TRPM5_MOUSE
ID TRPM5_MOUSE Reviewed; 1158 AA.
AC Q9JJH7; A3KN89; Q3TU14; Q7TPL4; Q99NF9; Q9EPM3; Q9EPM4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Transient receptor potential cation channel subfamily M member 5;
DE AltName: Full=Long transient receptor potential channel 5;
DE Short=LTrpC-5;
DE Short=LTrpC5;
DE AltName: Full=MLSN1- and TRP-related gene 1 protein;
GN Name=Trpm5 {ECO:0000312|MGI:MGI:1861718};
GN Synonyms=Ltrpc5 {ECO:0000312|EMBL:CAB94717.2},
GN Mtr1 {ECO:0000312|EMBL:BAA96877.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA96877.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10907850; DOI=10.1093/dnares/7.3.195;
RA Yatsuki H., Watanabe H., Hattori M., Joh K., Soejima H., Komoda H., Xin Z.,
RA Zhu X., Higashimoto K., Nishimura M., Kuratomi S., Sasaki H., Sakaki Y.,
RA Mukai T.;
RT "Sequence-based structural features between Kvlqt1 and Tapa1 on mouse
RT chromosome 7F4/F5 corresponding to the Beckwith-Wiedemann syndrome region
RT on human 11p15.5: long-stretches of unusually well conserved intronic
RT sequences of kvlqt1 between mouse and human.";
RL DNA Res. 7:195-206(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF98120.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10903843; DOI=10.1006/geno.2000.6234;
RA Enklaar T., Esswein M., Oswald M., Hilbert K., Winterpacht A., Higgins M.,
RA Zabel B., Prawitt D.;
RT "Mtr1, a novel biallelically expressed gene in the center of the mouse
RT distal chromosome 7 imprinting cluster, is a member of the Trp gene
RT family.";
RL Genomics 67:179-187(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAB94717.2}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RC STRAIN=129/Sv {ECO:0000312|EMBL:CAB94717.2};
RX PubMed=10915772; DOI=10.1093/hmg/9.12.1829;
RA Paulsen M., El-Maarri O., Engemann S., Stroedicke M., Franck O., Davies K.,
RA Reinhardt R., Reik W., Walter J.;
RT "Sequence conservation and variability of imprinting in the Beckwith-
RT Wiedemann syndrome gene cluster in human and mouse.";
RL Hum. Mol. Genet. 9:1829-1841(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAP44476.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND FUNCTION.
RC TISSUE=Testis {ECO:0000312|EMBL:AAP44477.1};
RX PubMed=12842017; DOI=10.1016/s0960-9822(03)00431-7;
RA Hofmann T., Chubanov V., Gudermann T., Montell C.;
RT "TRPM5 is a voltage-modulated and Ca(2+)-activated monovalent selective
RT cation channel.";
RL Curr. Biol. 13:1153-1158(2003).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAI33713.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6] {ECO:0000305, ECO:0000312|EMBL:BAE36157.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 441-1158 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE36157.1};
RC TISSUE=Embryonic liver {ECO:0000312|EMBL:BAE36157.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=12368808; DOI=10.1038/nn952;
RA Perez C.A., Huang L., Rong M., Kozak J.A., Preuss A.K., Zhang H., Max M.,
RA Margolskee R.F.;
RT "A transient receptor potential channel expressed in taste receptor
RT cells.";
RL Nat. Neurosci. 5:1169-1176(2002).
RN [8] {ECO:0000305}
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=14657398; DOI=10.1073/pnas.2334159100;
RA Liu D., Liman E.R.;
RT "Intracellular Ca2+ and the phospholipid PIP2 regulate the taste
RT transduction ion channel TRPM5.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15160-15165(2003).
RN [9] {ECO:0000305}
RP ACTIVITY REGULATION.
RX PubMed=15670874; DOI=10.1016/j.ceca.2004.11.001;
RA Ullrich N.D., Voets T., Prenen J., Vennekens R., Talavera K., Droogmans G.,
RA Nilius B.;
RT "Comparison of functional properties of the Ca2+-activated cation channels
RT TRPM4 and TRPM5 from mice.";
RL Cell Calcium 37:267-278(2005).
RN [10] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLU-831; HIS-897 AND HIS-935.
RX PubMed=15731110; DOI=10.1074/jbc.m414072200;
RA Liu D., Zhang Z., Liman E.R.;
RT "Extracellular acid block and acid-enhanced inactivation of the Ca2+-
RT activated cation channel TRPM5 involve residues in the S3-S4 and S5-S6
RT extracellular domains.";
RL J. Biol. Chem. 280:20691-20699(2005).
RN [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=16355226; DOI=10.1038/nature04248;
RA Talavera K., Yasumatsu K., Voets T., Droogmans G., Shigemura N.,
RA Ninomiya Y., Margolskee R.F., Nilius B.;
RT "Heat activation of TRPM5 underlies thermal sensitivity of sweet taste.";
RL Nature 438:1022-1025(2005).
RN [12] {ECO:0000305}
RP FUNCTION.
RX PubMed=16935556; DOI=10.1016/j.bbalip.2006.07.005;
RA Oike H., Wakamori M., Mori Y., Nakanishi H., Taguchi R., Misaka T.,
RA Matsumoto I., Abe K.;
RT "Arachidonic acid can function as a signaling modulator by activating the
RT TRPM5 cation channel in taste receptor cells.";
RL Biochim. Biophys. Acta 1761:1078-1084(2006).
RN [13] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16436689; DOI=10.1093/chemse/bjj027;
RA Damak S., Rong M., Yasumatsu K., Kokrashvili Z., Perez C.A., Shigemura N.,
RA Yoshida R., Mosinger B. Jr., Glendinning J.I., Ninomiya Y.,
RA Margolskee R.F.;
RT "Trpm5 null mice respond to bitter, sweet, and umami compounds.";
RL Chem. Senses 31:253-264(2006).
RN [14] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=17610722; DOI=10.1186/1471-2202-8-49;
RA Kaske S., Krasteva G., Koenig P., Kummer W., Hofmann T., Gudermann T.,
RA Chubanov V.;
RT "TRPM5, a taste-signaling transient receptor potential ion-channel, is a
RT ubiquitous signaling component in chemosensory cells.";
RL BMC Neurosci. 8:49-49(2007).
RN [15] {ECO:0000305}
RP FUNCTION.
RX PubMed=17522321; DOI=10.1523/jneurosci.4973-06.2007;
RA Zhang Z., Zhao Z., Margolskee R., Liman E.;
RT "The transduction channel TRPM5 is gated by intracellular calcium in taste
RT cells.";
RL J. Neurosci. 27:5777-5786(2007).
RN [16] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17267604; DOI=10.1073/pnas.0610201104;
RA Lin W., Margolskee R., Donnert G., Hell S.W., Restrepo D.;
RT "Olfactory neurons expressing transient receptor potential channel M5
RT (TRPM5) are involved in sensing semiochemicals.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2471-2476(2007).
