Q9JJH7 (TRPM5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transient receptor potential cation channel subfamily M member 5

Alternative name(s):
Long transient receptor potential channel 5
Short name=LTrpC-5
Short name=LTrpC5
MLSN1- and TRP-related gene 1 protein

Gene names

Name:	Trpm5
Synonyms:	Ltrpc5, Mtr1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1158 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Voltage-modulated Ca2+-activated, monovalent cation channel (VCAM) that mediates a transient membrane depolarization and plays a central role in taste transduction. Monovalent-specific, non-selective cation channel that mediates the transport of Na+, K+ and Cs+ ions equally well. Activated directly by increases in intracellular Ca2+, but is impermeable to it. Gating is voltage-dependent and displays rapid activation and deactivation kinetics upon channel stimulation even during sustained elevations in Ca2+. Also activated by a fast intracellular Ca2+ increase in response to inositol 1,4,5-triphosphate-producing receptor agonists. The channel is blocked by extracellular acidification. External acidification has 2 effects, a fast reversible block of the current and a slower irreversible enhancement of current inactivation. Is a highly temperature-sensitive, heat activated channel showing a steep increase of inward currents at temperatures between 15 and 35 degrees Celsius. Heat activation is due to a shift of the voltage-dependent activation curve to negative potentials. Activated by arachidonic acid in vitro. May be involved in perception of bitter, sweet and umami tastes. May also be involved in sensing semiochemicals. Ref.4 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16
Enzyme regulation	Phosphatidylinositol 4,5-bisphosphate (PIP2) is able to partially restore sensitivity to Ca2+ after desensitization. Inhibited by flufenamic acid with an IC50 of 24.5 µM and spermine with an IC50 of 37 µM. Ref.8 Ref.9
Subcellular location	Cell membrane; Multi-pass membrane protein Potential.
Tissue specificity	Strongly expressed in liver, heart, testis, brain and kidney. Detected in fetal liver, kidney, spleen, brain, heart and lung, and in adult skin, eyes, spleen, stomach, small intestine, colon, lung, bladder, pancreas and thymus. Biallelically expressed at all stages and tissues examined. Also expressed in subsets of taste receptor cells of the tongue, in olfactory sensory neurons of the main olfactory epithelium and in the vomeronasal organ. Ref.2 Ref.7 Ref.14 Ref.16
Disruption phenotype	Mice show diminished behavioral and nerve responses to bitter, sweet and umami tastes. Ref.13
Sequence similarities	Belongs to the transient receptor (TC 1.A.4) family. LTrpC subfamily. TRPM5 sub-subfamily. [View classification]
Sequence caution	The sequence CAB94717.2 differs from that shown. Reason: Frameshift at position 1130. The sequence CAC19456.1 differs from that shown. Reason: Frameshift at position 1130.

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Ion channel Ligand-gated ion channel Receptor Voltage-gated channel
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium activated cation channel activity Inferred from direct assay Ref.8. Source: MGI potassium channel activity Inferred from direct assay Ref.8. Source: MGI sodium channel activity Inferred from direct assay Ref.8. Source: MGI voltage-gated ion channel activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 (identifier: Q9JJH7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 Ref.3 (identifier: Q9JJH7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1108-1116: ANYCMLLLS → SKYGFRPWE
     1117-1158: Missing.

