ID   CAC1B_MOUSE             Reviewed;        2327 AA.
AC   O55017; Q60609;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 207.
DE   RecName: Full=Voltage-dependent N-type calcium channel subunit alpha-1B;
DE   AltName: Full=Brain calcium channel III;
DE            Short=BIII;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 5;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.2;
GN   Name=Cacna1b; Synonyms=Cach5, Cacnl1a5, Cchn1a;
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].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Hong T., Birnbaumer L.;
RT   "Nucleotide sequence polymorphism of mouse alpha1 B.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS NB1 AND NB2), AND VARIANT ALA-414 INS.
RC   TISSUE=Neuroblastoma;
RX   PubMed=8307146; DOI=10.1016/0014-5793(94)80105-3;
RA   Coppola T., Waldmann R., Borsotto M., Heurteaux C., Romey G., Mattei M.-G.,
RA   Lazdunski M.;
RT   "Molecular cloning of a murine N-type calcium channel alpha 1 subunit.
RT   Evidence for isoforms, brain distribution, and chromosomal localization.";
RL   FEBS Lett. 338:1-5(1994).
RN   [3]
RP   INTERACTION WITH RIMS1.
RC   TISSUE=Brain;
RX   PubMed=11438518; DOI=10.1074/jbc.m100929200;
RA   Coppola T., Magnin-Luethi S., Perret-Menoud V., Gattesco S., Schiavo G.,
RA   Regazzi R.;
RT   "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25,
RT   and synaptotagmin.";
RL   J. Biol. Chem. 276:32756-32762(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-745; SER-748;
RP   SER-783; SER-1058; SER-2056; SER-2212; SER-2221 AND SER-2244, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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 expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-22, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [8]
RP   INTERACTION WITH FMR1.
RX   PubMed=24709664; DOI=10.1038/ncomms4628;
RA   Ferron L., Nieto-Rostro M., Cassidy J.S., Dolphin A.C.;
RT   "Fragile X mental retardation protein controls synaptic vesicle exocytosis
RT   by modulating N-type calcium channel density.";
RL   Nat. Commun. 5:3628-3628(2014).
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. This alpha-1B subunit gives rise to N-type
CC       calcium currents. N-type calcium channels belong to the 'high-voltage
CC       activated' (HVA) group. They are involved in pain signaling. Calcium
CC       channels containing alpha-1B subunit may play a role in directed
CC       migration of immature neurons. Mediates Ca(2+) release probability at
CC       hippocampal neuronal soma and synaptic terminals (By similarity).
CC       {ECO:0000250|UniProtKB:Q02294}.
CC   -!- ACTIVITY REGULATION: Is specifically blocked by omega-conotoxin GVIA
CC       (By similarity). Is specifically blocked by omega-conotoxin MVIIA
CC       (ziconotide) (By similarity). Is insensitive to dihydropyridines (DHP).
CC       {ECO:0000250|UniProtKB:Q00975, ECO:0000250|UniProtKB:Q02294}.
CC   -!- SUBUNIT: Multisubunit complex consisting of alpha-1, alpha-2, beta and
CC       delta subunits in a 1:1:1:1 ratio. The channel activity is directed by
CC       the pore-forming and voltage-sensitive alpha-1 subunit. In many cases,
CC       this subunit is sufficient to generate voltage-sensitive calcium
CC       channel activity. The auxiliary subunits beta and alpha-2/delta linked
CC       by a disulfide bridge regulate the channel activity. Interacts with
CC       RIMS1 (PubMed:11438518). Interacts with FMR1 (via C-terminus); this
CC       interaction induces a decrease in the number of presynaptic functional
CC       CACNA1B channels at the cell surface (PubMed:24709664).
CC       {ECO:0000269|PubMed:11438518, ECO:0000269|PubMed:24709664}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q00975}; Multi-
CC       pass membrane protein {ECO:0000250|UniProtKB:Q00975}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=NB1;
CC         IsoId=O55017-1; Sequence=Displayed;
CC       Name=NB2;
CC         IsoId=O55017-2; Sequence=VSP_000883;
CC   -!- TISSUE SPECIFICITY: Widespread expression throughout the brain. Highest
CC       levels in pyramidal cell layers C1, C2 and C3 of the hippocampus, in
CC       the dentate gyrus, in the cortex layers 2 et 4, in the subiculum and
CC       the habenula.
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   -!- PTM: Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. CACNA1B subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB60437.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF042317; AAB97840.1; -; mRNA.
DR   EMBL; U04999; AAB60437.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS38065.1; -. [O55017-1]
DR   PIR; S41080; S41080.