CC -!- FUNCTION: Voltage-modulated Ca(2+)-activated, monovalent cation channel
CC (VCAM) that mediates a transient membrane depolarization and plays a
CC central role in taste transduction. Monovalent-specific, non-selective
CC cation channel that mediates the transport of Na(+), K(+) and Cs(+)
CC ions equally well. Activated directly by increases in intracellular
CC Ca(2+), but is impermeable to it. Gating is voltage-dependent and
CC displays rapid activation and deactivation kinetics upon channel
CC stimulation even during sustained elevations in Ca(2+). Also activated
CC by a fast intracellular Ca(2+) increase in response to inositol 1,4,5-
CC triphosphate-producing receptor agonists. The channel is blocked by
CC extracellular acidification. External acidification has 2 effects, a
CC fast reversible block of the current and a slower irreversible
CC enhancement of current inactivation. Is a highly temperature-sensitive,
CC heat activated channel showing a steep increase of inward currents at
CC temperatures between 15 and 35 degrees Celsius. Heat activation is due
CC to a shift of the voltage-dependent activation curve to negative
CC potentials. Activated by arachidonic acid in vitro. May be involved in
CC perception of bitter, sweet and umami tastes. May also be involved in
CC sensing semiochemicals. {ECO:0000269|PubMed:12842017,
CC ECO:0000269|PubMed:14657398, ECO:0000269|PubMed:15731110,
CC ECO:0000269|PubMed:16355226, ECO:0000269|PubMed:16436689,
CC ECO:0000269|PubMed:16935556, ECO:0000269|PubMed:17267604,
CC ECO:0000269|PubMed:17522321}.
CC -!- ACTIVITY REGULATION: Phosphatidylinositol 4,5-bisphosphate (PIP2) is
CC able to partially restore sensitivity to Ca(2+) after desensitization.
CC Inhibited by flufenamic acid with an IC(50) of 24.5 uM and spermine
CC with an IC(50) of 37 uM. {ECO:0000269|PubMed:14657398,
CC ECO:0000269|PubMed:15670874}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q8TD43, ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:10903843, ECO:0000269|PubMed:10907850,
CC ECO:0000269|PubMed:10915772, ECO:0000269|PubMed:12842017,
CC ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=Q9JJH7-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10915772};
CC IsoId=Q9JJH7-2; Sequence=VSP_052746, VSP_052747;
CC Name=3 {ECO:0000269|PubMed:12842017};
CC IsoId=Q9JJH7-3; Sequence=VSP_052744, VSP_052745;
CC -!- TISSUE SPECIFICITY: Strongly expressed in liver, heart, testis, brain
CC and kidney. Detected in fetal liver, kidney, spleen, brain, heart and
CC lung, and in adult skin, eyes, spleen, stomach, small intestine, colon,
CC lung, bladder, pancreas and thymus. Biallelically expressed at all
CC stages and tissues examined. Also expressed in subsets of taste
CC receptor cells of the tongue, in olfactory sensory neurons of the main
CC olfactory epithelium and in the vomeronasal organ.
CC {ECO:0000269|PubMed:10903843, ECO:0000269|PubMed:12368808,
CC ECO:0000269|PubMed:17267604, ECO:0000269|PubMed:17610722}.
CC -!- DISRUPTION PHENOTYPE: Mice show diminished behavioral and nerve
CC responses to bitter, sweet and umami tastes.
CC {ECO:0000269|PubMed:16436689}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. LTrpC
CC subfamily. TRPM5 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB94717.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAC19456.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB039952; BAA96877.1; -; mRNA.
DR EMBL; AF228681; AAF98120.1; -; mRNA.
DR EMBL; AJ251835; CAC19456.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AJ251835; CAC19457.1; -; Genomic_DNA.
DR EMBL; AJ271092; CAB94717.2; ALT_FRAME; mRNA.
DR EMBL; AY280364; AAP44476.1; -; mRNA.
DR EMBL; AY280365; AAP44477.1; -; mRNA.
DR EMBL; BC133712; AAI33713.1; -; mRNA.
DR EMBL; AK161030; BAE36157.1; -; mRNA.
DR CCDS; CCDS52462.1; -. [Q9JJH7-1]
DR RefSeq; NP_064673.2; NM_020277.2. [Q9JJH7-1]
DR RefSeq; XP_006508708.1; XM_006508645.1. [Q9JJH7-1]
DR RefSeq; XP_006508709.1; XM_006508646.3. [Q9JJH7-3]
DR AlphaFoldDB; Q9JJH7; -.
DR SMR; Q9JJH7; -.
