CAC1D_RAT
ID CAC1D_RAT Reviewed; 2203 AA.
AC P27732; O09022; O09023; O09024; Q01542; Q62691; Q62815; Q63491; Q63492;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 171.
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=Rat brain class D;
DE Short=RBD;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.3;
GN Name=Cacna1d; Synonyms=Cach3, Cacn4, Cacnl1a2, Cchl1a2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Insulinoma;
RX PubMed=7760845; DOI=10.1210/mend.9.1.7760845;
RA Ihara Y., Yamada Y., Fujii Y., Gonoi T., Yano H., Yasuda K., Inagaki N.,
RA Seino Y., Seino S.;
RT "Molecular diversity and functional characterization of voltage-dependent
RT calcium channels (CACN4) expressed in pancreatic beta-cells.";
RL Mol. Endocrinol. 9:121-130(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 6; 7; 8 AND 13).
RC TISSUE=Brain;
RX PubMed=1648940; DOI=10.1016/0896-6273(91)90072-8;
RA Hui A., Ellinor P.T., Krizanova O., Wang J.-J., Diebold R.J., Schwartz A.;
RT "Molecular cloning of multiple subtypes of a novel rat brain isoform of the
RT alpha-1 subunit of the voltage-dependent calcium channel.";
RL Neuron 7:35-44(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.
RX PubMed=7553731; DOI=10.1007/bf02089942;
RA Kamp T.J., Mitas M., Fields K.L., Asoh S., Chin H., Marban E.,
RA Nirenberg M.;
RT "Transcriptional regulation of the neuronal L-type calcium channel alpha 1D
RT subunit gene.";
RL Cell. Mol. Neurobiol. 15:307-326(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1100-1410 (ISOFORMS 4 AND 11).
RC TISSUE=Kidney;
RX PubMed=1279681; DOI=10.1073/pnas.89.21.10494;
RA Yu A.S.L., Hebert S.C., Brenner B.M., Lytton J.;
RT "Molecular characterization and nephron distribution of a family of
RT transcripts encoding the pore-forming subunit of Ca2+ channels in the
RT kidney.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10494-10498(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1218-1498 (ISOFORM 12).
RC TISSUE=Osteosarcoma;
RX PubMed=7479909; DOI=10.1073/pnas.92.24.10914;
RA Barry E.L.R., Gesek F.A., Froehner S.C., Friedman P.A.;
RT "Multiple calcium channel transcripts in rat osteosarcoma cells: selective
RT activation of alpha 1D isoform by parathyroid hormone.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10914-10918(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1200-1493 (ISOFORMS 3; 4; 5; 9 AND 10).
RC TISSUE=Hepatoma;
RX PubMed=9232351; DOI=10.1016/s0143-4160(97)90088-9;
RA Brereton H.M., Harland M.L., Froscio M., Petronijevic T., Barritt G.J.;
RT "Novel variants of voltage-operated calcium channel alpha-1 subunit
RT transcripts in a rat liver-derived cell line: deletion in the IVS4 voltage
RT sensing region.";
RL Cell Calcium 22:39-52(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE OF 1307-1479 (ISOFORM 3).
RX PubMed=1692134; DOI=10.1073/pnas.87.9.3391;
RA Snutch T.P., Leonard J.P., Gilbert M.M., Lester H.A., Davidson N.;
RT "Rat brain expresses a heterogeneous family of calcium channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3391-3395(1990).
RN [8]
RP FUNCTION, MUTAGENESIS OF 1656-ILE-GLN-1657, INTERACTION WITH CABP1 AND
RP CABP4, AND TISSUE SPECIFICITY.
RX PubMed=17050707; DOI=10.1523/jneurosci.3236-06.2006;
RA Yang P.S., Alseikhan B.A., Hiel H., Grant L., Mori M.X., Yang W.,
RA Fuchs P.A., Yue D.T.;
RT "Switching of Ca2+-dependent inactivation of Ca(v)1.3 channels by calcium
RT binding proteins of auditory hair cells.";
RL J. Neurosci. 26:10677-10689(2006).
CC -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC of calcium ions into excitable cells and are also involved in a variety
CC of calcium-dependent processes, including muscle contraction, hormone
CC or neurotransmitter release, gene expression, cell motility, cell
CC division and cell death. The isoform alpha-1D gives rise to L-type
CC calcium currents. Long-lasting (L-type) calcium channels belong to the
CC 'high-voltage activated' (HVA) group. They are blocked by
CC dihydropyridines (DHP), phenylalkylamines, and by benzothiazepines.
CC {ECO:0000269|PubMed:17050707}.
