Trpm7
entrez
679906
canonical
uniprot
Q925B3
canonical
ensembl
ENSRNOG00000057806
resolver
ensp
ENSRNOP00000092648
resolver
ensp
ENSRNOP00000105095
resolver
genesymbol
Trpm7
resolver
uniprot
A0A8I6AVX9
resolver
uniprot
A6HPZ2
resolver
uniprot
A7L642
resolver
uniprot_entry
TRPM7_RAT
resolver
uniprot_sec
A0A8I6AVX9
resolver
uniprot_sec
A6HPZ2
resolver
uniprot_sec
A7L642
resolver
activity_regulation
ACTIVITY REGULATION: Channel displays constitutive activity. Channel activity is negatively regulated by cytosolic Mg(2+), Mg-ATP, low intracellular pH. Resting free cytosolic Mg(2+) and Mg-ATP concentrations seem to be sufficient to block native TRPM7 channel activity (By similarity). TRPM7 channel activity is highly dependent on membrane levels of phosphatidylinositol 4,5 bisphosphate (PIP2) (By similarity). PIP2 hydrolysis negatively regulates TRPM7 channel activity (PubMed:11941371). TRPM7 kinase activity does not affect channel activity. The kinase activity is controlled through the autophosphorylation of a serine/threonine-rich region located N-terminal to the catalytic domain (By similarity). {ECO:0000250|UniProtKB:Q923J1, ECO:0000269|PubMed:11941371}.
uniprot
proteins
amino_acid_sequence
MSQKSWIESTLTKRECVYIIPSSKDPHRCLPGCQICQQLVRCFCGRLVKQHACFTASLATKYSDVKLGEHFNQAIEEWSVEKHTEQSPTDAYGVINFQGGSHSYRAKYVRLSYDTKPEIILQLLLKEWQMELPKLVISVHGGMQKFELHPRIKQLLGKGLIKAAVTTGAWILTGGVNTGVAKHVGDALKEHASRSSRKICTIGIAPWGVIENRNDLVGRDVVAPYQTLLNPLSKLNVLNNLHSHFILVDDGTVGKYGAEVRLRRELEKTINQQRIHARIGQGVPVVALIFEGGPNVILTVLEYLQESPPVPVVVCEGTGRAADLLAYIHKQTEEGGNLPDAAEPDIISTIKKTFNFGQSEAVHLFQTMMECMKKKELITVFHIGSEDHQDIDVAILTALLKGTNASAFDQLILTLAWDRVDIAKNHVFVYGQQWLVGSLEQAMLDALVMDRVSFVKLLIENGVSMHKFLTIPRLEELYNTKQGPTNPMLFHLIRDVKQGNLPPGYKITLIDIGLVIEYLMGGTYRCTYTRKRFRLIYNSLGGNNRRSGRNASSSTPQLRKSHETFGNRADKKEKMRHNHFIKTAQPYRPKMDASMEEGKKKRTKDEIVDIDDPETKRFPYPLNELLIWACLMKRQVMARFLWQHGEESMAKALVACKIYRSMAYEAKQSDLVDDTSEELKQYSNDFGQLAVELLEQSFRQDETMAMKLLTYELKNWSNSTCLKLAVSSRLRPFVAHTCTQMLLSDMWMGRLNMRKNSWYKVILSILVPPAILMLEYKTKAEMSHIPQSQDAHQMTMEDSENNFHNITEEIPMEVFKEVKILDSSEGKNEMEIHIKSKKLPITRKFYAFYHAPIVKFWFNTLAYLGFLMLYTFVVLVQMEQLPSVQEWIVIAYIFTYAIEKIREVFMSEAGKISQKIKVWFSDYFNVSDTIAIISFFVGFGLRFGAKWNYINAYDNHVFVAGRLIYCLNIIFWYVRLLDFLAVNQQAGPYVMMIGKMVANMFYIVVIMALVLLSFGVPRKAILYPHEEPSWSLAKDIVFHPYWMIFGEVYAYEIDVCANDSALPTICGPGTWLTPFLQAVYLFVQYIIMVNLLIAFFNNVYLQVKAISNIVWKYQRYHFIMAYHEKPVLPPPLIILSHIVSLFCCICKRRKKDKTSDGPKLFLTEEDQKKLHDFEEQCVEMYFDEKDDKFNSGSEERIRVTFERVEQMSIQIKEVGDRVNYIKRSLQSLDSQIGHLQDLSALTVDTLKTLTAQKASEASKVHNEITRELSISKHLAQNLIDDVPVRPMWKKPSVVNTLSSSLPQGDRESNNPFLCNIFMKDEKDPQYNLFGQDLPVIPQRKEFNIPEAGSSCGALFPSAVSPPELRQRRHGVEMLKIFNKNQKLGSSPNSSPHMSSPPTKFSVSTPSQPSCKSHLESTTKDPEPIFYKAAEGDNIEFGAFVGHRDSMDLQRFKETSNKIRELLSNDTPENTLKHVGAAGYNECHKTPTSLHSEQESCSRRASTEDSPDVDSRAALLPDWLRDRPTNREMPSEGGTLNGLASPFKPVLDTNYYYSAVERNNLMRLSQSIPFVPVPPRGEPVTVYRLEESSPSILNNSMSSWSQLGLCAKIEFLSKEEMGGGLRRAVKVLCTWSEHDVLRSGHLYIIKSFLPEVINTWSSIYKEDTVLHLCLREIQQQRAAQKLTFAFNQMKPKSIPYSPRFLEVFLLYCHSAGQWFAVEECMTGEFRKYNNNNGDEIIPTNTLEEIMLAFSHWTYEYTRGELLVLDLQGVGENLTDPSVIKAEEKRSCDMVFGPANLGEDAIKNFRAKHHCNSCCRKLKLPDLKRNDYTPDKIIFPQDESSDLNLQAGNSTKESEATNSVRLML