DR BioGRID; 208190; 1.
DR STRING; 10090.ENSMUSP00000009390; -.
DR ChEMBL; CHEMBL3886124; -.
DR GuidetoPHARMACOLOGY; 497; -.
DR iPTMnet; Q9JJH7; -.
DR PhosphoSitePlus; Q9JJH7; -.
DR PaxDb; Q9JJH7; -.
DR PRIDE; Q9JJH7; -.
DR ProteomicsDB; 300022; -. [Q9JJH7-1]
DR ProteomicsDB; 300023; -. [Q9JJH7-2]
DR ProteomicsDB; 300024; -. [Q9JJH7-3]
DR Antibodypedia; 23152; 165 antibodies from 30 providers.
DR DNASU; 56843; -.
DR Ensembl; ENSMUST00000009390; ENSMUSP00000009390; ENSMUSG00000009246. [Q9JJH7-1]
DR Ensembl; ENSMUST00000150867; ENSMUSP00000114302; ENSMUSG00000009246. [Q9JJH7-3]
DR GeneID; 56843; -.
DR KEGG; mmu:56843; -.
DR UCSC; uc009koz.1; mouse. [Q9JJH7-1]
DR CTD; 29850; -.
DR MGI; MGI:1861718; Trpm5.
DR VEuPathDB; HostDB:ENSMUSG00000009246; -.
DR eggNOG; KOG3614; Eukaryota.
DR GeneTree; ENSGT00940000160588; -.
DR HOGENOM; CLU_001390_0_1_1; -.
DR InParanoid; Q9JJH7; -.
DR OMA; ICYCTAV; -.
DR OrthoDB; 738147at2759; -.
DR PhylomeDB; Q9JJH7; -.
DR TreeFam; TF314204; -.
DR Reactome; R-MMU-3295583; TRP channels.
DR BioGRID-ORCS; 56843; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Trpm5; mouse.
DR PRO; PR:Q9JJH7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JJH7; protein.
DR Bgee; ENSMUSG00000009246; Expressed in islet of Langerhans and 85 other tissues.
DR ExpressionAtlas; Q9JJH7; baseline and differential.
DR Genevisible; Q9JJH7; MM.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005227; F:calcium activated cation channel activity; IDA:MGI.
DR GO; GO:0005261; F:cation channel activity; IBA:GO_Central.
DR GO; GO:0099604; F:ligand-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; IDA:MGI.
DR GO; GO:0005272; F:sodium channel activity; IDA:MGI.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0050909; P:sensory perception of taste; IEA:InterPro.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR029577; TRPM5.
DR InterPro; IPR041491; TRPM_SLOG.
DR PANTHER; PTHR13800:SF5; PTHR13800:SF5; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF18139; LSDAT_euk; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Coiled coil; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..1158
FT /note="Transient receptor potential cation channel
FT subfamily M member 5"
FT /id="PRO_0000328934"
FT TOPO_DOM 1..645
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 667..732
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 733..753
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 754..810
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 811..831
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 832..834
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 835..855
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 856..871
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 872..892
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 893..953
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 954..974
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 975..1158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 488..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 552..572
FT /evidence="ECO:0000255"
FT VAR_SEQ 978..1000
FT /note="SYTFQVVQGNADMFWKFQRYHLI -> RVLTETGPMSWYFAAVSSGLDLQ
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12842017"
FT /id="VSP_052744"
FT VAR_SEQ 1001..1158
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12842017"
FT /id="VSP_052745"
FT VAR_SEQ 1108..1116
FT /note="ANYCMLLLS -> SKYGFRPWE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10915772"
FT /id="VSP_052746"
FT VAR_SEQ 1117..1158
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10915772"
FT /id="VSP_052747"
FT MUTAGEN 831
FT /note="E->Q: Reduces sensitivity to block by extracellular
FT acidification. Sensitivity to block by low extracellular pH
FT is nearly abolished; when associated with N-935."
