PK1L3_MOUSE
ID PK1L3_MOUSE Reviewed; 2201 AA.
AC Q2EG98; E9QPA5; Q2EG93; Q2EG94; Q2EG95; Q2EG96; Q2EG97; Q2EG99; Q7TN87;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Polycystic kidney disease protein 1-like 3;
DE AltName: Full=PC1-like 3 protein;
DE AltName: Full=Polycystin-1L3;
DE Flags: Precursor;
GN Name=Pkd1l3; ORFNames=71B10;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), AND ALTERNATIVE SPLICING.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=12782129; DOI=10.1016/s0888-7543(03)00048-x;
RA Li A., Tian X., Sung S.-W., Somlo S.;
RT "Identification of two novel polycystic kidney disease-1-like genes in
RT human and mouse genomes.";
RL Genomics 81:596-608(2003).
RN [2]
RP ERRATUM OF PUBMED:12782129.
RA Li A., Tian X., Sung S.-W., Somlo S.;
RL Genomics 82:498-500(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 6), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 1405-2201 (ISOFORMS 3; 4 AND 5), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 829-2201 (ISOFORM 7), FUNCTION, ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Taste bud;
RX PubMed=16805797; DOI=10.1111/j.1471-4159.2006.03842.x;
RA LopezJimenez N.D., Cavenagh M.M., Sainz E., Cruz-Ithier M.A., Battey J.F.,
RA Sullivan S.L.;
RT "Two members of the TRPP family of ion channels, Pkd1l3 and Pkd2l1, are co-
RT expressed in a subset of taste receptor cells.";
RL J. Neurochem. 98:68-77(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16929298; DOI=10.1038/nature05084;
RA Huang A.L., Chen X., Hoon M.A., Chandrashekar J., Guo W., Trankner D.,
RA Ryba N.J., Zuker C.S.;
RT "The cells and logic for mammalian sour taste detection.";
RL Nature 442:934-938(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PKD2L1, AND TISSUE
RP SPECIFICITY.
RX PubMed=16891422; DOI=10.1073/pnas.0602702103;
RA Ishimaru Y., Inada H., Kubota M., Zhuang H., Tominaga M., Matsunami H.;
RT "Transient receptor potential family members PKD1L3 and PKD2L1 form a
RT candidate sour taste receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12569-12574(2006).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=20605874; DOI=10.1093/chemse/bjq070;
RA Nelson T.M., Lopezjimenez N.D., Tessarollo L., Inoue M., Bachmanov A.A.,
RA Sullivan S.L.;
RT "Taste function in mice with a targeted mutation of the pkd1l3 gene.";
RL Chem. Senses 35:565-577(2010).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=20406802; DOI=10.1074/jbc.c110.132944;
RA Kawaguchi H., Yamanaka A., Uchida K., Shibasaki K., Sokabe T., Maruyama Y.,
RA Yanagawa Y., Murakami S., Tominaga M.;
RT "Activation of polycystic kidney disease-2-like 1 (PKD2L1)-PKD1L3 complex
RT by acid in mouse taste cells.";
RL J. Biol. Chem. 285:17277-17281(2010).
RN [9]
RP FUNCTION.
RX PubMed=21098668; DOI=10.1073/pnas.1013664107;
RA Chang R.B., Waters H., Liman E.R.;
RT "A proton current drives action potentials in genetically identified sour
RT taste cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:22320-22325(2010).
RN [10]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-2059 AND GLU-2082.
RX PubMed=21185261; DOI=10.1016/j.bbrc.2010.12.086;
RA Fujimoto C., Ishimaru Y., Katano Y., Misaka T., Yamasoba T., Asakura T.,
RA Abe K.;
RT "The single pore residue Asp523 in PKD2L1 determines Ca2+ permeation of the
RT PKD1L3/PKD2L1 complex.";
RL Biochem. Biophys. Res. Commun. 404:946-951(2011).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21625513; DOI=10.1371/journal.pone.0020007;
RA Horio N., Yoshida R., Yasumatsu K., Yanagawa Y., Ishimaru Y., Matsunami H.,
RA Ninomiya Y.;
RT "Sour taste responses in mice lacking PKD channels.";
RL PLoS ONE 6:E20007-E20007(2011).