CC -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit complexes,
CC consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1
CC ratio. The channel activity is directed by the pore-forming and
CC voltage-sensitive alpha-1 subunit. In many cases, this subunit is
CC sufficient to generate voltage-sensitive calcium channel activity. The
CC auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge
CC regulate the channel activity. Interacts with CABP1 and CABP4,
CC resulting in a near elimination of calcium-dependent inactivation of
CC the channel. Interacts with RIMBP2 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P27732; O88871: Gabbr2; NbExp=6; IntAct=EBI-8072674, EBI-7090239;
CC P27732; Q9QX74-7: Shank2; NbExp=2; IntAct=EBI-8072674, EBI-20939146;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=13;
CC Comment=The region sequenced in isoforms ROB3 and RKC5 is identical
CC to CACN4.;
CC Name=1; Synonyms=CACN4A;
CC IsoId=P27732-1; Sequence=Displayed;
CC Name=2; Synonyms=CACN4B;
CC IsoId=P27732-2; Sequence=VSP_000923, VSP_000924;
CC Name=3; Synonyms=CACH3A, RB48, RBD-55;
CC IsoId=P27732-3; Sequence=VSP_000921;
CC Name=4; Synonyms=Delta-IV-S3, RKC6;
CC IsoId=P27732-4; Sequence=VSP_000919;
CC Name=5; Synonyms=Delta-IV-S4;
CC IsoId=P27732-5; Sequence=VSP_000922;
CC Name=6; Synonyms=RB9;
CC IsoId=P27732-6; Sequence=VSP_000920, VSP_000921;
CC Name=7; Synonyms=RB11;
CC IsoId=P27732-7; Sequence=VSP_000917;
CC Name=8; Synonyms=RB34;
CC IsoId=P27732-8; Sequence=VSP_000916;
CC Name=9; Synonyms=RH1;
CC IsoId=P27732-9; Sequence=VSP_000918;
CC Name=10; Synonyms=RH2;
CC IsoId=P27732-10; Sequence=VSP_000919, VSP_000922;
CC Name=11; Synonyms=RKC5;
CC IsoId=P27732-13; Sequence=Not described;
CC Name=12; Synonyms=ROB3;
CC IsoId=P27732-14; Sequence=Not described;
CC Name=13; Synonyms=Truncated;
CC IsoId=P27732-12; Sequence=VSP_000925, VSP_000926;
CC -!- TISSUE SPECIFICITY: Expressed in brain, pancreatic islets and B-
CC lymphocytes. {ECO:0000269|PubMed:17050707}.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1D subfamily. {ECO:0000305}.
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DR EMBL; D38101; BAA07282.1; -; mRNA.
DR EMBL; D38102; BAA07283.1; -; mRNA.
DR EMBL; M57682; AAA42015.1; -; mRNA.
DR EMBL; U14005; AAB60515.1; -; Genomic_DNA.
DR EMBL; M99221; AAA40895.1; -; mRNA.
DR EMBL; U31772; AAA89156.1; -; mRNA.
DR EMBL; U49126; AAB61634.1; -; mRNA.
DR EMBL; U49127; AAB61635.1; -; mRNA.
DR EMBL; U49128; AAB61636.1; -; mRNA.
DR PIR; JH0422; JH0422.
DR PIR; T42742; T42742.
DR RefSeq; NP_058994.1; NM_017298.1. [P27732-1]
DR AlphaFoldDB; P27732; -.
DR SMR; P27732; -.
DR BioGRID; 248333; 1.
DR DIP; DIP-60740N; -.
DR IntAct; P27732; 5.
DR MINT; P27732; -.
DR STRING; 10116.ENSRNOP00000051407; -.
DR BindingDB; P27732; -.
DR ChEMBL; CHEMBL4132; -.
DR DrugCentral; P27732; -.
DR GuidetoPHARMACOLOGY; 530; -.
DR TCDB; 1.A.1.11.1; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; P27732; 3 sites.
DR iPTMnet; P27732; -.
DR PhosphoSitePlus; P27732; -.
DR PaxDb; P27732; -.
DR PRIDE; P27732; -.
DR ABCD; P27732; 2 sequenced antibodies.
DR GeneID; 29716; -.
DR CTD; 776; -.
DR RGD; 70973; Cacna1d.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; P27732; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; P27732; -.
DR Reactome; R-RNO-422356; Regulation of insulin secretion.
DR PRO; PR:P27732; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0098683; C:cochlear hair cell ribbon synapse; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0032590; C:dendrite membrane; IDA:RGD.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:RGD.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:RGD.
DR GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
DR GO; GO:0005262; F:calcium channel activity; ISO:RGD.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IDA:RGD.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:BHF-UCL.
DR GO; GO:0086007; F:voltage-gated calcium channel activity involved in cardiac muscle cell action potential; IC:BHF-UCL.
DR GO; GO:0099635; F:voltage-gated calcium channel activity involved in positive regulation of presynaptic cytosolic calcium levels; ISO:RGD.
