GenomeNet

Database: UniProt
Entry: CAC1D_MOUSE
LinkDB: CAC1D_MOUSE
Original site: CAC1D_MOUSE 
ID   CAC1D_MOUSE             Reviewed;        2179 AA.
AC   Q99246; Q7TSD2; Q8R2I9; Q8R2J0;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   20-JUN-2018, entry version 160.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1D;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 2;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.3;
GN   Name=Cacna1d; Synonyms=Cach3, Cacn4, Cacnl1a2, Cchl1a2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), INDUCTION, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=12900400; DOI=10.1074/jbc.M307598200;
RA   Xu M., Welling A., Paparisto S., Hofmann F., Klugbauer N.;
RT   "Enhanced expression of L-type Cav1.3 calcium channels in murine
RT   embryonic hearts from Cav1.2-deficient mice.";
RL   J. Biol. Chem. 278:40837-40841(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RA   Okamoto T., Kobayashi T., Hino O.;
RT   "Cloning of the L-type Ca2+ channel alpha1D-subunit from mouse brain
RT   and characterization of its expression in the liver.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1168-1463 (ISOFORMS 2/3).
RC   STRAIN=ICR; TISSUE=Ovary;
RX   PubMed=2173707;
RA   Perez-Reyes E., Wei X., Castellano A., Birnbaumer L.;
RT   "Molecular diversity of L-type calcium channels. Evidence for
RT   alternative splicing of the transcripts of three non-allelic genes.";
RL   J. Biol. Chem. 265:20430-20436(1990).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=10929716; DOI=10.1016/S0092-8674(00)00013-1;
RA   Platzer J., Engel J., Schrott-Fischer A., Stephan K., Bova S.,
RA   Chen H., Zheng H., Striessnig J.;
RT   "Congenital deafness and sinoatrial node dysfunction in mice lacking
RT   class D L-type Ca2+ channels.";
RL   Cell 102:89-97(2000).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=11581302; DOI=10.1172/JCI200113310;
RA   Namkung Y., Skrypnyk N., Jeong M.J., Lee T., Lee M.S., Kim H.L.,
RA   Chin H., Suh P.G., Kim S.S., Shin H.S.;
RT   "Requirement for the L-type Ca(2+) channel alpha(1D) subunit in
RT   postnatal pancreatic beta cell generation.";
RL   J. Clin. Invest. 108:1015-1022(2001).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12700358; DOI=10.1073/pnas.0935295100;
RA   Mangoni M.E., Couette B., Bourinet E., Platzer J., Reimer D.,
RA   Striessnig J., Nargeot J.;
RT   "Functional role of L-type Cav1.3 Ca2+ channels in cardiac pacemaker
RT   activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5543-5548(2003).
RN   [8]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16354915; DOI=10.1523/JNEUROSCI.3411-05.2005;
RA   Brandt A., Khimich D., Moser T.;
RT   "Few CaV1.3 channels regulate the exocytosis of a synaptic vesicle at
RT   the hair cell ribbon synapse.";
RL   J. Neurosci. 25:11577-11585(2005).
RN   [9]
RP   INTERACTION WITH CABP1 AND CABP4.
RX   PubMed=17947313; DOI=10.1113/jphysiol.2007.142307;
RA   Cui G., Meyer A.C., Calin-Jageman I., Neef J., Haeseleer F., Moser T.,
RA   Lee A.;
RT   "Ca2+-binding proteins tune Ca2+-feedback to Cav1.3 channels in mouse
RT   auditory hair cells.";
RL   J. Physiol. (Lond.) 585:791-803(2007).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1D
CC       gives rise to L-type calcium currents. Long-lasting (L-type)
CC       calcium channels belong to the 'high-voltage activated' (HVA)
CC       group. They are blocked by dihydropyridines (DHP),
CC       phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA
CC       (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-
CC       GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
CC       {ECO:0000269|PubMed:16354915}.