CC -!- FUNCTION: Component of a calcium channel. May act as a sour taste
CC receptor by forming a calcium channel with PKD1L3 in gustatory cells;
CC however, its contribution to sour taste perception is unclear in vivo
CC and may be indirect. {ECO:0000269|PubMed:16805797,
CC ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:16929298,
CC ECO:0000269|PubMed:21098668, ECO:0000269|PubMed:21625513}.
CC -!- ACTIVITY REGULATION: The calcium channel is gated following an off-
CC response property by acid: gated open after the removal of acid
CC stimulus, but not during acid application.
CC {ECO:0000269|PubMed:20406802}.
CC -!- SUBUNIT: Calcium channels are probably composed of 3 subunit of PKD2L1
CC and 1 subunit of PKD1L3.
CC -!- INTERACTION:
CC Q2EG98; A2A259: Pkd2l1; NbExp=2; IntAct=EBI-15594779, EBI-15594711;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16891422,
CC ECO:0000269|PubMed:21185261}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:21185261}.
CC Note=Interaction with PKD2L1 is required for localization to the cell
CC membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=Variant 1a;
CC IsoId=Q2EG98-1; Sequence=Displayed;
CC Name=2; Synonyms=Variant 1b;
CC IsoId=Q2EG98-2; Sequence=VSP_031953, VSP_031954;
CC Name=3; Synonyms=Variant 2;
CC IsoId=Q2EG98-3; Sequence=VSP_031961;
CC Name=4; Synonyms=Variant 3;
CC IsoId=Q2EG98-4; Sequence=VSP_031962;
CC Name=5; Synonyms=Variant 4;
CC IsoId=Q2EG98-5; Sequence=VSP_031959;
CC Name=6; Synonyms=Variant 5;
CC IsoId=Q2EG98-6; Sequence=VSP_031952, VSP_031953, VSP_031954,
CC VSP_031955, VSP_031958;
CC Name=7; Synonyms=Variant 6;
CC IsoId=Q2EG98-7; Sequence=VSP_031956, VSP_031957;
CC Name=8;
CC IsoId=Q2EG98-8; Sequence=VSP_031953, VSP_031954, VSP_031960;
CC -!- TISSUE SPECIFICITY: Expressed in a subset of taste receptor cells
CC distinct from those involved in bitter, sweet and umami taste.
CC Expressed in circumvallate and foliate taste buds, but not in
CC surrounding non-gustatory lingual epithelium cells. Expressed in
CC testis. {ECO:0000269|PubMed:16805797, ECO:0000269|PubMed:16891422,
CC ECO:0000269|PubMed:16929298}.
CC -!- DISRUPTION PHENOTYPE: No significant reduction in taste responsiveness:
CC mice have normal nerve and behavioral responses to sour stimuli.
CC {ECO:0000269|PubMed:20605874, ECO:0000269|PubMed:21625513}.
CC -!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
CC -!- CAUTION: Pkd1l3 and Pkd2l1 have been identified as sour taste receptor
CC in gustatory cells based on a number of indirect evidences: Pkd2l1 is
CC expressed in circumvallate papillae cells on the posterior part of the
CC tongue distinct from those responsible for sweet, bitter and unami
CC taste and genetic elimination of cells expressing Pkd2l1 reduces
CC gustatory nerve responses to sour taste stimuli (PubMed:16891422,
CC PubMed:16929298). However, a number of experiments have recently shown
CC that the sour taste receptor activity is probably indirect: mice
CC lacking Pkd1l3 do not show defects in sour taste perception
CC (PubMed:20605874, PubMed:21625513). Moreover, the Pkd1l3-Pkd2l1
CC heteromer, when expressed in cells does not respond to acid stimuli
CC used to evoke proton currents in taste cells (PubMed:21098668).
