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Protein

Transient receptor potential cation channel subfamily M member 7

Gene

Trpm7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential ion channel and serine/threonine-protein kinase. Divalent cation channel permeable to calcium and magnesium. Has a central role in magnesium ion homeostasis and in the regulation of anoxic neuronal cell death. Involved in TNF-induced necroptosis downstream of MLKL by mediating calcium influx. The kinase activity is essential for the channel function. May be involved in a fundamental process that adjusts plasma membrane divalent cation fluxes according to the metabolic state of the cell. Phosphorylates annexin A1 (ANXA1).1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei1622ATP1
Binding sitei1646ATP1
Binding sitei1718ATP1
Metal bindingi1751Zinc1
Active sitei1765Proton acceptor1
Binding sitei1767ATP1
Binding sitei1775ATP1
Metal bindingi1808Zinc1
Metal bindingi1810Zinc1
Metal bindingi1814Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1792 – 1798ATP7

GO - Molecular functioni

  • actin binding Source: MGI
  • ATP binding Source: UniProtKB-KW
  • calcium channel activity Source: MGI
  • kinase activity Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • myosin binding Source: MGI
  • protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  • actomyosin structure organization Source: MGI
  • calcium-dependent cell-matrix adhesion Source: MGI
  • calcium ion transport Source: MGI
  • cellular magnesium ion homeostasis Source: InterPro
  • necroptotic process Source: UniProtKB
  • protein autophosphorylation Source: MGI
  • protein phosphorylation Source: MGI
  • protein tetramerization Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Calcium transport, Ion transport, Necrosis, Transport

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-3295583. TRP channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Transient receptor potential cation channel subfamily M member 7 (EC:2.7.11.1)
Alternative name(s):
Channel-kinase 1
Long transient receptor potential channel 7
Short name:
LTrpC-7
Short name:
LTrpC7
Transient receptor potential-phospholipase C-interacting kinase
Short name:
TRP-PLIK
Gene namesi
Name:Trpm7
Synonyms:Chak, Ltrpc7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1929996. Trpm7.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 755CytoplasmicSequence analysisAdd BLAST755
Transmembranei756 – 776HelicalSequence analysisAdd BLAST21
Topological domaini777 – 855ExtracellularSequence analysisAdd BLAST79
Transmembranei856 – 876HelicalSequence analysisAdd BLAST21
Topological domaini877 – 918CytoplasmicSequence analysisAdd BLAST42
Transmembranei919 – 939HelicalSequence analysisAdd BLAST21
Topological domaini940 – 962ExtracellularSequence analysisAdd BLAST23
Transmembranei963 – 983HelicalSequence analysisAdd BLAST21
Topological domaini984 – 995CytoplasmicSequence analysisAdd BLAST12
Transmembranei996 – 1016HelicalSequence analysisAdd BLAST21
Topological domaini1017 – 1035ExtracellularSequence analysisAdd BLAST19
Intramembranei1036 – 1056Pore-formingSequence analysisAdd BLAST21
Topological domaini1057 – 1074ExtracellularSequence analysisAdd BLAST18
Transmembranei1075 – 1095HelicalSequence analysisAdd BLAST21
Topological domaini1096 – 1863CytoplasmicSequence analysisAdd BLAST768

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: MGI
  • ruffle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1797G → D: Severe reduction of kinase activity. 1 Publication1
Mutagenesisi1810C → A: Loss of kinase activity; when associated with A-1813. 1 Publication1
Mutagenesisi1813C → A: Loss of kinase activity; when associated with A-1820. 1 Publication1

Chemistry databases

GuidetoPHARMACOLOGYi499.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002153321 – 1863Transient receptor potential cation channel subfamily M member 7Add BLAST1863

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei101PhosphoserineBy similarity1
Modified residuei1224Phosphoserine1 Publication1
Modified residuei1255PhosphoserineCombined sources1
Modified residuei1300Phosphoserine1 Publication1
Modified residuei1385Phosphoserine1 Publication1
Modified residuei1386Phosphoserine1 Publication1
Modified residuei1389PhosphoserineBy similarity1
Modified residuei1394PhosphoserineBy similarity1
Modified residuei1403PhosphoserineBy similarity1
Modified residuei1404Phosphothreonine1 Publication1
Modified residuei1445PhosphoserineCombined sources1
Modified residuei1466Phosphothreonine1 Publication1
Modified residuei1498Phosphoserine1 Publication1
Modified residuei1502PhosphoserineCombined sources1
Modified residuei1525PhosphoserineBy similarity1
Modified residuei1567Phosphoserine1 Publication1
Modified residuei1846Phosphoserine1 Publication1
Modified residuei1849Phosphoserine1 Publication1

Post-translational modificationi

Autophosphorylated.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ923J1.
PaxDbiQ923J1.
PRIDEiQ923J1.