DR GO; GO:0086059; F:voltage-gated calcium channel activity involved SA node cell action potential; ISO:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0070509; P:calcium ion import; IMP:RGD.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; IDA:BHF-UCL.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA:RGD.
DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
DR GO; GO:0007507; P:heart development; IEP:RGD.
DR GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; IC:BHF-UCL.
DR GO; GO:0086046; P:membrane depolarization during SA node cell action potential; ISO:RGD.
DR GO; GO:0007613; P:memory; IEP:RGD.
DR GO; GO:0030001; P:metal ion transport; IMP:RGD.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISS:UniProtKB.
DR GO; GO:1904879; P:positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IMP:RGD.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:RGD.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IMP:RGD.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
DR GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; ISO:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IDA:BHF-UCL.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
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 Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16885; CAC1F_C; 2.
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 Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..2203
FT /note="Voltage-dependent L-type calcium channel subunit
FT alpha-1D"
FT /id="PRO_0000053936"
FT TOPO_DOM 1..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..145
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..163
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..183
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..214
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..254
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..293
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..381
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..406
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 407..582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..602
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..617
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..636
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 637..644
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 645..663
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 664..673
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 674..692
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 693..711
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 712..732
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 733..786
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..811
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 812..945
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 946..964
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 965..980
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 981..1000
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1001..1012
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1013..1031
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1032..1037
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1038..1057
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1058..1076
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1077..1096
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1097..1186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1187..1207
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1208..1264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1265..1283
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1284..1298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1299..1318
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1319..1325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1326..1347
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1348..1357
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1358..1377
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1378..1396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1397..1416
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1417..1483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1484..1508
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1509..2203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 112..408
FT /note="I"
FT REPEAT 528..774
FT /note="II"
FT REPEAT 892..1174
FT /note="III"
FT REPEAT 1211..1486
FT /note="IV"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..446
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000250"
FT REGION 449..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1224
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 1464..1530
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 1476..1519
FT /note="Phenylalkylamine binding"
FT /evidence="ECO:0000250"
FT REGION 1734..1766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1795..1816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1920..1963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2176..2195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..897
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1736..1755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1795..1809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1921..1950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 764
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 1160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 481..492
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:1648940"
FT /id="VSP_000916"
FT VAR_SEQ 493..512
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:1648940"
FT /id="VSP_000917"
FT VAR_SEQ 1322..1392
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:9232351"
FT /id="VSP_000918"
FT VAR_SEQ 1322..1349
FT /note="Missing (in isoform 4 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:1279681,
FT ECO:0000303|PubMed:9232351"
FT /id="VSP_000919"
FT VAR_SEQ 1322..1348
FT /note="GYFSDAWNTFDSLIVIGSIIDVALSEA -> HYFTDAWNTFDALIVVGSVVD
FT IAITEVN (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:1648940"
FT /id="VSP_000920"
FT VAR_SEQ 1349
FT /note="D -> DPSDSENIPLPTATPG (in isoform 6 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:1648940,
FT ECO:0000303|PubMed:9232351"
FT /id="VSP_000921"
FT VAR_SEQ 1354..1368
FT /note="Missing (in isoform 10 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:9232351"
FT /id="VSP_000922"
FT VAR_SEQ 1642..1668
FT /note="DDEVTVGKFYATFLIQDYFRKFKKRKE -> GNSRSGKSKAWWGNTLRRTPR
FT SPYRRD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7760845"
FT /id="VSP_000923"
FT VAR_SEQ 1669..2203
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7760845"
FT /id="VSP_000924"
FT VAR_SEQ 1686..1691
FT /note="AGLRTL -> MLERML (in isoform 13)"
FT /evidence="ECO:0000303|PubMed:1648940"
FT /id="VSP_000925"
FT VAR_SEQ 1692..2203
FT /note="Missing (in isoform 13)"
FT /evidence="ECO:0000303|PubMed:1648940"
FT /id="VSP_000926"
FT MUTAGEN 1656..1657
FT /note="IQ->AA: Loss of calcium-dependent inactivation
FT related to the C-terminal lobe of calmodulin."