Isoform 3 Ref.4 (identifier: Q9JJH7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     978-1000: SYTFQVVQGNADMFWKFQRYHLI → RVLTETGPMSWYFAAVSSGLDLQ
     1001-1158: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1158	1158	Transient receptor potential cation channel subfamily M member 5		PRO_0000328934
Regions
	Topological domain	1 – 645	645	Cytoplasmic Potential
	Transmembrane	646 – 666	21	Helical; Potential
	Topological domain	667 – 732	66	Extracellular Potential
	Transmembrane	733 – 753	21	Helical; Potential
	Topological domain	754 – 810	57	Cytoplasmic Potential
	Transmembrane	811 – 831	21	Helical; Potential
	Topological domain	832 – 834	3	Extracellular Potential
	Transmembrane	835 – 855	21	Helical; Potential
	Topological domain	856 – 871	16	Cytoplasmic Potential
	Transmembrane	872 – 892	21	Helical; Potential
	Topological domain	893 – 953	61	Extracellular Potential
	Transmembrane	954 – 974	21	Helical; Potential
	Topological domain	975 – 1158	184	Cytoplasmic Potential
	Coiled coil	552 – 572	21	Potential
Natural variations
	Alternative sequence	978 – 1000	23	SYTFQ…RYHLI → RVLTETGPMSWYFAAVSSGL DLQ in isoform 3. Ref.4		VSP_052744
	Alternative sequence	1001 – 1158	158	Missing in isoform 3. Ref.4		VSP_052745
	Alternative sequence	1108 – 1116	9	ANYCMLLLS → SKYGFRPWE in isoform 2. Ref.3		VSP_052746
	Alternative sequence	1117 – 1158	42	Missing in isoform 2. Ref.3		VSP_052747
Experimental info
	Mutagenesis	831	1	E → Q: Reduces sensitivity to block by extracellular acidification. Sensitivity to block by low extracellular pH is nearly abolished; when associated with N-935. Ref.10
	Mutagenesis	897	1	H → N: Shows normal sensitivity to acid block and significant recovery from acid-enhanced inactivation. Ref.10
	Mutagenesis	935	1	H → N: Reduces sensitivity to block by extracellular acidification. Sensitivity to block by low extracellular pH is nearly abolished; when associated with Q-831. Ref.10
	Sequence conflict	24	1	C → S in AAI33713. Ref.5
	Sequence conflict	612	1	H → P in CAB94717. Ref.3
	Sequence conflict	871	1	D → E in BAE36157. Ref.6
	Sequence conflict	897	1	H → N in AAI33713. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: F0A5237EC67867CE	FASTA	1,158	130,844
	10 20 30 40 50 60 MQTTQSSCPG SPPDTEDGWE PILCRGEINF GGSGKKRGKF VKVPSSVAPS VLFELLLTEW 70 80 90 100 110 120 HLPAPNLVVS LVGEERPLAM KSWLRDVLRK GLVKAAQSTG AWILTSALHV GLARHVGQAV 130 140 150 160 170 180 RDHSLASTST KIRVVAIGMA SLDRILHRQL LDGVHQKEDT PIHYPADEGN IQGPLCPLDS 190 200 210 220 230 240 NLSHFILVES GALGSGNDGL TELQLSLEKH ISQQRTGYGG TSCIQIPVLC LLVNGDPNTL 250 260 270 280 290 300 ERISRAVEQA APWLILAGSG GIADVLAALV SQPHLLVPQV AEKQFREKFP SECFSWEAIV 310 320 330 340 350 360 HWTELLQNIA AHPHLLTVYD FEQEGSEDLD TVILKALVKA CKSHSQEAQD YLDELKLAVA 370 380 390 400 410 420 WDRVDIAKSE IFNGDVEWKS CDLEEVMTDA LVSNKPDFVR LFVDSGADMA EFLTYGRLQQ 430 440 450 460 470 480 LYHSVSPKSL LFELLQRKHE EGRLTLAGLG AQQARELPIG LPAFSLHEVS RVLKDFLHDA 490 500 510 520 530 540 CRGFYQDGRR MEERGPPKRP AGQKWLPDLS RKSEDPWRDL FLWAVLQNRY EMATYFWAMG 550 560 570 580 590 600 REGVAAALAA CKIIKEMSHL EKEAEVARTM REAKYEQLAL DLFSECYGNS EDRAFALLVR 610 620 630 640 650 660 RNHSWSRTTC LHLATEADAK AFFAHDGVQA FLTKIWWGDM ATGTPILRLL GAFTCPALIY 670 680 690 700 710 720 TNLISFSEDA PQRMDLEDLQ EPDSLDMEKS FLCSRGGQLE KLTEAPRAPG DLGPQAAFLL 730 740 750 760 770 780 TRWRKFWGAP VTVFLGNVVM YFAFLFLFTY VLLVDFRPPP QGPSGSEVTL YFWVFTLVLE 790 800 810 820 830 840 EIRQGFFTDE DTHLVKKFTL YVEDNWNKCD MVAIFLFIVG VTCRMVPSVF EAGRTVLAID 850 860 870 880 890 900 FMVFTLRLIH IFAIHKQLGP KIIIVERMMK DVFFFLFFLS VWLVAYGVTT QALLHPHDGR 910 920 930 940 950 960 LEWIFRRVLY RPYLQIFGQI PLDEIDEARV NCSLHPLLLE SSASCPNLYA NWLVILLLVT 970 980 990 1000 1010 1020 FLLVTNVLLM NLLIAMFSYT FQVVQGNADM FWKFQRYHLI VEYHGRPALA PPFILLSHLS 1030 1040 1050 1060 1070 1080 LVLKQVFRKE AQHKRQHLER DLPDPLDQKI ITWETVQKEN FLSTMEKRRR DSEGEVLRKT 1090 1100 1110 1120 1130 1140 AHRVDLIAKY IGGLREQEKR IKCLESQANY CMLLLSSMTD TLAPGGTYSS SQNCGCRSQP 1150 ASARDREYLE SGLPPSDT
	Isoform 2 [UniParc]. Checksum: 32DFFABCF2835E48	FASTA	1,116	126,609
	10 20 30 40 50 60 MQTTQSSCPG SPPDTEDGWE PILCRGEINF GGSGKKRGKF VKVPSSVAPS VLFELLLTEW 70 80 90 100 110 120 HLPAPNLVVS LVGEERPLAM KSWLRDVLRK GLVKAAQSTG AWILTSALHV GLARHVGQAV 130 140 150 160 170 180 RDHSLASTST KIRVVAIGMA SLDRILHRQL LDGVHQKEDT PIHYPADEGN IQGPLCPLDS 190 200 210 220 230 240 NLSHFILVES GALGSGNDGL TELQLSLEKH ISQQRTGYGG TSCIQIPVLC LLVNGDPNTL 250 260 270 280 290 300 ERISRAVEQA APWLILAGSG GIADVLAALV SQPHLLVPQV AEKQFREKFP SECFSWEAIV 310 320 330 340 350 360 HWTELLQNIA AHPHLLTVYD FEQEGSEDLD TVILKALVKA CKSHSQEAQD YLDELKLAVA 370 380 390 400 410 420 WDRVDIAKSE IFNGDVEWKS CDLEEVMTDA LVSNKPDFVR LFVDSGADMA EFLTYGRLQQ 430 440 450 460 470 480 LYHSVSPKSL LFELLQRKHE EGRLTLAGLG AQQARELPIG LPAFSLHEVS RVLKDFLHDA 490 500 510 520 530 540 CRGFYQDGRR MEERGPPKRP AGQKWLPDLS RKSEDPWRDL FLWAVLQNRY EMATYFWAMG 550 560 570 580 590 600 REGVAAALAA CKIIKEMSHL EKEAEVARTM REAKYEQLAL DLFSECYGNS EDRAFALLVR 610 620 630 640 650 660 RNHSWSRTTC LHLATEADAK AFFAHDGVQA FLTKIWWGDM ATGTPILRLL GAFTCPALIY 670 680 690 700 710 720 TNLISFSEDA PQRMDLEDLQ EPDSLDMEKS FLCSRGGQLE KLTEAPRAPG DLGPQAAFLL 730 740 750 760 770 780 TRWRKFWGAP VTVFLGNVVM YFAFLFLFTY VLLVDFRPPP QGPSGSEVTL YFWVFTLVLE 790 800 810 820 830 840 EIRQGFFTDE DTHLVKKFTL YVEDNWNKCD MVAIFLFIVG VTCRMVPSVF EAGRTVLAID 850 860 870 880 890 900 FMVFTLRLIH IFAIHKQLGP KIIIVERMMK DVFFFLFFLS VWLVAYGVTT QALLHPHDGR 910 920 930 940 950 960 LEWIFRRVLY RPYLQIFGQI PLDEIDEARV NCSLHPLLLE SSASCPNLYA NWLVILLLVT 970 980 990 1000 1010 1020 FLLVTNVLLM NLLIAMFSYT FQVVQGNADM FWKFQRYHLI VEYHGRPALA PPFILLSHLS 1030 1040 1050 1060 1070 1080 LVLKQVFRKE AQHKRQHLER DLPDPLDQKI ITWETVQKEN FLSTMEKRRR DSEGEVLRKT 1090 1100 1110 AHRVDLIAKY IGGLREQEKR IKCLESQSKY GFRPWE
	Isoform 3 [UniParc]. Checksum: BB107610176E6660	FASTA	1,000	112,460
	10 20 30 40 50 60 MQTTQSSCPG SPPDTEDGWE PILCRGEINF GGSGKKRGKF VKVPSSVAPS VLFELLLTEW 70 80 90 100 110 120 HLPAPNLVVS LVGEERPLAM KSWLRDVLRK GLVKAAQSTG AWILTSALHV GLARHVGQAV 130 140 150 160 170 180 RDHSLASTST KIRVVAIGMA SLDRILHRQL LDGVHQKEDT PIHYPADEGN IQGPLCPLDS 190 200 210 220 230 240 NLSHFILVES GALGSGNDGL TELQLSLEKH ISQQRTGYGG TSCIQIPVLC LLVNGDPNTL 250 260 270 280 290 300 ERISRAVEQA APWLILAGSG GIADVLAALV SQPHLLVPQV AEKQFREKFP SECFSWEAIV 310 320 330 340 350 360 HWTELLQNIA AHPHLLTVYD FEQEGSEDLD TVILKALVKA CKSHSQEAQD YLDELKLAVA 370 380 390 400 410 420 WDRVDIAKSE IFNGDVEWKS CDLEEVMTDA LVSNKPDFVR LFVDSGADMA EFLTYGRLQQ 430 440 450 460 470 480 LYHSVSPKSL LFELLQRKHE EGRLTLAGLG AQQARELPIG LPAFSLHEVS RVLKDFLHDA 490 