CC {ECO:0000305|PubMed:16891422, ECO:0000305|PubMed:16929298,
CC ECO:0000305|PubMed:20605874, ECO:0000305|PubMed:21098668,
CC ECO:0000305|PubMed:21625513}.
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DR EMBL; AY164486; AAO32799.1; -; mRNA.
DR EMBL; DQ382344; ABD36562.1; -; mRNA.
DR EMBL; DQ382345; ABD36563.1; -; mRNA.
DR EMBL; DQ382346; ABD36564.1; -; mRNA.
DR EMBL; DQ382347; ABD36565.1; -; mRNA.
DR EMBL; DQ382348; ABD36566.1; -; mRNA.
DR EMBL; DQ382349; ABD36567.1; -; mRNA.
DR EMBL; DQ382350; ABD36568.1; -; mRNA.
DR EMBL; AC125162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS22654.1; -. [Q2EG98-8]
DR CCDS; CCDS40472.1; -. [Q2EG98-1]
DR CCDS; CCDS85608.1; -. [Q2EG98-2]
DR RefSeq; NP_001034789.2; NM_001039700.2. [Q2EG98-1]
DR RefSeq; NP_001273383.1; NM_001286454.1. [Q2EG98-2]
DR RefSeq; NP_853522.2; NM_181544.2. [Q2EG98-8]
DR PDB; 7D7E; EM; 3.40 A; A=1642-2160.
DR PDB; 7D7F; EM; 3.00 A; A=1642-2160.
DR PDBsum; 7D7E; -.
DR PDBsum; 7D7F; -.
DR AlphaFoldDB; Q2EG98; -.
DR SMR; Q2EG98; -.
DR BioGRID; 232669; 2.
DR DIP; DIP-61249N; -.
DR IntAct; Q2EG98; 1.
DR STRING; 10090.ENSMUSP00000104865; -.
DR GlyGen; Q2EG98; 6 sites.
DR iPTMnet; Q2EG98; -.
DR PhosphoSitePlus; Q2EG98; -.
DR MaxQB; Q2EG98; -.
DR PaxDb; Q2EG98; -.
DR PRIDE; Q2EG98; -.
DR Antibodypedia; 72636; 50 antibodies from 7 providers.
DR DNASU; 244646; -.
DR Ensembl; ENSMUST00000057344; ENSMUSP00000051512; ENSMUSG00000048827. [Q2EG98-8]
DR Ensembl; ENSMUST00000109242; ENSMUSP00000104865; ENSMUSG00000048827. [Q2EG98-1]
DR Ensembl; ENSMUST00000212537; ENSMUSP00000148592; ENSMUSG00000048827. [Q2EG98-2]
DR GeneID; 244646; -.
DR KEGG; mmu:244646; -.
DR UCSC; uc009niu.1; mouse. [Q2EG98-1]
DR UCSC; uc009niv.1; mouse. [Q2EG98-2]
DR CTD; 342372; -.
DR MGI; MGI:2664670; Pkd1l3.
DR VEuPathDB; HostDB:ENSMUSG00000048827; -.
DR eggNOG; KOG3599; Eukaryota.
DR GeneTree; ENSGT00940000162813; -.
DR HOGENOM; CLU_000913_1_0_1; -.
DR InParanoid; Q2EG98; -.
DR OMA; QKWRFFT; -.
DR OrthoDB; 1276906at2759; -.
DR PhylomeDB; Q2EG98; -.
DR TreeFam; TF316484; -.
DR BioGRID-ORCS; 244646; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Pkd1l3; mouse.
DR PRO; PR:Q2EG98; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q2EG98; protein.
DR Bgee; ENSMUSG00000048827; Expressed in vallate papilla and 54 other tissues.
DR ExpressionAtlas; Q2EG98; baseline and differential.
DR GO; GO:0034703; C:cation channel complex; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0006812; P:cation transport; IDA:BHF-UCL.
DR GO; GO:0071468; P:cellular response to acidic pH; IDA:BHF-UCL.