CC   -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit
CC       complexes, consisting of alpha-1, alpha-2, beta and delta subunits
CC       in a 1:1:1:1 ratio. The channel activity is directed by the pore-
CC       forming and voltage-sensitive alpha-1 subunit. In many cases, this
CC       subunit is sufficient to generate voltage-sensitive calcium
CC       channel activity. The auxiliary subunits beta and alpha-2/delta
CC       linked by a disulfide bridge regulate the channel activity.
CC       Interacts (via IQ domain) with CABP1 and CABP4 in a calcium
CC       independent manner. Interacts with RIMBP2 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q99246-2; Sequence=Displayed;
CC       Name=2; Synonyms=Cav1.3(1a);
CC         IsoId=Q99246-3; Sequence=VSP_027091, VSP_027092;
CC       Name=3; Synonyms=Cav1.3(1b);
CC         IsoId=Q99246-4; Sequence=VSP_027090, VSP_027091, VSP_027092;
CC   -!- TISSUE SPECIFICITY: Expressed in the inner hair cells (IHC) of the
CC       cochlea. {ECO:0000269|PubMed:16354915}.
CC   -!- DEVELOPMENTAL STAGE: Isoform 2 and isoform 3 are expressed in
CC       heart at 12.5 dpc (at protein level). Expressed in the heart at
CC       9.5, 12.5 and 15.5 dpc. Isoform 2 and isoform 3 are expressed in
CC       heart at 9.5 and 12.5 dpc. {ECO:0000269|PubMed:12900400}.
CC   -!- INDUCTION: Up-regulated in CACNA1C knockout mice.
CC       {ECO:0000269|PubMed:12900400}.
CC   -!- DOMAIN: Each of the four internal repeats contains five
CC       hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
CC       positively charged transmembrane segment (S4). S4 segments
CC       probably represent the voltage-sensor and are characterized by a
CC       series of positively charged amino acids at every third position.
CC   -!- DISRUPTION PHENOTYPE: deafness, bradycardia and diabetic traits.
CC       {ECO:0000269|PubMed:10929716, ECO:0000269|PubMed:11581302,
CC       ECO:0000269|PubMed:12700358}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. CACNA1D subfamily. {ECO:0000305}.
DR   EMBL; AJ437291; CAD26883.1; -; mRNA.
DR   EMBL; AJ437292; CAD26884.1; -; mRNA.
DR   EMBL; AB086123; BAC77259.1; -; mRNA.
DR   EMBL; AC119886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT009536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M57975; AAA63292.1; -; mRNA.
DR   CCDS; CCDS36846.1; -. [Q99246-4]
DR   CCDS; CCDS36847.1; -. [Q99246-3]
DR   RefSeq; NP_001077085.1; NM_001083616.2. [Q99246-3]
DR   RefSeq; NP_001289566.1; NM_001302637.1. [Q99246-2]
DR   RefSeq; NP_083257.2; NM_028981.3. [Q99246-4]
DR   UniGene; Mm.9772; -.
DR   ProteinModelPortal; Q99246; -.
DR   SMR; Q99246; -.
DR   BioGrid; 198433; 2.
DR   IntAct; Q99246; 2.
DR   STRING; 10090.ENSMUSP00000107869; -.
DR   GuidetoPHARMACOLOGY; 530; -.
DR   iPTMnet; Q99246; -.
DR   PhosphoSitePlus; Q99246; -.
DR   SwissPalm; Q99246; -.
DR   PaxDb; Q99246; -.
DR   PRIDE; Q99246; -.
DR   Ensembl; ENSMUST00000112250; ENSMUSP00000107869; ENSMUSG00000015968. [Q99246-4]
DR   Ensembl; ENSMUST00000223803; ENSMUSP00000153586; ENSMUSG00000015968. [Q99246-3]
DR   Ensembl; ENSMUST00000224198; ENSMUSP00000153250; ENSMUSG00000015968. [Q99246-2]
DR   GeneID; 12289; -.