500 510 520 530 540 CRGFYQDGRR MEERGPPKRP AGQKWLPDLS RKSEDPWRDL FLWAVLQNRY EMATYFWAMG 550 560 570 580 590 600 REGVAAALAA CKIIKEMSHL EKEAEVARTM REAKYEQLAL DLFSECYGNS EDRAFALLVR 610 620 630 640 650 660 RNHSWSRTTC LHLATEADAK AFFAHDGVQA FLTKIWWGDM ATGTPILRLL GAFTCPALIY 670 680 690 700 710 720 TNLISFSEDA PQRMDLEDLQ EPDSLDMEKS FLCSRGGQLE KLTEAPRAPG DLGPQAAFLL 730 740 750 760 770 780 TRWRKFWGAP VTVFLGNVVM YFAFLFLFTY VLLVDFRPPP QGPSGSEVTL YFWVFTLVLE 790 800 810 820 830 840 EIRQGFFTDE DTHLVKKFTL YVEDNWNKCD MVAIFLFIVG VTCRMVPSVF EAGRTVLAID 850 860 870 880 890 900 FMVFTLRLIH IFAIHKQLGP KIIIVERMMK DVFFFLFFLS VWLVAYGVTT QALLHPHDGR 910 920 930 940 950 960 LEWIFRRVLY RPYLQIFGQI PLDEIDEARV NCSLHPLLLE SSASCPNLYA NWLVILLLVT 970 980 990 1000 FLLVTNVLLM NLLIAMFRVL TETGPMSWYF AAVSSGLDLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence-based structural features between Kvlqt1 and Tapa1 on mouse chromosome 7F4/F5 corresponding to the Beckwith-Wiedemann syndrome region on human 11p15.5: long-stretches of unusually well conserved intronic sequences of kvlqt1 between mouse and human." Yatsuki H., Watanabe H., Hattori M., Joh K., Soejima H., Komoda H., Xin Z., Zhu X., Higashimoto K., Nishimura M., Kuratomi S., Sasaki H., Sakaki Y., Mukai T. DNA Res. 7:195-206(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Mtr1, a novel biallelically expressed gene in the center of the mouse distal chromosome 7 imprinting cluster, is a member of the Trp gene family." Enklaar T., Esswein M., Oswald M., Hilbert K., Winterpacht A., Higgins M., Zabel B., Prawitt D. Genomics 67:179-187(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]	"Sequence conservation and variability of imprinting in the Beckwith-Wiedemann syndrome gene cluster in human and mouse." Paulsen M., El-Maarri O., Engemann S., Stroedicke M., Franck O., Davies K., Reinhardt R., Reik W., Walter J. Hum. Mol. Genet. 9:1829-1841(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2). Strain: 129/Sv.
[4]	"TRPM5 is a voltage-modulated and Ca(2+)-activated monovalent selective cation channel." Hofmann T., Chubanov V., Gudermann T., Montell C. Curr. Biol. 13:1153-1158(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION. Tissue: Testis.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 441-1158 (ISOFORM 1). Strain: C57BL/6J. Tissue: Embryonic liver.
[7]	"A transient receptor potential channel expressed in taste receptor cells." Perez C.A., Huang L., Rong M., Kozak J.A., Preuss A.K., Zhang H., Max M., Margolskee R.F. Nat. Neurosci. 5:1169-1176(2002) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"Intracellular Ca2+ and the phospholipid PIP2 regulate the taste transduction ion channel TRPM5." Liu D., Liman E.R. Proc. Natl. Acad. Sci. U.S.A. 100:15160-15165(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[9]	"Comparison of functional properties of the Ca2+-activated cation channels TRPM4 and TRPM5 from mice." Ullrich N.D., Voets T., Prenen J., Vennekens R., Talavera K., Droogmans G., Nilius B. Cell Calcium 37:267-278(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[10]	"Extracellular acid block and acid-enhanced inactivation of the Ca2+-activated cation channel TRPM5 involve residues in the S3-S4 and S5-S6 extracellular domains." Liu D., Zhang Z., Liman E.R. J. Biol. Chem. 280:20691-20699(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLU-831; HIS-897 AND HIS-935.