DR GO; GO:0001581; P:detection of chemical stimulus involved in sensory perception of sour taste; IDA:BHF-UCL.
DR GO; GO:0050982; P:detection of mechanical stimulus; IBA:GO_Central.
DR GO; GO:0050915; P:sensory perception of sour taste; ISO:MGI.
DR CDD; cd01752; PLAT_polycystin; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR013122; PKD1_2_channel.
DR InterPro; IPR003915; PKD_2.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR042060; PLAT_polycystin1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF08016; PKD_channel; 1.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR01433; POLYCYSTIN2.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium transport;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Lectin; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..2201
FT /note="Polycystic kidney disease protein 1-like 3"
FT /id="PRO_0000322579"
FT TOPO_DOM 25..1083
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1084..1104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1105..1293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1294..1314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1315..1330
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1331..1351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1352..1543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1544..1564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1565..1585
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1586..1606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1607..1666
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1667..1687
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1688..1855
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1856..1876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1877..1902
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1903..1923
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1924..1944
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1945..1965
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1966..2032
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2033..2053
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2054..2060
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2061..2078
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2079..2098
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2099..2119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2120..2201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 34..142
FT /note="C-type lectin"
FT DOMAIN 1018..1067
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT DOMAIN 1129..1246
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 222..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2053..2091
FT /note="Channel pore-region"
FT REGION 2152..2201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2154..2175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 923
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 961
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 116..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT VAR_SEQ 102
FT /note="T -> TDYIL (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16805797"
FT /id="VSP_031952"
FT VAR_SEQ 698
FT /note="Q -> QVSVANLLIDLSEQLLVLPFQ (in isoform 2, isoform 6
FT and isoform 8)"
FT /evidence="ECO:0000303|PubMed:12782129,
FT ECO:0000303|PubMed:16805797"
FT /id="VSP_031953"
FT VAR_SEQ 738..767
FT /note="Missing (in isoform 2, isoform 6 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:12782129,
FT ECO:0000303|PubMed:16805797"
FT /id="VSP_031954"
FT VAR_SEQ 1391..1409
FT /note="ELKETVGFLLRRNTQLLSE -> QCLKTITISAATFSNFCGD (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:16805797"
FT /id="VSP_031955"
FT VAR_SEQ 1391..1398
FT /note="ELKETVGF -> VSLVSTVF (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16805797"
FT /id="VSP_031956"
FT VAR_SEQ 1399..2201
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16805797"
FT /id="VSP_031957"
FT VAR_SEQ 1410..2201
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16805797"
FT /id="VSP_031958"
FT VAR_SEQ 1885..2201
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16805797"
FT /id="VSP_031959"
FT VAR_SEQ 2161..2201
FT /note="SSNLRERSSKSMSSDAEVLAPADAVGSVSGTDGNSGSTKVL -> Y (in
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:12782129"
FT /id="VSP_031960"
FT VAR_SEQ 2200..2201
FT /note="VL -> GTRDI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16805797"
FT /id="VSP_031961"
FT VAR_SEQ 2200..2201
FT /note="VL -> IPASTVTKKCKQARHGGACL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16805797"
FT /id="VSP_031962"
FT MUTAGEN 2059
FT /note="D->N: Little or no effect on calcium channel
FT activity."
FT /evidence="ECO:0000269|PubMed:21185261"
FT MUTAGEN 2082
FT /note="E->Q: Little or no effect on calcium channel
FT activity."