DR   KEGG; mmu:12289; -.
DR   UCSC; uc007suu.2; mouse. [Q99246-3]
DR   UCSC; uc007suw.2; mouse. [Q99246-2]
DR   UCSC; uc007sux.2; mouse. [Q99246-4]
DR   CTD; 776; -.
DR   MGI; MGI:88293; Cacna1d.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   HOGENOM; HOG000231529; -.
DR   HOVERGEN; HBG050763; -.
DR   InParanoid; Q99246; -.
DR   KO; K04851; -.
DR   OMA; LIQVERP; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Reactome; R-MMU-422356; Regulation of insulin secretion.
DR   Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR   Reactome; R-MMU-5576893; Phase 2 - plateau phase.
DR   ChiTaRS; Cacna1d; mouse.
DR   PRO; PR:Q99246; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   Bgee; ENSMUSG00000015968; -.
DR   Genevisible; Q99246; MM.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0032590; C:dendrite membrane; ISO:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IC:MGI.
DR   GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; ISO:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR   GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
DR   GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
DR   GO; GO:0005262; F:calcium channel activity; ISO:MGI.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; ISO:MGI.
DR   GO; GO:0086059; F:voltage-gated calcium channel activity involved SA node cell action potential; IMP:MGI.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IMP:MGI.
DR   GO; GO:0070509; P:calcium ion import; ISO:MGI.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IMP:MGI.
DR   GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR   GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR   GO; GO:0061337; P:cardiac conduction; ISS:UniProtKB.
DR   GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:MGI.
DR   GO; GO:0070838; P:divalent metal ion transport; ISO:MGI.
DR   GO; GO:0086046; P:membrane depolarization during SA node cell action potential; IMP:MGI.
DR   GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
DR   GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISO:MGI.
DR   GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR   GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:MGI.
DR   GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IMP:BHF-UCL.
DR   GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IMP:BHF-UCL.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   Gene3D; 1.20.120.350; -; 4.
DR   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005452; LVDCC_a1dsu.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF139; PTHR10037:SF139; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01636; LVDCCALPHA1D.
DR   SMART; SM01062; Ca_chan_IQ; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW   Coiled coil; Complete proteome; Disulfide bond; Ion channel;
KW   Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   CHAIN         1   2179       Voltage-dependent L-type calcium channel
FT                                subunit alpha-1D.
FT                                /FTId=PRO_0000053935.
FT   TOPO_DOM      1    126       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    127    145       Helical; Name=S1 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    146    163       Extracellular. {ECO:0000255}.
FT   TRANSMEM    164    183       Helical; Name=S2 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    184    195       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    196    214       Helical; Name=S3 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    215    235       Extracellular. {ECO:0000255}.
FT   TRANSMEM    236    254       Helical; Name=S4 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    255    273       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    274    293       Helical; Name=S5 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    294    381       Extracellular. {ECO:0000255}.
FT   TRANSMEM    382    406       Helical; Name=S6 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    407    543       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    544    563       Helical; Name=S1 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    564    578       Extracellular. {ECO:0000255}.
FT   TRANSMEM    579    597       Helical; Name=S2 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    598    605       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    606    624       Helical; Name=S3 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    625    634       Extracellular. {ECO:0000255}.
FT   TRANSMEM    635    653       Helical; Name=S4 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    654    672       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    673    693       Helical; Name=S5 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    694    747       Extracellular. {ECO:0000255}.
FT   TRANSMEM    748    772       Helical; Name=S6 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    773    906       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    907    925       Helical; Name=S1 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM    926    941       Extracellular. {ECO:0000255}.
FT   TRANSMEM    942    961       Helical; Name=S2 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM    962    973       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    974    992       Helical; Name=S3 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM    993    998       Extracellular. {ECO:0000255}.