DR   RefSeq; NP_001035993.1; NM_001042528.2. [O55017-1]
DR   AlphaFoldDB; O55017; -.
DR   BMRB; O55017; -.
DR   SMR; O55017; -.
DR   BioGRID; 198431; 20.
DR   IntAct; O55017; 2.
DR   MINT; O55017; -.
DR   STRING; 10090.ENSMUSP00000037416; -.
DR   ChEMBL; CHEMBL3637936; -.
DR   TCDB; 1.A.1.11.9; the voltage-gated ion channel (vic) superfamily.
DR   GlyCosmos; O55017; 3 sites, No reported glycans.
DR   GlyGen; O55017; 5 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; O55017; -.
DR   PhosphoSitePlus; O55017; -.
DR   SwissPalm; O55017; -.
DR   MaxQB; O55017; -.
DR   PaxDb; 10090-ENSMUSP00000037416; -.
DR   ProteomicsDB; 273879; -. [O55017-1]
DR   ProteomicsDB; 273880; -. [O55017-2]
DR   Antibodypedia; 32538; 161 antibodies from 28 providers.
DR   DNASU; 12287; -.
DR   Ensembl; ENSMUST00000041342.12; ENSMUSP00000037416.6; ENSMUSG00000004113.20. [O55017-1]
DR   GeneID; 12287; -.
DR   KEGG; mmu:12287; -.
DR   UCSC; uc008ipe.2; mouse. [O55017-1]
DR   AGR; MGI:88296; -.
DR   CTD; 774; -.
DR   MGI; MGI:88296; Cacna1b.
DR   VEuPathDB; HostDB:ENSMUSG00000004113; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   GeneTree; ENSGT00940000155275; -.
DR   InParanoid; O55017; -.
DR   OMA; DPNKECA; -.
DR   OrthoDB; 1110761at2759; -.
DR   TreeFam; TF312805; -.
DR   Reactome; R-MMU-112308; Presynaptic depolarization and calcium channel opening.
DR   BioGRID-ORCS; 12287; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Cacna1b; mouse.
DR   PRO; PR:O55017; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; O55017; Protein.
DR   Bgee; ENSMUSG00000004113; Expressed in supraoptic nucleus and 134 other cell types or tissues.
DR   ExpressionAtlas; O55017; baseline and differential.
DR   GO; GO:0043679; C:axon terminus; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0048786; C:presynaptic active zone; IDA:SynGO.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:MGI.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
DR   GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; ISO:MGI.
DR   GO; GO:0070509; P:calcium ion import; ISO:MGI.
DR   GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IMP:MGI.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR   GO; GO:0007269; P:neurotransmitter secretion; IMP:MGI.
DR   GO; GO:0001956; P:positive regulation of neurotransmitter secretion; ISO:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0051924; P:regulation of calcium ion transport; IMP:MGI.
DR   GO; GO:0150037; P:regulation of calcium-dependent activation of synaptic vesicle fusion; ISO:MGI.
DR   GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR   GO; GO:1904645; P:response to amyloid-beta; ISO:MGI.
DR   GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR   GO; GO:0048265; P:response to pain; IMP:MGI.
DR   GO; GO:0033574; P:response to testosterone; ISO:MGI.
DR   Gene3D; 1.10.287.70; -; 4.
DR   Gene3D; 6.10.250.2180; -; 1.
DR   Gene3D; 6.10.250.2500; -; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005447; VDCC_N_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR45628; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR   PANTHER; PTHR45628:SF6; VOLTAGE-DEPENDENT N-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1B; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01631; NVDCCALPHA1.
