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 (TC
CC 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 Genevisible; O55017; MM.
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.
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
//