FT   TRANSMEM    999   1018       Helical; Name=S4 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1019   1037       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1038   1057       Helical; Name=S5 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1058   1147       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1148   1168       Helical; Name=S6 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1169   1225       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1226   1244       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1245   1259       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1260   1279       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1280   1286       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1287   1308       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1309   1333       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1334   1353       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1354   1372       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1373   1392       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1393   1459       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1460   1484       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1485   2179       Cytoplasmic. {ECO:0000255}.
FT   REPEAT      113    409       I.
FT   REPEAT      529    775       II.
FT   REPEAT      893   1175       III.
FT   REPEAT     1212   1487       IV.
FT   CA_BIND    1513   1524       {ECO:0000250}.
FT   REGION      429    446       Binding to the beta subunit.
FT                                {ECO:0000250}.
FT   REGION     1095   1185       Dihydropyridine binding. {ECO:0000250}.
FT   REGION     1440   1506       Dihydropyridine binding. {ECO:0000250}.
FT   REGION     1452   1495       Phenylalkylamine binding. {ECO:0000250}.
FT   COILED      771    810       {ECO:0000255}.
FT   COMPBIAS      1      7       Poly-Met.
FT   COMPBIAS    673    679       Poly-Leu.
FT   COMPBIAS    847    858       Poly-Glu.
FT   SITE        364    364       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE        725    725       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1121   1121       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1426   1426       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   MOD_RES    1495   1495       Phosphoserine; by PKA. {ECO:0000250}.
FT   VAR_SEQ       1     22       MMMMMMMKKMQHQRQHQEDHAN -> MNLPTFSSDLILIKS
FT                                VLSQETDARYKGRVVSAVESTEDFSQAFA (in isoform
FT                                3). {ECO:0000303|PubMed:12900400}.
FT                                /FTId=VSP_027090.
FT   VAR_SEQ     493    513       WCWWKRRGAAKTGPSGCRRWG -> C (in isoform 2
FT                                and isoform 3).
FT                                {ECO:0000303|PubMed:12900400}.
FT                                /FTId=VSP_027091.
FT   VAR_SEQ    1311   1325       Missing (in isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:12900400}.
FT                                /FTId=VSP_027092.
FT   CONFLICT    445    445       A -> V (in Ref. 1; CAD26883/CAD26884).