DR   SMART; SM01062; Ca_chan_IQ; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   Genevisible; O55017; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Calcium; Calcium channel;
KW   Calcium transport; Disulfide bond; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Metal-binding; Methylation; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..2327
FT                   /note="Voltage-dependent N-type calcium channel subunit
FT                   alpha-1B"
FT                   /id="PRO_0000053922"
FT   TOPO_DOM        1..90
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        91..114
FT                   /note="Helical; Name=S1 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        115..131
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        132..152
FT                   /note="Helical; Name=S2 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        153..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        164..182
FT                   /note="Helical; Name=S3 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        183..187
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        188..211
FT                   /note="Helical; Name=S4 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        212..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        222..244
FT                   /note="Helical; Name=S5 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        245..331
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        332..356
FT                   /note="Helical; Name=S6 of repeat I"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        357..482
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        483..501
FT                   /note="Helical; Name=S1 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        502..511
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        512..534
FT                   /note="Helical; Name=S2 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        535..544
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        545..566
FT                   /note="Helical; Name=S3 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        567..573
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        574..586
FT                   /note="Helical; Name=S4 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        587..604
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        605..630
FT                   /note="Helical; Name=S5 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        631..682
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        683..709
FT                   /note="Helical; Name=S6 of repeat II"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        710..1140
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1141..1159
FT                   /note="Helical; Name=S1 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1160..1167
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1168..1192
FT                   /note="Helical; Name=S2 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1193..1206
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1207..1231
FT                   /note="Helical; Name=S3 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1232..1237
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1238..1258
FT                   /note="Helical; Name=S4 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1259..1276
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1277..1296
FT                   /note="Helical; Name=S5 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1297..1383
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1384..1409
FT                   /note="Helical; Name=S6 of repeat III"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1410..1464
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1465..1483
FT                   /note="Helical; Name=S1 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1484..1491
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1492..1516
FT                   /note="Helical; Name=S2 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1517..1526
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1527..1548
FT                   /note="Helical; Name=S3 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1549..1554
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1555..1573
FT                   /note="Helical; Name=S4 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1574..1592
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1593..1612
FT                   /note="Helical; Name=S5 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1613..1674
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TRANSMEM        1675..1698
FT                   /note="Helical; Name=S6 of repeat IV"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   TOPO_DOM        1699..2327
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   REPEAT          82..359
FT                   /note="I"
FT   REPEAT          468..712
FT                   /note="II"
FT   REPEAT          1126..1412
FT                   /note="III"
FT   REPEAT          1449..1702
FT                   /note="IV"
FT   DOMAIN          1715..1750
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..396
FT                   /note="Binding to the beta subunit"
FT                   /evidence="ECO:0000250"
FT   REGION          801..1015
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1042..1066
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1972..2193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2230..2249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2273..2292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..821
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..937
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        957..1015
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1050..1066
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2005..2022
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2038..2054
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2085..2108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2152..2193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         451..458
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         544
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   BINDING         584
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   BINDING         587
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-4,5-bisphosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58456"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   BINDING         1728
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         1734
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         1739