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Bifunctional protein that combines an ion channel with an intrinsic kinase domain, enabling it to modulate cellular functions either by conducting ions through the pore or by phosphorylating downstream proteins via its kinase domain. The channel is highly permeable to divalent cations, specifically calcium (Ca2+), magnesium (Mg2+) and zinc (Zn2+) and mediates their influx. Controls a wide range of biological processes such as Ca2(+), Mg(2+) and Zn(2+) homeostasis, vesicular Zn(2+) release channel and intracellular Ca(2+) signaling, embryonic development, immune responses, cell motility, proliferation and differentiation. The C-terminal alpha-kinase domain autophosphorylates cytoplasmic residues of TRPM7. TRPM7 phosphorylates SMAD2, suggesting that TRPM7 kinase may play a role in activating SMAD signaling pathways (By similarity). In vitro, TRPM7 kinase phosphorylates ANXA1 (annexin A1), myosin II isoforms and a variety of proteins with diverse cellular functions (By similarity). {ECO:0000250|UniProtKB:Q923J1, ECO:0000250|UniProtKB:Q96QT4}.; FUNCTION: [TRPM7 channel, cleaved form]: The cleaved channel exhibits substantially higher current and potentiates Fas receptor signaling. {ECO:0000250|UniProtKB:Q923J1}.; FUNCTION: [TRPM7 kinase, cleaved form]: The C-terminal kinase domain can be cleaved from the channel segment in a cell-type-specific fashion. In immune cells, the TRPM7 kinase domain is clipped from the channel domain by caspases in response to Fas-receptor stimulation. The cleaved kinase fragments can translocate to the nucleus, and bind chromatin-remodeling complex proteins in a Zn(2+)-dependent manner to ultimately phosphorylate specific Ser/Thr residues of histones known to be functionally important for cell differentiation and embryonic development. {ECO:0000250|UniProtKB:Q923J1}.
uniprot
proteins
mass_dalton
212422
uniprot
proteins
post_translational_modification
PTM: Palmitoylated; palmitoylation at Cys-1143, Cys-1144 and Cys-1146 promotes TRPM7 trafficking from the Golgi to the surface membrane. {ECO:0000250|UniProtKB:Q96QT4}.; PTM: Autophosphorylated; autophosphorylation regulates TRPM7 kinase activity towards its substrates. {ECO:0000250|UniProtKB:Q96QT4}.; PTM: The C-terminal kinase domain can be cleaved from the channel segment in a cell-type-specific fashion. TRPM7 is cleaved by caspase-8, dissociating the kinase from the ion-conducting pore. The cleaved kinase fragments (M7CKs) can translocate to the cell nucleus and binds chromatin-remodeling complex proteins in a Zn(2+)-dependent manner to ultimately phosphorylate specific Ser/Thr residues of histones. {ECO:0000250|UniProtKB:Q923J1}.
uniprot
proteins
protein_family
ALPK subfamily; Transient receptor (TC 1.A.4) family
uniprot
proteins
protein_family
Alpha-type protein kinase family
uniprot
proteins
protein_family
LTrpC subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
TRPM7 sub-subfamily
uniprot
proteins
pubmed
11161216
uniprot
proteins
pubmed
11941371
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
18782578
uniprot
proteins
sequence_length
1862
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96QT4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q923J1}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q923J1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q923J1}. Note=Localized largely in intracellular Zn(2+)-storage vesicles. {ECO:0000250|UniProtKB:Q923J1}.; SUBCELLULAR LOCATION: [TRPM7 kinase, cleaved form]: Nucleus {ECO:0000250|UniProtKB:Q923J1}.
uniprot
proteins
transmembrane_region
TRANSMEM 851..876; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:Q923J1"; TRANSMEM 883..904; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:Q923J1"; TRANSMEM 924..943; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:Q923J1"; TRANSMEM 957..980; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:Q923J1"; TRANSMEM 1000..1023; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:Q923J1"; TRANSMEM 1070..1098; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:Q923J1
uniprot
proteins