PTM databases

iPTMnetiQ923J1.
PhosphoSitePlusiQ923J1.

Expressioni

Tissue specificityi

Found to be expressed in brain and skeletal muscle, with stronger signals in kidney, heart, liver and spleen.1 Publication

Gene expression databases

BgeeiENSMUSG00000027365.
ExpressionAtlasiQ923J1. baseline and differential.
GenevisibleiQ923J1. MM.

Interactioni

Subunit structurei

Forms heterodimers with TRPM6. Interacts with PLCB1 (By similarity). Homodimer.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ActbP607102EBI-8010314,EBI-353957
Ddb1Q3U1J42EBI-8010314,EBI-2552275
DDX3XO005712EBI-8010314,EBI-353779From a different organism.
Myh9Q8VDD54EBI-8010314,EBI-400906
RYBPQ8N4883EBI-8010314,EBI-752324From a different organism.

GO - Molecular functioni

  • actin binding Source: MGI
  • myosin binding Source: MGI

Protein-protein interaction databases

BioGridi208438. 1 interactor.
IntActiQ923J1. 105 interactors.
MINTiMINT-2524821.
STRINGi10090.ENSMUSP00000099513.

Structurei

Secondary structure

11863
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1555 – 1562Combined sources8
Helixi1563 – 1565Combined sources3
Beta strandi1576 – 1583Combined sources8
Beta strandi1585 – 1588Combined sources4
Helixi1590 – 1595Combined sources6
Beta strandi1598 – 1600Combined sources3
Beta strandi1605 – 1613Combined sources9
Beta strandi1620 – 1632Combined sources13
Helixi1633 – 1635Combined sources3
Beta strandi1641 – 1648Combined sources8
Helixi1650 – 1655Combined sources6
Turni1657 – 1659Combined sources3
Helixi1664 – 1689Combined sources26
Beta strandi1704 – 1708Combined sources5
Turni1709 – 1712Combined sources4
Beta strandi1713 – 1719Combined sources7
Beta strandi1726 – 1729Combined sources4
Helixi1741 – 1756Combined sources16
Turni1757 – 1759Combined sources3
Beta strandi1760 – 1764Combined sources5
Beta strandi1767 – 1769Combined sources3
Beta strandi1772 – 1775Combined sources4
Beta strandi1777 – 1780Combined sources4
Helixi1786 – 1788Combined sources3
Beta strandi1790 – 1793Combined sources4
Helixi1800 – 1807Combined sources8
Helixi1812 – 1816Combined sources5
Beta strandi1822 – 1824Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IA9X-ray2.00A/B1549-1828[»]
1IAHX-ray2.40A/B1549-1828[»]
1IAJX-ray2.80A/B1549-1828[»]
ProteinModelPortaliQ923J1.
SMRiQ923J1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ923J1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1592 – 1822Alpha-type protein kinasePROSITE-ProRule annotationAdd BLAST231

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1198 – 1250By similarityAdd BLAST53

Sequence similaritiesi

In the C-terminal section; belongs to the protein kinase superfamily. Alpha-type protein kinase family. ALPK subfamily.Curated
Contains 1 alpha-type protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3614. Eukaryota.
ENOG410XR5B. LUCA.
GeneTreeiENSGT00760000119127.
HOVERGENiHBG055663.
InParanoidiQ923J1.
KOiK04982.
OMAiKQGPTNP.
OrthoDBiEOG091G0DHL.
PhylomeDBiQ923J1.
TreeFamiTF314204.