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   SITE            314
FT                   /note="Calcium ion selectivity and permeability"
FT                   /evidence="ECO:0000250"
FT   SITE            663
FT                   /note="Calcium ion selectivity and permeability"
FT                   /evidence="ECO:0000250"
FT   SITE            1358
FT                   /note="Calcium ion selectivity and permeability"
FT                   /evidence="ECO:0000250"
FT   SITE            1646
FT                   /note="Calcium ion selectivity and permeability"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         22
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         411
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         745
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         748
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         783
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1058
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2056
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2212
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00975"
FT   CARBOHYD        1554
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1666
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         756
FT                   /note="A -> AFVKQTRGTVSRSSSVSSVNSP (in isoform NB2)"
FT                   /evidence="ECO:0000303|PubMed:8307146"
FT                   /id="VSP_000883"
FT   VARIANT         414
FT                   /note="D -> DA"
FT                   /evidence="ECO:0000269|PubMed:8307146"
FT   CONFLICT        238
FT                   /note="A -> G (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        645
FT                   /note="N -> I (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        757..759
FT                   /note="RQQ -> QE (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        880
FT                   /note="A -> P (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1128
FT                   /note="L -> F (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1173
FT                   /note="K -> E (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1185
FT                   /note="F -> C (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1227..1230
FT                   /note="Missing (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1388
FT                   /note="F -> L (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1549
FT                   /note="A -> AET (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1615
FT                   /note="I -> S (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1636
FT                   /note="L -> I (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1657
FT                   /note="G -> D (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1802..1837
FT                   /note="Missing (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1942
FT                   /note="A -> G (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1949
FT                   /note="G -> D (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1963
FT                   /note="A -> L (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1979
FT                   /note="E -> D (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1994
FT                   /note="P -> L (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2021
FT                   /note="H -> D (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2075
FT                   /note="A -> AA (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2141
FT                   /note="T -> A (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2168
FT                   /note="S -> I (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2309
FT                   /note="S -> N (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2313
FT                   /note="R -> G (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2316
FT                   /note="H -> A (in Ref. 2; AAB60437)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2327 AA;  261481 MW;  AD42CDD38482895A CRC64;
     MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA QRARTMALYN
     PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD
     GDKTPMSERL DDTEPYFIGI FCFEAGIKII ALGFVFHKGS YLRNGWNVMD FVVVLTGILA
     TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII
     GLEFYMGKFH KACFPNSTDT EPVGDFPCGK DPPARQCDGD TECREYWPGP NFGITNFDNI
     LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA
     KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDKNAEEK SPLDVLKRAA
     TKKSRNDLIH AEEGEDRFVD LCAVGSPFAR ASLKSGKTES SSYFRRKEKM FRFFIRRMVK
     AQSFYWVVLC VVALNTLCVA MVHYNQPQRL TTALYFAEFV FLGLFLTEMS LKMYGLGPRS
     YFRSSFNCFD FGVIVGSIFE VVWAAIKPGT SFGISVLRAL RLLRIFKVTK YWNSLRNLVV
     SLLNSMKSII SLLFLLFLFI VVFALLGMQL FGGQFNFQDE TPTTNFDTFP AAILTVFQIL
     TGEDWNAVMY HGIESQGGVS KGMFSSFYFI VLTLFGNYTL LNVFLAIAVD NLANAQELTK
     DEEEMEEAAN QKLALQKAKE VAEVSPMSAA NISIAARQQN SAKARSVWEQ RASQLRLQNL
     RASCEALYSE MDPEERLRYA STRHVRPDMK THMDRPLVVE PGRDGLRGPV GSKSKPEGTE
     ATESADLPRR HHRHRDRDKT SATAPAGGEQ DRTESTETGA REERARPRRS HSKETPGADT
     QVRCERSRRH HRRGSPEEAT EREPRRHRAH RHAQDSSKEG TAPVLVPKGE RRARHRGPRT
     GPREAENNEE PTRRHRARHK VPPTLQPPER EAAEKESNAV EGDKETRNHQ PKEPHCDLEA
     IAVTGVGPLH MLPSTCLQKV DEQPEDADNQ RNVTRMGSQP SDPSTTVHVP VTLTGPPGET
     PVVPSGNMNL EGQAEGKKEA EADDVLRRGP RPIVPYSSMF CLSPTNLLRR FCHYIVTMRY
     FEMVILVVIA LSSIALAAED PVRTDSFRNN ALKYMDYIFT GVFTFEMVIK MIDLGLLLHP
     GAYFRDLWNI LDFIVVSGAL VAFAFSSFMG GSKGKDINTI KSLRVLRVLR PLKTIKRLPK
     LKAVFDCVVN SLKNVLNILI VYMLFMFIFA VIAVQLFKGK FFYCTDESKE LERDCRGQYL
     DYEKEEVEAQ PRQWKKYDFH YDNVLWALLT LFTVSTGEGW PMVLKHSVDA TYEEQGPSPG
     FRMELSIFYV VYFVVFPFFF VNIFVALIII TFQEQGDKVM SECSLEKNER ACIDFAISAK
     PLTRYMPQNK QSFQYKTWTF VVSPPFEYFI MAMIALNTVV LMMKFYDAPY EYELMLKCLN
     IVFTSMFSME CILKIIAFGV LNYFRDAWNV FDFVTVLGSI TDILVTEIAN NFINLSFLRL
     FRAARLIKLL RQGYTIRILL WTFVQSFKAL PYVCLLIAML FFIYAIIGMQ VFGNIALDDD
     TSINRHNNFR TFLQALMLLF RSATGEAWHE IMLSCLGNRA CDPHANASEC GSDFAYFYFV
     SFIFLCSFLM LNLFVAVIMD NFEYLTRDSS ILGPHHLDEF IRVWAEYDPA ACGRISYNDM
     FEMLKHMSPP LGLGKKCPAR VAYKRLVRMN MPISNEDMTV HFTSTLMALI RTALEIKLAP
     AGTKQHQCDA ELRKEISSVW ANLPQKTLDL LVPPHKPDEM TVGKVYAALM IFDFYKQNKT
     TRDQTHQAPG GLSQMGPVSL FHPLKATLEQ TQPAVLRGAR VFLRQKSATS LSNGGAIQTQ
     ESGIKESLSW GTQRTQDALY EARAPLERGH SAEIPVGQSG TLAVDVQMQN MTLRGPDGEP
     QPGLESQGRA ASMPRLAAET QPAPNASPMK RSISTLAPRP HGTQLCSTVL DRPPPSQASH
     HHHHRCHRRR DKKQRSLEKG PSLSVDPEGA PSTAAGPGLP HGEGSTACRR DRKQERGRSQ
     ERRQPSSSSS EKQRFYSCDR FGSREPPQLM PSLSSHPTSP TAALEPAPHP QGSGSVNGSP
     LMSTSGASTP GRGGRRQLPQ TPLTPRPSIT YKTANSSPVH FAEGQSGLPA FSPGRLSRGL
     SEHNALLQKE PLSQPLAPGS RIGSDPYLGQ RLDSEASAHT LPEDTLTFEE AVATNSGRSS
     RTSYVSSLTS QSHPLRRVPN GYHCTLGLST GVRARHSYHH PDQDHWC
//