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Q9JJH7

- TRPM5_MOUSE

UniProt

Q9JJH7 - TRPM5_MOUSE

Protein

Transient receptor potential cation channel subfamily M member 5

Gene

Trpm5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    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.8 Publications

    Enzyme regulationi

    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.2 Publications

    GO - Molecular functioni

    1. calcium activated cation channel activity Source: MGI
    2. potassium channel activity Source: MGI
    3. sodium channel activity Source: MGI
    4. voltage-gated ion channel activity Source: UniProtKB-KW

    GO - Biological processi

    1. cation transport Source: GOC
    2. ion transmembrane transport Source: MGI
    3. potassium ion transmembrane transport Source: GOC
    4. sodium ion transmembrane transport Source: GOC

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor, Voltage-gated channel

    Keywords - Biological processi

    Ion transport, Transport

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_227861. TRP channels.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:Trpm5Imported
    Synonyms:Ltrpc5Imported, Mtr1Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1861718. Trpm5.

    Subcellular locationi

    Cell membrane Sequence Analysis; Multi-pass membrane protein By similaritySequence Analysis

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice show diminished behavioral and nerve responses to bitter, sweet and umami tastes.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi831 – 8311E → Q: Reduces sensitivity to block by extracellular acidification. Sensitivity to block by low extracellular pH is nearly abolished; when associated with N-935. 1 Publication
    Mutagenesisi897 – 8971H → N: Shows normal sensitivity to acid block and significant recovery from acid-enhanced inactivation. 1 Publication
    Mutagenesisi935 – 9351H → N: Reduces sensitivity to block by extracellular acidification. Sensitivity to block by low extracellular pH is nearly abolished; when associated with Q-831. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11581158Transient receptor potential cation channel subfamily M member 5PRO_0000328934Add
    BLAST

    Proteomic databases

    PRIDEiQ9JJH7.

    PTM databases

    PhosphoSiteiQ9JJH7.

    Expressioni

    Tissue specificityi

    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.4 Publications

    Gene expression databases

    BgeeiQ9JJH7.
    GenevestigatoriQ9JJH7.

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 645645CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini667 – 73266ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini754 – 81057CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini832 – 8343ExtracellularSequence Analysis
    Topological domaini856 – 87116CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini893 – 95361ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini975 – 1158184CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei646 – 66621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei733 – 75321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei811 – 83121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei835 – 85521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei872 – 89221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei954 – 97421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili552 – 57221Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG253824.
    GeneTreeiENSGT00650000093200.
    HOVERGENiHBG108337.
    InParanoidiQ9JJH7.
    KOiK04980.
    OMAiECYSNSE.
    OrthoDBiEOG725DH1.
    PhylomeDBiQ9JJH7.
    TreeFamiTF314204.