Family and domain databases

InterProiIPR005821. Ion_trans_dom.
IPR011009. Kinase-like_dom.
IPR004166. MHCK_EF2_kinase.
IPR029601. TRPM7.
IPR032415. TRPM_tetra.
[Graphical view]
PANTHERiPTHR13800:SF8. PTHR13800:SF8. 3 hits.
PfamiPF02816. Alpha_kinase. 1 hit.
PF00520. Ion_trans. 1 hit.
PF16519. TRPM_tetra. 1 hit.
[Graphical view]
SMARTiSM00811. Alpha_kinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51158. ALPHA_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q923J1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQKSWIEST LTKRECVYII PSSKDPHRCL PGCQICQQLV RCFCGRLVKQ
60 70 80 90 100
HACFTASLAM KYSDVKLGEH FNQAIEEWSV EKHTEQSPTD AYGVINFQGG
110 120 130 140 150
SHSYRAKYVR LSYDTKPEII LQLLLKEWQM ELPKLVISVH GGMQKFELHP
160 170 180 190 200
RIKQLLGKGL IKAAVTTGAW ILTGGVNTGV AKHVGDALKE HASRSSRKIC
210 220 230 240 250
TIGIAPWGVI ENRNDLVGRD VVAPYQTLLN PLSKLNVLNN LHSHFILVDD
260 270 280 290 300
GTVGKYGAEV RLRRELEKTI NQQRIHARIG QGVPVVALIF EGGPNVILTV
310 320 330 340 350
LEYLQESPPV PVVVCEGTGR AADLLAYIHK QTEEGGNLPD AAEPDIISTI
360 370 380 390 400
KKTFNFGQSE AVHLFQTMME CMKKKELITV FHIGSEDHQD IDVAILTALL
410 420 430 440 450
KGTNASAFDQ LILTLAWDRV DIAKNHVFVY GQQWLVGSLE QAMLDALVMD
460 470 480 490 500
RVSFVKLLIE NGVSMHKFLT IPRLEELYNT KQGPTNPMLF HLIRDVKQGN
510 520 530 540 550
LPPGYKITLI DIGLVIEYLM GGTYRCTYTR KRFRLIYNSL GGNNRRSGRN
560 570 580 590 600
TSSSTPQLRK SHETFGNRAD KKEKMRHNHF IKTAQPYRPK MDASMEEGKK
610 620 630 640 650
KRTKDEIVDI DDPETKRFPY PLNELLIWAC LMKRQVMARF LWQHGEESMA
660 670 680 690 700
KALVACKIYR SMAYEAKQSD LVDDTSEELK QYSNDFGQLA VELLEQSFRQ
710 720 730 740 750
DETMAMKLLT YELKNWSNST CLKLAVSSRL RPFVAHTCTQ MLLSDMWMGR
760 770 780 790 800
LNMRKNSWYK VILSILVPPA ILMLEYKTKA EMSHIPQSQD AHQMTMEDSE
810 820 830 840 850
NNFHNITEEI PMEVFKEVKI LDSSDGKNEM EIHIKSKKLP ITRKFYAFYH
860 870 880 890 900
APIVKFWFNT LAYLGFLMLY TFVVLVKMEQ LPSVQEWIVI AYIFTYAIEK
910 920 930 940 950
VREVFMSEAG KISQKIKVWF SDYFNVSDTI AIISFFVGFG LRFGAKWNYI
960 970 980 990 1000
NAYDNHVFVA GRLIYCLNII FWYVRLLDFL AVNQQAGPYV MMIGKMVANM
1010 1020 1030 1040 1050
FYIVVIMALV LLSFGVPRKA ILYPHEEPSW SLAKDIVFHP YWMIFGEVYA
1060 1070 1080 1090 1100
YEIDVCANDS TLPTICGPGT WLTPFLQAVY LFVQYIIMVN LLIAFFNNVY
1110 1120 1130 1140 1150
LQVKAISNIV WKYQRYHFIM AYHEKPVLPP PLIILSHIVS LFCCVCKRRK
1160 1170 1180 1190 1200
KDKTSDGPKL FLTEEDQKKL HDFEEQCVEM YFDEKDDKFN SGSEERIRVT
1210 1220 1230 1240 1250
FERVEQMSIQ IKEVGDRVNY IKRSLQSLDS QIGHLQDLSA LTVDTLKTLT
1260 1270 1280 1290 1300
AQKASEASKV HNEITRELSI SKHLAQNLID DVPVRPLWKK PSAVNTLSSS
1310 1320 1330 1340 1350
LPQGDRESNN PFLCNIFMKD EKDPQYNLFG QDLPVIPQRK EFNIPEAGSS
1360 1370 1380 1390 1400
CGALFPSAVS PPELRQRRHG VEMLKIFNKN QKLGSSPNSS PHMSSPPTKF
1410 1420 1430 1440 1450
SVSTPSQPSC KSHLESTTKD QEPIFYKAAE GDNIEFGAFV GHRDSMDLQR
1460 1470 1480 1490 1500
FKETSNKIRE LLSNDTPENT LKHVGAAGYS ECCKTSTSLH SVQAESCSRR
1510 1520 1530 1540 1550
ASTEDSPEVD SKAALLPDWL RDRPSNREMP SEGGTLNGLA SPFKPVLDTN
1560 1570 1580 1590 1600
YYYSAVERNN LMRLSQSIPF VPVPPRGEPV TVYRLEESSP SILNNSMSSW
1610 1620 1630 1640 1650
SQLGLCAKIE FLSKEEMGGG LRRAVKVLCT WSEHDILKSG HLYIIKSFLP
1660 1670 1680 1690 1700
EVINTWSSIY KEDTVLHLCL REIQQQRAAQ KLTFAFNQMK PKSIPYSPRF
1710 1720 1730 1740 1750
LEVFLLYCHS AGQWFAVEEC MTGEFRKYNN NNGDEIIPTN TLEEIMLAFS
1760 1770 1780 1790 1800
HWTYEYTRGE LLVLDLQGVG ENLTDPSVIK AEEKRSCDMV FGPANLGEDA
1810 1820 1830 1840 1850
IKNFRAKHHC NSCCRKLKLP DLKRNDYTPD KIIFPQDESS DLNLQSGNST
1860
KESEATNSVR LML
Length:1,863
Mass (Da):212,399
Last modified:December 1, 2001 - v1
Checksum:i87551B4431CAD773
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti66K → R in AAF73131 (Ref. 3) Curated1
Sequence conflicti338L → F in BAB29509 (PubMed:16141072).Curated1
Sequence conflicti723K → E in BAC33685 (PubMed:16141072).Curated1
Sequence conflicti810I → T in BAC33685 (PubMed:16141072).Curated1
Sequence conflicti1494Missing in AAK57433 (PubMed:11161216).Curated1
Sequence conflicti1494Missing in BAC26234 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY032951 mRNA. Translation: AAK50377.1.
AF376052 mRNA. Translation: AAK57433.1.
AF149013 mRNA. Translation: AAF73131.1.
AL732330 Genomic DNA. Translation: CAM14550.1.
AK049329 mRNA. Translation: BAC33685.1.
AK029000 mRNA. Translation: BAC26234.1.
AK014698 mRNA. Translation: BAB29509.1.
BC009137 mRNA. Translation: AAH09137.1.
CCDSiCCDS16689.1.
RefSeqiNP_001157797.1. NM_001164325.1.
NP_067425.2. NM_021450.2.
UniGeneiMm.244705.

