Q923J1 (TRPM7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Trpm7
Synonyms:	Chak, Ltrpc7

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1863 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. 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). Ref.1
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Binds 1 zinc ion per subunit. Ref.8
Subunit structure	Forms heterodimers with TRPM6. Interacts with PLCB1 By similarity. Homodimer. Ref.8
Subcellular location	Membrane; Multi-pass membrane protein Probable.
Tissue specificity	Found to be expressed in brain and skeletal muscle, with stronger signals in kidney, heart, liver and spleen. Ref.2
Post-translational modification	Autophosphorylated. Ref.2 Ref.7
Sequence similarities	In the C-terminal section; belongs to the protein kinase superfamily. Alpha-type protein kinase family. ALPK subfamily. In the N-terminal section; belongs to the transient receptor (TC 1.A.4) family. LTrpC subfamily. TRPM7 sub-subfamily. [View classification] Contains 1 alpha-type protein kinase domain.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Membrane
Domain	Coiled coil Transmembrane Transmembrane helix
Ligand	ATP-binding Calcium Metal-binding Nucleotide-binding Zinc
Molecular function	Calcium channel Ionic channel Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	actomyosin structure organization Inferred from direct assay. Source: MGI calcium-dependent cell-matrix adhesion Inferred from direct assay. Source: MGI protein autophosphorylation Inferred from direct assay. Source: MGI
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay. Source: MGI ruffle Inferred from direct assay. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW actin binding Inferred from direct assay. Source: MGI calcium channel activity Inferred from direct assay. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW myosin binding Inferred from direct assay. Source: MGI protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1863

1863

Transient receptor potential cation channel subfamily M member 7

PRO_0000215332

Regions

Topological domain

1 – 755

755

Cytoplasmic Potential

Transmembrane

756 – 776

21

Helical; Potential

Topological domain

777 – 855

79

Extracellular Potential

Transmembrane

856 – 876

21

Helical; Potential

Topological domain

877 – 918

42

Cytoplasmic Potential

Transmembrane

919 – 939

21

Helical; Potential

Topological domain

940 – 962

23

Extracellular Potential

Transmembrane

963 – 983

21

Helical; Potential

Topological domain

984 – 995

12

Cytoplasmic Potential

Transmembrane

996 – 1016

21

Helical; Potential

Topological domain

1017 – 1035

19

Extracellular Potential

Intramembrane

1036 – 1056

21

Pore-forming; Potential

Topological domain

1057 – 1074

18

Extracellular Potential

Transmembrane

1075 – 1095

21

Helical; Potential

Topological domain

1096 – 1863

768

Cytoplasmic Potential

Domain

1592 – 1822

231

Alpha-type protein kinase

Nucleotide binding

1792 – 1798

7

ATP

Coiled coil

1198 – 1250

53

By similarity

Sites

Active site

1765

1

Proton acceptor

Metal binding

1751

1

Zinc

Metal binding

1808

1

Zinc

Metal binding

1810

1

Zinc

Metal binding

1814

1

Zinc

Binding site

1622

1

ATP

Binding site

1646

1

ATP

Binding site

1718

1

ATP

Binding site

1767

1

ATP

Binding site

1775

1

ATP

Amino acid modifications

Modified residue

1403

1

Phosphoserine By similarity

Modified residue

1491

1

Phosphoserine Ref.7

Experimental info

Mutagenesis

1797

1

G → D: Severe reduction of kinase activity. Ref.2

Mutagenesis

1810

1

C → A: Loss of kinase activity; when associated with A-1813. Ref.2

Mutagenesis

1813

1

C → A: Loss of kinase activity; when associated with A-1820. Ref.2

Sequence conflict

66

1

K → R in AAF73131. Ref.3

Sequence conflict

338

1

L → F in BAB29509. Ref.5

Sequence conflict

723

1

K → E in BAC33685. Ref.5

Sequence conflict

810

1

I → T in BAC33685. Ref.5

Sequence conflict

1494

1

Missing in AAK57433. Ref.2

Sequence conflict

1494

1

Missing in BAC26234. Ref.5

Secondary structure

1

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1863

Helix Strand Turn

Details...