    Family and domain databases

    InterProiIPR029577. TRPM5.
    [Graphical view]
    PANTHERiPTHR13800:SF5. PTHR13800:SF5. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 16 Publications (identifier: Q9JJH7-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MQTTQSSCPG SPPDTEDGWE PILCRGEINF GGSGKKRGKF VKVPSSVAPS     50
    VLFELLLTEW HLPAPNLVVS LVGEERPLAM KSWLRDVLRK GLVKAAQSTG 100
    AWILTSALHV GLARHVGQAV RDHSLASTST KIRVVAIGMA SLDRILHRQL 150
    LDGVHQKEDT PIHYPADEGN IQGPLCPLDS NLSHFILVES GALGSGNDGL 200
    TELQLSLEKH ISQQRTGYGG TSCIQIPVLC LLVNGDPNTL ERISRAVEQA 250
    APWLILAGSG GIADVLAALV SQPHLLVPQV AEKQFREKFP SECFSWEAIV 300
    HWTELLQNIA AHPHLLTVYD FEQEGSEDLD TVILKALVKA CKSHSQEAQD 350
    YLDELKLAVA WDRVDIAKSE IFNGDVEWKS CDLEEVMTDA LVSNKPDFVR 400
    LFVDSGADMA EFLTYGRLQQ LYHSVSPKSL LFELLQRKHE EGRLTLAGLG 450
    AQQARELPIG LPAFSLHEVS RVLKDFLHDA CRGFYQDGRR MEERGPPKRP 500
    AGQKWLPDLS RKSEDPWRDL FLWAVLQNRY EMATYFWAMG REGVAAALAA 550
    CKIIKEMSHL EKEAEVARTM REAKYEQLAL DLFSECYGNS EDRAFALLVR 600
    RNHSWSRTTC LHLATEADAK AFFAHDGVQA FLTKIWWGDM ATGTPILRLL 650
    GAFTCPALIY TNLISFSEDA PQRMDLEDLQ EPDSLDMEKS FLCSRGGQLE 700
    KLTEAPRAPG DLGPQAAFLL TRWRKFWGAP VTVFLGNVVM YFAFLFLFTY 750
    VLLVDFRPPP QGPSGSEVTL YFWVFTLVLE EIRQGFFTDE DTHLVKKFTL 800
    YVEDNWNKCD MVAIFLFIVG VTCRMVPSVF EAGRTVLAID FMVFTLRLIH 850
    IFAIHKQLGP KIIIVERMMK DVFFFLFFLS VWLVAYGVTT QALLHPHDGR 900
    LEWIFRRVLY RPYLQIFGQI PLDEIDEARV NCSLHPLLLE SSASCPNLYA 950
    NWLVILLLVT FLLVTNVLLM NLLIAMFSYT FQVVQGNADM FWKFQRYHLI 1000
    VEYHGRPALA PPFILLSHLS LVLKQVFRKE AQHKRQHLER DLPDPLDQKI 1050
    ITWETVQKEN FLSTMEKRRR DSEGEVLRKT AHRVDLIAKY IGGLREQEKR 1100
    IKCLESQANY CMLLLSSMTD TLAPGGTYSS SQNCGCRSQP ASARDREYLE 1150
    SGLPPSDT 1158
    Length:1,158
    Mass (Da):130,844
    Last modified:October 1, 2000 - v1
    Checksum:iF0A5237EC67867CE
    GO
    Isoform 21 Publication (identifier: Q9JJH7-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,116
    Mass (Da):126,609
    Checksum:i32DFFABCF2835E48
    GO
    Isoform 31 Publication (identifier: Q9JJH7-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,000
    Mass (Da):112,460
    Checksum:iBB107610176E6660
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241C → S in AAI33713. (PubMed:15489334)Curated
    Sequence conflicti612 – 6121H → P in CAB94717. (PubMed:10915772)Curated
    Sequence conflicti871 – 8711D → E in BAE36157. (PubMed:16141072)Curated
    Sequence conflicti897 – 8971H → N in AAI33713. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei978 – 100023SYTFQ…RYHLI → RVLTETGPMSWYFAAVSSGL DLQ in isoform 3. 1 PublicationVSP_052744Add
    BLAST
    Alternative sequencei1001 – 1158158Missing in isoform 3. 1 PublicationVSP_052745Add
    BLAST
    Alternative sequencei1108 – 11169ANYCMLLLS → SKYGFRPWE in isoform 2. 1 PublicationVSP_052746
    Alternative sequencei1117 – 115842Missing in isoform 2. 1 PublicationVSP_052747Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS52462.1. [Q9JJH7-1]
    RefSeqiNP_064673.2. NM_020277.2. [Q9JJH7-1]
    XP_006508708.1. XM_006508645.1. [Q9JJH7-1]
    XP_006508709.1. XM_006508646.1. [Q9JJH7-3]
    UniGeneiMm.286668.

    Genome annotation databases

    EnsembliENSMUST00000009390; ENSMUSP00000009390; ENSMUSG00000009246. [Q9JJH7-1]
    ENSMUST00000150867; ENSMUSP00000114302; ENSMUSG00000009246. [Q9JJH7-3]
    GeneIDi56843.
    KEGGimmu:56843.
    UCSCiuc009koz.1. mouse. [Q9JJH7-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS52462.1. [Q9JJH7-1 ]
    RefSeqi NP_064673.2. NM_020277.2. [Q9JJH7-1 ]
    XP_006508708.1. XM_006508645.1. [Q9JJH7-1 ]
    XP_006508709.1. XM_006508646.1. [Q9JJH7-3 ]
    UniGenei Mm.286668.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Chemistry

    GuidetoPHARMACOLOGYi 497.

    PTM databases

    PhosphoSitei Q9JJH7.

    Proteomic databases

    PRIDEi Q9JJH7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000009390 ; ENSMUSP00000009390 ; ENSMUSG00000009246 . [Q9JJH7-1 ]
    ENSMUST00000150867 ; ENSMUSP00000114302 ; ENSMUSG00000009246 . [Q9JJH7-3 ]
    GeneIDi 56843.
    KEGGi mmu:56843.
    UCSCi uc009koz.1. mouse. [Q9JJH7-1 ]

    Organism-specific databases

    CTDi 29850.
    MGIi MGI:1861718. Trpm5.

    Phylogenomic databases

    eggNOGi NOG253824.
    GeneTreei ENSGT00650000093200.
    HOVERGENi HBG108337.
    InParanoidi Q9JJH7.
    KOi K04980.
    OMAi ECYSNSE.
    OrthoDBi EOG725DH1.
    PhylomeDBi Q9JJH7.
    TreeFami TF314204.

    Enzyme and pathway databases

    Reactomei REACT_227861. TRP channels.

    Miscellaneous databases

    NextBioi 313391.
    PROi Q9JJH7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9JJH7.
    Genevestigatori Q9JJH7.

    Family and domain databases

    InterProi IPR029577. TRPM5.
    [Graphical view ]
    PANTHERi PTHR13800:SF5. PTHR13800:SF5. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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/SvImported.
    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: TestisImported.
    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/6JImported.
      Tissue: Embryonic liverImported.
    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. 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.

    Entry informationi

    Entry nameiTRPM5_MOUSE
    AccessioniPrimary (citable) accession number: Q9JJH7
    Secondary accession number(s): A3KN89
    , Q3TU14, Q7TPL4, Q99NF9, Q9EPM3, Q9EPM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 90 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

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3