FT /evidence="ECO:0000269|PubMed:17050707"
FT CONFLICT 124
FT /note="D -> N (in Ref. 2; AAA42015)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="S -> Y (in Ref. 2; AAA42015)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="S -> Y (in Ref. 2; AAA42015)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="G -> C (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 522..560
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1452
FT /note="W -> R (in Ref. 5; AAA89156)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2203 AA; 250136 MW; 8E746A8D988050C6 CRC64;
MMMMMMMKKM QHQRQQQEDH ANEANYARGT RLPISGEGPT SQPNSSKQTV LSWQAAIDAA
RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS RPARALFCLS LNNPIRRACI
SIVDWKPFDI FILLAIFANC VALAIYIPFP EDDSNSTNHN LEKVEYAFLI IFTVETFLKI
IASGLLLHPN ASVRNGWNLL DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR
AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT
CFFADSDIVA EEDPAPCAFS GNGRQCAANG TECRSGWVGP NGGITNFDNF AFAMLTVFQC
ITMEGWTDVL YWVNDAIGWE WPWVYFVSLI ILGSFFVLNL VLGVLSGEFS KEREKAKARG
DFQKLREKQQ LEEDLKGYLD WITQAEDIDP ENEEEGGEEG KRNTSMPTSE TESVNTENVS
GEGETQGCCG SLWCWWKRRG AAKTGPSGCR RWGQAISKSK LRSHGAREAL CVCRCSLESL
VKLWTSRFSA HLQAAYVRPY SRRWRRWNRF NRRRCRAAVK SVTFYWLVIV LVFLNTLTIS
SEHYNQPDWL TQIQDIANKV LLALFTCEML VKMYSLGLQA YFVSLFNRFD CFVVCGGITE
TILVELELMS PLGVSVFRCV RLLRIFKVTR HWTSLSNLVA SLLNSMKSIA SLLLLLFLFI
IIFSLLGMQL FGGKFNFDET QTKRSTFDNF PQALLTVFQI LTGEDWNAVM YDGIMAYGGP
SSSGMIVCIY FIILFICGNY ILLKLFLAIA VDNLADAESL NTAQKEEAEE KERKKIARKE
SLENKKNNKP EVNQIANSDN KVTIDDYQEE AEDKDPYPPC DVPVGEEEEE EEEDEPEVPA
GPRPRRISEL NMKEKIAPIP EGSAFFILSK TNPIRVGCHK LINHHIFTNL ILVFIMLSSA
ALAAEDPIRS HSFRNTILGY FDYAFTAIFT VEILLKMTTF GAFLHKGAFC RNYFNLLDML
VVGVSLVSFG IQSSAISVVK ILRVLRVLRP LRAINRAKGL KHVVQCVFVA IRTIGNIMIV
TTLLQFMFAC IGVQLFKGKF YRCTDEAKSN PEECRGLFIL YKDGDVDSPV VRERIWQNSD
FNFDNVLSAM MALFTVSTFE GWPALLYKAI DSNGENVGPV YNYRVEISIF FIIYIIIVAF
FMMNIFVGFV IVTFQEQGEK EYKNCELDKN QRQCVEYALK ARPLRRYIPK NPYQYKFWYV
VNSSPFEYMM FVLIMLNTLC LAMQHYEQSK MFNDAMDILN MVFTGVFTVE MVLKVIAFKP
KGYFSDAWNT FDSLIVIGSI IDVALSEADN SEESNRISIT FFRLFRVMRL VKLLSRGEGI
RTLLWTFIKS FQALPYVALL IAMLFFIYAV IGMQMFGKVA MRDNNQINRN NNFQTFPQAV
LLLFRCATGE AWQEIMLACL PGKLCDPDSD YNPGEEYTCG SNFAIVYFIS FYMLCAFLII
NLFVAVIMDN FDYLTRDWSI LGPHHLDEFK RIWSEYDPEA KGRIKHLDVV TLLRRIQPPL
GFGKLCPHRV ACKRLVAMNM PLNSDGTVMF NATLFALVRT ALKIKTEGNL EQANEELRAV
IKKIWKKTSM KLLDQVVPPA GDDEVTVGKF YATFLIQDYF RKFKKRKEQG LVGKYPAKNT
TIALQAGLRT LHDIGPEIRR AISCDLQDDE PEDSKPEEED VFKRNGALLG NYVNHVNSDR
RESLQQTNTT HRPLHVQRPS IPPASDTEKP LFPPAGNSVC HNHHNHNSIG KQVPTSTNAN
LNNANMSKAA HGKRPSIGDL EHVSENGHYS YKHDRELQRR SSIKRTRYYE TYIRSESGDE
QLPTIFREDP EIHGYFRDPR CFGEQEYFSS EECCEDDSSP TWSRQNYSYY NRYPGSSMDF
ERPRGYHHPQ GFLEDDDSPI GYDSRRSPRR RLLPPTPPSH RRSSFNFECL RRQNSQDDVL
PSPALPHRAA LPLHLMQQQI MAVAGLDSSK AQKYSPSHST RSWATPPATP PYRDWTPCYT
PLIQVDRSES MDQVNGSLPS LHRSSWYTDE PDISYRTFTP ASLTVPSSFR NKNSDKQRSA
DSLVEAVLIS EGLGRYARDP KFVSATKHEI ADACDLTIDE MESAASTLLN GSVCPRANGD
MGPISHRQDY ELQDFGPGYS DEEPDPGREE EDLADEMICI TTL