Helix

1555 – 1562

8

Helix

1563 – 1565

3

Beta strand

1576 – 1583

8

Beta strand

1585 – 1588

4

Helix

1590 – 1595

6

Beta strand

1598 – 1600

3

Beta strand

1605 – 1613

9

Beta strand

1620 – 1632

13

Helix

1633 – 1635

3

Beta strand

1641 – 1648

8

Helix

1650 – 1655

6

Turn

1657 – 1659

3

Helix

1664 – 1689

26

Beta strand

1704 – 1708

5

Turn

1709 – 1712

4

Beta strand

1713 – 1719

7

Beta strand

1726 – 1729

4

Helix

1741 – 1756

16

Turn

1757 – 1759

3

Beta strand

1760 – 1764

5

Beta strand

1767 – 1769

3

Beta strand

1777 – 1780

4

Helix

1786 – 1788

3

Beta strand

1790 – 1793

4

Helix

1800 – 1807

8

Helix

1812 – 1816

5

Sequences

	Sequence		Length	Mass (Da)
	Q923J1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 87551B4431CAD773	FASTA	1,863	212,399
	10 20 30 40 50 60 MSQKSWIEST LTKRECVYII PSSKDPHRCL PGCQICQQLV RCFCGRLVKQ HACFTASLAM 70 80 90 100 110 120 KYSDVKLGEH FNQAIEEWSV EKHTEQSPTD AYGVINFQGG SHSYRAKYVR LSYDTKPEII 130 140 150 160 170 180 LQLLLKEWQM ELPKLVISVH GGMQKFELHP RIKQLLGKGL IKAAVTTGAW ILTGGVNTGV 190 200 210 220 230 240 AKHVGDALKE HASRSSRKIC TIGIAPWGVI ENRNDLVGRD VVAPYQTLLN PLSKLNVLNN 250 260 270 280 290 300 LHSHFILVDD GTVGKYGAEV RLRRELEKTI NQQRIHARIG QGVPVVALIF EGGPNVILTV 310 320 330 340 350 360 LEYLQESPPV PVVVCEGTGR AADLLAYIHK QTEEGGNLPD AAEPDIISTI KKTFNFGQSE 370 380 390 400 410 420 AVHLFQTMME CMKKKELITV FHIGSEDHQD IDVAILTALL KGTNASAFDQ LILTLAWDRV 430 440 450 460 470 480 DIAKNHVFVY GQQWLVGSLE QAMLDALVMD RVSFVKLLIE NGVSMHKFLT IPRLEELYNT 490 500 510 520 530 540 KQGPTNPMLF HLIRDVKQGN LPPGYKITLI DIGLVIEYLM GGTYRCTYTR KRFRLIYNSL 550 560 570 580 590 600 GGNNRRSGRN TSSSTPQLRK SHETFGNRAD KKEKMRHNHF IKTAQPYRPK MDASMEEGKK 610 620 630 640 650 660 KRTKDEIVDI DDPETKRFPY PLNELLIWAC LMKRQVMARF LWQHGEESMA KALVACKIYR 670 680 690 700 710 720 SMAYEAKQSD LVDDTSEELK QYSNDFGQLA VELLEQSFRQ DETMAMKLLT YELKNWSNST 730 740 750 760 770 780 CLKLAVSSRL RPFVAHTCTQ MLLSDMWMGR LNMRKNSWYK VILSILVPPA ILMLEYKTKA 790 800 810 820 830 840 EMSHIPQSQD AHQMTMEDSE NNFHNITEEI PMEVFKEVKI LDSSDGKNEM EIHIKSKKLP 850 860 870 880 890 900 ITRKFYAFYH APIVKFWFNT LAYLGFLMLY TFVVLVKMEQ LPSVQEWIVI AYIFTYAIEK 910 920 930 940 950 960 VREVFMSEAG KISQKIKVWF SDYFNVSDTI AIISFFVGFG LRFGAKWNYI NAYDNHVFVA 970 980 990 1000 1010 1020 GRLIYCLNII FWYVRLLDFL AVNQQAGPYV MMIGKMVANM FYIVVIMALV LLSFGVPRKA 1030 1040 1050 1060 1070 1080 ILYPHEEPSW SLAKDIVFHP YWMIFGEVYA YEIDVCANDS TLPTICGPGT WLTPFLQAVY 1090 1100 1110 1120 1130 1140 LFVQYIIMVN LLIAFFNNVY LQVKAISNIV WKYQRYHFIM AYHEKPVLPP PLIILSHIVS 1150 1160 1170 1180 1190 1200 LFCCVCKRRK KDKTSDGPKL FLTEEDQKKL HDFEEQCVEM YFDEKDDKFN SGSEERIRVT 1210 1220 1230 1240 1250 1260 FERVEQMSIQ IKEVGDRVNY IKRSLQSLDS QIGHLQDLSA LTVDTLKTLT AQKASEASKV 1270 1280 1290 1300 1310 1320 HNEITRELSI SKHLAQNLID DVPVRPLWKK PSAVNTLSSS LPQGDRESNN PFLCNIFMKD 1330 1340 1350 1360 1370 1380 EKDPQYNLFG QDLPVIPQRK EFNIPEAGSS CGALFPSAVS PPELRQRRHG VEMLKIFNKN 1390 1400 1410 1420 1430 1440 QKLGSSPNSS PHMSSPPTKF SVSTPSQPSC KSHLESTTKD QEPIFYKAAE GDNIEFGAFV 1450 1460 1470 1480 1490 1500 GHRDSMDLQR FKETSNKIRE LLSNDTPENT LKHVGAAGYS ECCKTSTSLH SVQAESCSRR 1510 1520 1530 1540 1550 1560 ASTEDSPEVD SKAALLPDWL RDRPSNREMP SEGGTLNGLA SPFKPVLDTN YYYSAVERNN 1570 1580 1590 1600 1610 1620 LMRLSQSIPF VPVPPRGEPV TVYRLEESSP SILNNSMSSW SQLGLCAKIE FLSKEEMGGG 1630 1640 1650 1660 1670 1680 LRRAVKVLCT WSEHDILKSG HLYIIKSFLP EVINTWSSIY KEDTVLHLCL REIQQQRAAQ 1690 1700 1710 1720 1730 1740 KLTFAFNQMK PKSIPYSPRF LEVFLLYCHS AGQWFAVEEC MTGEFRKYNN NNGDEIIPTN 1750 1760 1770 1780 1790 1800 TLEEIMLAFS HWTYEYTRGE LLVLDLQGVG ENLTDPSVIK AEEKRSCDMV FGPANLGEDA 1810 1820 1830 1840 1850 1860 IKNFRAKHHC NSCCRKLKLP DLKRNDYTPD KIIFPQDESS DLNLQSGNST KESEATNSVR LML