FT /evidence="ECO:0000269|PubMed:21185261"
FT CONFLICT 294
FT /note="G -> V (in Ref. 3; ABD36563)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="T -> A (in Ref. 3; ABD36562/ABD36564)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="Q -> L (in Ref. 3; ABD36564)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="N -> K (in Ref. 3; ABD36564)"
FT /evidence="ECO:0000305"
FT CONFLICT 822
FT /note="T -> P (in Ref. 3; ABD36564)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="D -> G (in Ref. 3; ABD36564)"
FT /evidence="ECO:0000305"
FT CONFLICT 1063
FT /note="I -> S (in Ref. 1; AAO32799)"
FT /evidence="ECO:0000305"
FT CONFLICT 1113
FT /note="Q -> L (in Ref. 3; ABD36564)"
FT /evidence="ECO:0000305"
FT CONFLICT 1130
FT /note="H -> L (in Ref. 3; ABD36564)"
FT /evidence="ECO:0000305"
FT CONFLICT 1341
FT /note="S -> P (in Ref. 3; ABD36562)"
FT /evidence="ECO:0000305"
FT CONFLICT 1538
FT /note="R -> K (in Ref. 3; ABD36562)"
FT /evidence="ECO:0000305"
FT CONFLICT 1618
FT /note="H -> R (in Ref. 3; ABD36563/ABD36566/ABD36567/
FT ABD36568)"
FT /evidence="ECO:0000305"
FT HELIX 1675..1686
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 1692..1704
FT /evidence="ECO:0007829|PDB:7D7F"
FT TURN 1705..1707
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 1708..1710
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 1717..1724
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 1726..1729
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 1732..1735
FT /evidence="ECO:0007829|PDB:7D7E"
FT STRAND 1736..1744
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 1749..1754
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 1767..1769
FT /evidence="ECO:0007829|PDB:7D7E"
FT TURN 1784..1786
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 1790..1793
FT /evidence="ECO:0007829|PDB:7D7E"
FT STRAND 1797..1801
FT /evidence="ECO:0007829|PDB:7D7F"
FT TURN 1805..1807
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 1824..1828
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 1831..1833
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 1834..1845
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 1853..1864
FT /evidence="ECO:0007829|PDB:7D7F"
FT TURN 1865..1868
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 1869..1879
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 1881..1883
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 1885..1894
FT /evidence="ECO:0007829|PDB:7D7F"
FT TURN 1904..1906
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 1907..1929
FT /evidence="ECO:0007829|PDB:7D7F"
FT STRAND 1932..1934
FT /evidence="ECO:0007829|PDB:7D7F"
FT TURN 1935..1937
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 1939..1974
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 1983..2013
FT /evidence="ECO:0007829|PDB:7D7F"
FT TURN 2014..2016
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 2029..2032
