As a channel, it conducts calcium and monovalent cations to depolarize cells and increase intracellular calcium. As a kinase, it is capable of phosphorylating itself and other substrates. The kinase activity is necessary for channel function, as shown by its dependence on intracellular ATP and by the kinase mutants.[supplied by OMIM][5]

Interactions

TRPM7 has been shown to interact with PLCB1[6] and PLCB2.[6]

Clinical relevance

Defects in this gene have been associated to magnesium deficiency in human microvascular endothelial cells.[7]

References

GRCh38: Ensembl release 89: ENSG00000092439 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000027365 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: TRPM7 transient receptor potential cation channel, subfamily M, member 7".
Runnels LW, Yue L, Clapham DE (May 2002). "The TRPM7 channel is inactivated by PIP(2) hydrolysis". Nat. Cell Biol. 4 (5): 329–36. doi:10.1038/ncb781. PMID 11941371.
Baldoli E, Maier JA (2012). "Silencing TRPM7 mimics the effects of magnesium deficiency in human microvascular endothelial cells". Angiogenesis. 15 (1): 47–57. doi:10.1007/s10456-011-9242-0. PMID 22183257.

External links

TRPM7+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000092439 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000027365 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] "Entrez Gene: TRPM7 transient receptor potential cation channel, subfamily M, member 7".

[pmid11941371-6] Runnels LW, Yue L, Clapham DE (May 2002). "The TRPM7 channel is inactivated by PIP(2) hydrolysis". Nat. Cell Biol. 4 (5): 329–36. doi:10.1038/ncb781. PMID 11941371.

[doi.10.1007/s10456-011-9242-0-7] Baldoli E, Maier JA (2012). "Silencing TRPM7 mimics the effects of magnesium deficiency in human microvascular endothelial cells". Angiogenesis. 15 (1): 47–57. doi:10.1007/s10456-011-9242-0. PMID 22183257.