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"LTRPC7 is a Mg.ATP-regulated divalent cation channel required for cell viability." Nadler M.J.S., Hermosura M.C., Inabe K., Perraud A.-L., Zhu Q., Stokes A.J., Kurosaki T., Kinet J.-P., Penner R., Scharenberg A.M., Fleig A. Nature 411:590-595(2001) [PubMed: 11385574] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, FUNCTION.
[2]	"TRP-PLIK, a bifunctional protein with kinase and ion channel activities." Runnels L.W., Yue L., Clapham D.E. Science 291:1043-1047(2001) [PubMed: 11161216] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, PHOSPHORYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-1797; CYS-1810 AND CYS-1813. Strain: BALB/c.
[3]	Matsushita M. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-372; 632-1146 AND 1243-1863. Strain: C57BL/6J. Tissue: Head and Skin.
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1687-1863. Strain: FVB/N. Tissue: Mammary gland.
[7]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1491, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity." Yamaguchi H., Matsushita M., Nairn A.C., Kuriyan J. Mol. Cell 7:1047-1057(2001) [PubMed: 11389851] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1551-1828, COFACTOR, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00312024.

RefSeq

NP_001157797.1. NM_001164325.1.
NP_067425.2. NM_021450.2.

UniGene

Mm.244705.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IA9	X-ray	2.00	A/B	1549-1828	[»]
1IAH	X-ray	2.40	A/B	1549-1828	[»]
1IAJ	X-ray	2.80	A/B	1549-1828	[»]

ProteinModelPortal

Q923J1.

SMR

Q923J1. Positions 1198-1249, 1549-1828.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-2524821.

STRING

Q923J1.

PTM databases

PhosphoSite

Q923J1.

Proteomic databases

PRIDE

Q923J1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000103224; ENSMUSP00000099513; ENSMUSG00000027365.

GeneID

58800.

KEGG

mmu:58800.

NMPDR

fig|10090.3.peg.6845.

UCSC

uc008mef.2. mouse.

Organism-specific databases

CTD

54822.

MGI

MGI:1929996. Trpm7.

Phylogenomic databases

GeneTree

ENSGT00550000074246.

HOVERGEN

HBG055663.

InParanoid

Q923J1.

OMA

NAYDNHV.

OrthoDB

EOG4SN1MS.

PhylomeDB

Q923J1.

Gene expression databases

ArrayExpress

Q923J1.

Bgee

Q923J1.

Genevestigator

Q923J1.

GermOnline

ENSMUSG00000027365. Mus musculus.

Family and domain databases

InterPro

IPR005821. Ion_trans.
IPR011009. Kinase-like_dom.
IPR004166. MHCK_EF2_kinase.
[Graphical view]

KO

K04982.

Pfam

PF02816. Alpha_kinase. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]

SMART

SM00811. Alpha_kinase. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS51158. ALPHA_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

314370.

SOURCE

Search...

Entry information

Entry name

TRPM7_MOUSE

Accession

Primary (citable) accession number: Q923J1
Secondary accession number(s): A2AI58 , Q8C7S7, Q8CE54, Q921Y5, Q925B2, Q9CUT2, Q9JLQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	December 1, 2001
Last modified:	November 16, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program