FT                                {ECO:0000305}.
FT   CONFLICT    868    868       I -> T (in Ref. 1; CAD26883/CAD26884).
FT                                {ECO:0000305}.
FT   CONFLICT   1871   1871       E -> G (in Ref. 1; CAD26883/CAD26884).
FT                                {ECO:0000305}.
FT   CONFLICT   2043   2043       Y -> S (in Ref. 2; BAC77259).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2179 AA;  247061 MW;  BEED5EF140E75782 CRC64;
     MMMMMMMKKM QHQRQHQEDH ANEANYARGT RLPISGEGPT SQPNSSKQTV LSWQAAIDAA
     RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS RPARALFCLS LNNPIRRACI
     SIVEWKPFDI FILLAIFANC VALAIYIPFP EDDSNSTNHN LEKVEYAFLI IFTVETFLKI
     IAYGLLLHPN AYVRNGWNLL DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR
     AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT
     CFFADSDIVA EEDPAPCAFS GNGRQCTANG TECRSGWVGP NGGITNFDNF AFAMLTVFQC
     ITMEGWTDVL YWVNDAIGWE WPWVYFVSLI ILGSFFVLNL VLGVLSGEFS KEREKAKARG
     DFQKLREKQQ LEEDLKGYLD WITQAEDIDP ENEEEGGEEG KRNTSMPTSE TESVNTENVS
     GEGETQGCCG TLWCWWKRRG AAKTGPSGCR RWGQAISKSK LSRRWRRWNR FNRRRCRAAV
     KSVTFYWLVI VLVFLNTLTI SSEHYNQPDW LTQIQDIANK VLLALFTCEM LVKMYSLGLQ
     AYFVSLFNRF DCFVVCGGIT ETILVELELM SPLGVSVFRC VRLLRIFKVT RHWTSLSNLV
     ASLLNSMKSI ASLLLLLFLF IIIFSLLGMQ LFGGKFNFDE TQTKRSTFDN FPQALLTVFQ
     ILTGEDWNAV MYDGIMAYGG PSSSGMIVCI YFIILFICGN YILLNVFLAI AVDNLADAES
     LNTAQKEEAE EKERKKIARK ESLENKKNNK PEVNQIANSD NKVTIDDYQE DAEDKDPYPP
     CDVPVGEEEE EEEEDEPEVP AGPRPRRISE LNMKEKIAPI PEGSAFFILS KTNPIRVGCH
     KLINHHIFTN LILVFIMLSS AALAAEDPIR SHSFRNTILG YFDYAFTAIF TVEILLKMTT
     FGAFLHKGAF CRNYFNLLDM LVVGVSLVSF GIQSSAISVV KILRVLRVLR PLRAINRAKG
     LKHVVQCVFV AIRTIGNIMI VTTLLQFMFA CIGVQLFKGK FYRCTDEAKS NPEECRGLFI
     LYKDGDVDSP VVRERIWQNS DFNFDNVLSA MMALFTVSTF EGWPALLYKA IDSNGENVGP
     VYNYRVEISI FFIIYIIIVA FFMMNIFVGF VIVTFQEQGE KEYKNCELDK NQRQCVEYAL
     KARPLRRYIP KNPYQYKFWY VVNSSPFEYM MFVLIMLNTL CLAMQHYEQS KMFNDAMDIL
     NMVFTGVFTV EMVLKVIAFK PKGYFSDAWN TFDSLIVIGS IIDVALSEAD PSESETIPLP
     TATPGNSEES NRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIAML
     FFIYAVIGMQ MFGKVAMRDN NQINRNNNFQ TFPQAVLLLF RCATGEAWQE IMLACLPGKL
     CDPDSDYNPG EEYTCGSNFA IVYFISFYML CAFLIINLFV AVIMDNFDYL TRDWSILGPH
     HLDEFKRIWS EYDPEAKGRI KHLDVVTLLR RIQPPLGFGK LCPHRVACKR LVAMNMPLNS
     DGTVMFNATL FALVRTALKI KTEGNLEQAN EELRAVIKKI WKKTSMKLLD QVVPPAGDDE
     VTVGKFYATF LIQDYFRKFK KRKEQGLVGK YPAKNTTIAL QAGLRTLHDI GPEIRRAISC
     DLQDDEPEDS KPEEEDVFKR NGALLGNHVN HVNSDRRDSL QQTNTTHRPL HVQRPSMPPA
     SDTEKPLFPP AGNSGCHNHH NHNSIGKQAP TSTNANLNNA NMSKAAHGKP PSIGNLEHVS
     ENGHYSCKHD RELQRRSSIK RTRYYETYIR SESGDEQFPT ICREDPEIHG YFRDPRCLGE
     QEYFSSEECC EDDSSPTWSR QNYNYYNRYP GSSMDFERPR GYHHPQGFLE DDDSPTGYDS
     RRSPRRRLLP PTPPSHRRSS FNFECLRRQS SQDDVLPSPA LPHRAALPLH LMQQQIMAVA
     GLDSSKAQKY SPSHSTRSWA TPPATPPYRD WSPCYTPLIQ VDRSESMDQV NGSLPSLHRS
     SWYTDEPDIS YRTFTPASLT VPSSFRNKNS DKQRSADSLV EAVLISEGLG RYARDPKFVS
     ATKHEIADAC DLTIDEMESA ASTLLNGSVC PRANGDMGPI SHRQDYELQD FGPGYSDEEP
     DPGREEEDLA DEMICITTL
//
DBGET integrated database retrieval system