[11]	"Heat activation of TRPM5 underlies thermal sensitivity of sweet taste." Talavera K., Yasumatsu K., Voets T., Droogmans G., Shigemura N., Ninomiya Y., Margolskee R.F., Nilius B. Nature 438:1022-1025(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Arachidonic acid can function as a signaling modulator by activating the TRPM5 cation channel in taste receptor cells." Oike H., Wakamori M., Mori Y., Nakanishi H., Taguchi R., Misaka T., Matsumoto I., Abe K. Biochim. Biophys. Acta 1761:1078-1084(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Trpm5 null mice respond to bitter, sweet, and umami compounds." Damak S., Rong M., Yasumatsu K., Kokrashvili Z., Perez C.A., Shigemura N., Yoshida R., Mosinger B. Jr., Glendinning J.I., Ninomiya Y., Margolskee R.F. Chem. Senses 31:253-264(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[14]	"TRPM5, a taste-signaling transient receptor potential ion-channel, is a ubiquitous signaling component in chemosensory cells." Kaske S., Krasteva G., Koenig P., Kummer W., Hofmann T., Gudermann T., Chubanov V. BMC Neurosci. 8:49-49(2007) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[15]	"The transduction channel TRPM5 is gated by intracellular calcium in taste cells." Zhang Z., Zhao Z., Margolskee R., Liman E. J. Neurosci. 27:5777-5786(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"Olfactory neurons expressing transient receptor potential channel M5 (TRPM5) are involved in sensing semiochemicals." Lin W., Margolskee R., Donnert G., Hell S.W., Restrepo D. Proc. Natl. Acad. Sci. U.S.A. 104:2471-2476(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB039952 mRNA. Translation: BAA96877.1. AF228681 mRNA. Translation: AAF98120.1. AJ251835 Genomic DNA. Translation: CAC19456.1. Frameshift. AJ251835 Genomic DNA. Translation: CAC19457.1. AJ271092 mRNA. Translation: CAB94717.2. Frameshift. AY280364 mRNA. Translation: AAP44476.1. AY280365 mRNA. Translation: AAP44477.1. BC133712 mRNA. Translation: AAI33713.1. AK161030 mRNA. Translation: BAE36157.1.
IPI	IPI00344348. IPI00886240. IPI00890160.
RefSeq	NP_064673.2. NM_020277.2.
UniGene	Mm.286668.
3D structure databases
ProteinModelPortal	Q9JJH7.
SMR	Q9JJH7. Positions 1078-1123.
ModBase	Search...
PTM databases
PhosphoSite	Q9JJH7.
Proteomic databases
PRIDE	Q9JJH7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000009390; ENSMUSP00000009390; ENSMUSG00000009246. ENSMUST00000150867; ENSMUSP00000114302; ENSMUSG00000009246.
GeneID	56843.
KEGG	mmu:56843.
UCSC	uc009koz.1. mouse.
Organism-specific databases
CTD	29850.
MGI	MGI:1861718. Trpm5.
Phylogenomic databases
eggNOG	NOG253824.
GeneTree	ENSGT00650000093200.
HOVERGEN	HBG108337.
InParanoid	Q9JJH7.
KO	K04980.
OMA	ECYSNSE.
OrthoDB	EOG47D9FD.
Gene expression databases
Bgee	Q9JJH7.
Genevestigator	Q9JJH7.
Family and domain databases
ProtoNet	Search...
Other
NextBio	313391.
SOURCE	Search...

Entry information

Entry name

TRPM5_MOUSE

Accession

Primary (citable) accession number: Q9JJH7
Secondary accession number(s): A3KN89 , Q3TU14, Q7TPL4, Q99NF9, Q9EPM3, Q9EPM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program