FT /evidence="ECO:0000269|PubMed:15731110"
FT MUTAGEN 897
FT /note="H->N: Shows normal sensitivity to acid block and
FT significant recovery from acid-enhanced inactivation."
FT /evidence="ECO:0000269|PubMed:15731110"
FT MUTAGEN 935
FT /note="H->N: Reduces sensitivity to block by extracellular
FT acidification. Sensitivity to block by low extracellular pH
FT is nearly abolished; when associated with Q-831."
FT /evidence="ECO:0000269|PubMed:15731110"
FT CONFLICT 24
FT /note="C -> S (in Ref. 5; AAI33713)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="H -> P (in Ref. 3; CAB94717)"
FT /evidence="ECO:0000305"
FT CONFLICT 871
FT /note="D -> E (in Ref. 6; BAE36157)"
FT /evidence="ECO:0000305"
FT CONFLICT 897
FT /note="H -> N (in Ref. 5; AAI33713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1158 AA; 130844 MW; F0A5237EC67867CE CRC64;
MQTTQSSCPG SPPDTEDGWE PILCRGEINF GGSGKKRGKF VKVPSSVAPS VLFELLLTEW
HLPAPNLVVS LVGEERPLAM KSWLRDVLRK GLVKAAQSTG AWILTSALHV GLARHVGQAV
RDHSLASTST KIRVVAIGMA SLDRILHRQL LDGVHQKEDT PIHYPADEGN IQGPLCPLDS
NLSHFILVES GALGSGNDGL TELQLSLEKH ISQQRTGYGG TSCIQIPVLC LLVNGDPNTL
ERISRAVEQA APWLILAGSG GIADVLAALV SQPHLLVPQV AEKQFREKFP SECFSWEAIV
HWTELLQNIA AHPHLLTVYD FEQEGSEDLD TVILKALVKA CKSHSQEAQD YLDELKLAVA
WDRVDIAKSE IFNGDVEWKS CDLEEVMTDA LVSNKPDFVR LFVDSGADMA EFLTYGRLQQ
LYHSVSPKSL LFELLQRKHE EGRLTLAGLG AQQARELPIG LPAFSLHEVS RVLKDFLHDA
CRGFYQDGRR MEERGPPKRP AGQKWLPDLS RKSEDPWRDL FLWAVLQNRY EMATYFWAMG
REGVAAALAA CKIIKEMSHL EKEAEVARTM REAKYEQLAL DLFSECYGNS EDRAFALLVR
RNHSWSRTTC LHLATEADAK AFFAHDGVQA FLTKIWWGDM ATGTPILRLL GAFTCPALIY
TNLISFSEDA PQRMDLEDLQ EPDSLDMEKS FLCSRGGQLE KLTEAPRAPG DLGPQAAFLL
TRWRKFWGAP VTVFLGNVVM YFAFLFLFTY VLLVDFRPPP QGPSGSEVTL YFWVFTLVLE
EIRQGFFTDE DTHLVKKFTL YVEDNWNKCD MVAIFLFIVG VTCRMVPSVF EAGRTVLAID
FMVFTLRLIH IFAIHKQLGP KIIIVERMMK DVFFFLFFLS VWLVAYGVTT QALLHPHDGR
LEWIFRRVLY RPYLQIFGQI PLDEIDEARV NCSLHPLLLE SSASCPNLYA NWLVILLLVT
FLLVTNVLLM NLLIAMFSYT FQVVQGNADM FWKFQRYHLI VEYHGRPALA PPFILLSHLS
LVLKQVFRKE AQHKRQHLER DLPDPLDQKI ITWETVQKEN FLSTMEKRRR DSEGEVLRKT
AHRVDLIAKY IGGLREQEKR IKCLESQANY CMLLLSSMTD TLAPGGTYSS SQNCGCRSQP
ASARDREYLE SGLPPSDT