Genome annotation databases

EnsembliENSMUST00000103224; ENSMUSP00000099513; ENSMUSG00000027365.
GeneIDi58800.
KEGGimmu:58800.
UCSCiuc008mef.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY032951 mRNA. Translation: AAK50377.1.
AF376052 mRNA. Translation: AAK57433.1.
AF149013 mRNA. Translation: AAF73131.1.
AL732330 Genomic DNA. Translation: CAM14550.1.
AK049329 mRNA. Translation: BAC33685.1.
AK029000 mRNA. Translation: BAC26234.1.
AK014698 mRNA. Translation: BAB29509.1.
BC009137 mRNA. Translation: AAH09137.1.
CCDSiCCDS16689.1.
RefSeqiNP_001157797.1. NM_001164325.1.
NP_067425.2. NM_021450.2.
UniGeneiMm.244705.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IA9X-ray2.00A/B1549-1828[»]
1IAHX-ray2.40A/B1549-1828[»]
1IAJX-ray2.80A/B1549-1828[»]
ProteinModelPortaliQ923J1.
SMRiQ923J1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208438. 1 interactor.
IntActiQ923J1. 105 interactors.
MINTiMINT-2524821.
STRINGi10090.ENSMUSP00000099513.

Chemistry databases

GuidetoPHARMACOLOGYi499.

PTM databases

iPTMnetiQ923J1.
PhosphoSitePlusiQ923J1.

Proteomic databases

MaxQBiQ923J1.
PaxDbiQ923J1.
PRIDEiQ923J1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103224; ENSMUSP00000099513; ENSMUSG00000027365.
GeneIDi58800.
KEGGimmu:58800.
UCSCiuc008mef.2. mouse.

Organism-specific databases

CTDi54822.
MGIiMGI:1929996. Trpm7.

Phylogenomic databases

eggNOGiKOG3614. Eukaryota.
ENOG410XR5B. LUCA.
GeneTreeiENSGT00760000119127.
HOVERGENiHBG055663.
InParanoidiQ923J1.
KOiK04982.
OMAiKQGPTNP.
OrthoDBiEOG091G0DHL.
PhylomeDBiQ923J1.
TreeFamiTF314204.

Enzyme and pathway databases

ReactomeiR-MMU-3295583. TRP channels.

Miscellaneous databases

EvolutionaryTraceiQ923J1.
PROiQ923J1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027365.
ExpressionAtlasiQ923J1. baseline and differential.
GenevisibleiQ923J1. MM.

Family and domain databases

InterProiIPR005821. Ion_trans_dom.
IPR011009. Kinase-like_dom.
IPR004166. MHCK_EF2_kinase.
IPR029601. TRPM7.
IPR032415. TRPM_tetra.
[Graphical view]
PANTHERiPTHR13800:SF8. PTHR13800:SF8. 3 hits.
PfamiPF02816. Alpha_kinase. 1 hit.
PF00520. Ion_trans. 1 hit.
PF16519. TRPM_tetra. 1 hit.
[Graphical view]
SMARTiSM00811. Alpha_kinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51158. ALPHA_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRPM7_MOUSE
AccessioniPrimary (citable) accession number: Q923J1
Secondary accession number(s): A2AI58
, Q8C7S7, Q8CE54, Q921Y5, Q925B2, Q9CUT2, Q9JLQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 1, 2001
Last modified: November 2, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.