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 2035..2053
FT /evidence="ECO:0007829|PDB:7D7F"
FT TURN 2054..2056
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 2058..2060
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 2063..2075
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 2082..2086
FT /evidence="ECO:0007829|PDB:7D7F"
FT HELIX 2088..2116
FT /evidence="ECO:0007829|PDB:7D7F"
SQ SEQUENCE 2201 AA; 241253 MW; 389C31618FA84C07 CRC64;
MLLQRRSWLW LYIRIGVILG DILGRKPSIR EQHGGNSCYQ LNRLFCDFQE ADNYCHAQRG
RLAHTWNPKL RGFLKSFLNE ETVWWVRGNL TLPGSHPGIN QTGGDDVLRN QKPGECPSVV
THSNAVFSRW NLCIEKHHFI CQAAAFPPQG ASIWRNEFGP GPLLPMKRRG AETERHMIPG
NGPPLAMCHQ PAPPELFETL CFPIDPASSA PPKATHRMTI TSLTGRPQVT SDTLASSSPP
QGTSDTPASS SPPQVTSATS ASSSPPQGTS DTPASSSPPQ VTSATSASSS PPQGTSDTPA
SSSPPQVTSA TSASSSPPQG TSDTPASSSP PQVTSATSAS SSPPQGTSDT PASSSPPQGT
LDTPSSSSPP QGTSDTPASS SPPQGTSETP ASNSPPQGTS ETPGFSSPPQ VTTATLVSSS
PPQVTSETPA SSSPTQVTSE TPASSSPTQV TSDTPASNSP PQGTSDTPGF SSPTQVTTAT
LVSSSPPQVT SDTPASSSPP QVTSDTPASS SPPQVTSETP ASSSPPQVTS DTSASISPPQ
VISDTPASSS PPQVTSETPA SSSPTNMTSD TPASSSPTNM TSDTPASSSP TNMTSDTPAS
SSPPWPVITE VTRPESTIPA GRSLANITSK AQEDSPLGVI STHPQMSFQS STSQALDETA
GERVPTIPDF QAHSEFQKAC AILQRLRDFL PTSPTSAQKN NSWSSQTPAV SCPFQPLGRL
TTTEKSSHQM AQQDMEQHPM DGAHNAFGIS AGGSEIQSDI QLRSEFEVED MLETSLMALG
EIHRAFCQQS LCPQSAVTLA SPSATLMLSS QNVSTLPLST YTLGEPAPLT LGFPSAEALK
ELLNKHPGVN LQVTGLAFNP FKTLDDKNIV GSIGNVQLSS AYQSIRVHDL IEDIEIMLWR
NASMETQPTS LNTSTDHFTI SVNITSLEKT LIVTIEPESP LLMTLHLGFQ DQLAHTHFYL
NISLPRDQVW QKDEEYTWVL TPENLWYGTG TYYIMAVENK STEAAQHTPV LVSVVTAVTQ
CYFWDRYNRT WKSDGCQVGP KSTILKTQCL CDHLTFFSSD FFIVPRTVDV ENTIKLLLHV
TNNPVGVSLL SSLLGFYILL AMWASRKDRE DMQKVKVTVL ADNDPSSASH YLIQVYTGYR
RRAATTAKVV ITLYGSEGHS EPHHLCDPEK TVFERGALDV FLLSTGSWLG DLHGLRLWHD
NSGDSPSWYV SQVIVSDMTT RKKWHFQCNC WLAVDLGNCE RDRVFTPASR SELSSFRHLF
SSTIVEKFTQ DYLWLSVATR HPWNQFTRVQ RLSCCMALLL CDMVINIMFW KMGGTTAKRG
TEQLGPLAVT LSELLVSIQT SIILFPIHLI FGRLFQLIHP PEALPQLPFI QAAWPPALVC
ESPSLTQVVK ELKETVGFLL RRNTQLLSEC EPSSCSSCDI NKLAKLLSGL IYCHLEDEGC
HQQTESHWED AVSENHYHFC RYLLQLLRRL KAHLEALGAT QDHQSCDFSE AVSQLQNLQE
LLETQTLRRG PGPCRHSTSF PILSPGEGKK PMSFCLFRWL KCSCWLLLGV ISLASAFFIT
LYSLELDKDQ ATSWVISMML SVLQDIFISQ PIKVIFLTLL FSLMANHMPW LNKDKEQHAR
RIVALWAKCP WSAPGLRDKN NPIYTAPAMN NLAKPTRKAW KKQLSKLTGG TLVQILFLTL
LMTTVYSAKD SSRFFLHRAI WKRFSHRFSE IKTVEDFYPW ANGTLLPNLY GDYRGFITDG
NSFLLGNVLI RQTRIPNDIF FPGSLHKQMK SPPQHQEDRE NYGAGWVPPD TNITKVDSIW
HYQNQESLGG YPIQGELATY SGGGYVVRLG RNHSAATRVL QHLEQRRWLD HCTKALFVEF
TVFNANVNLL CAVTLILESS GVGTFLTSLQ LDSLTSLQSS ERGFAWIVSQ VVYYLLVCYY
AFIQGCRLKR QRLAFFTRKR NLLDTSIVLI SFSILGLSMQ SLSLLHKKMQ QYHCDRDRFI
SFYEALRVNS AVTHLRGFLL LFATVRVWDL LRHHAQLQVI NKTLSKAWDE VLGFILIIVV
LLSSYAMTFN LLFGWSISDY QSFFRSIVTV VGLLMGTSKH KEVIALYPIL GSLLVLSSII
LMGLVIINLF VSAILIAFGK ERKACEKEAT LTDMLLQKLS SLLGIRLHQN PSEEHADNTG
SSNLRERSSK SMSSDAEVLA PADAVGSVSG TDGNSGSTKV L
