CAC1B_RAT
ID CAC1B_RAT Reviewed; 2336 AA.
AC Q02294;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
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;
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], FUNCTION, INTERACTION WITH THE OMEGA-CONOTOXIN
RP GVIA, AND ACTIVITY REGULATION.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=1317580; DOI=10.1073/pnas.89.11.5058;
RA Dubel S.J., Starr T.V.B., Hell J.W., Ahlijanian M.K., Enyeart J.J.,
RA Catterall W.A., Snutch T.P.;
RT "Molecular cloning of the alpha-1 subunit of an omega-conotoxin-sensitive
RT calcium channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5058-5062(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1516-1679 (CLONE RBB-10).
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 [3]
RP PHOSPHORYLATION.
RX PubMed=8125957; DOI=10.1016/s0021-9258(17)37297-6;
RA Hell J.W., Appleyard S.M., Yokoyama C.T., Warner C., Catterall W.A.;
RT "Differential phosphorylation of two size forms of the N-type calcium
RT channel alpha 1 subunit which have different COOH termini.";
RL J. Biol. Chem. 269:7390-7396(1994).
RN [4]
RP BETA-SUBUNIT BINDING DOMAIN.
RX PubMed=7509046; DOI=10.1038/368067a0;
RA Pragnell M., de Waard M., Mori Y., Tanabe T., Snutch T.P., Campbell K.P.;
RT "Calcium channel beta-subunit binds to a conserved motif in the I-II
RT cytoplasmic linker of the alpha 1-subunit.";
RL Nature 368:67-70(1994).
RN [5]
RP ACTIVITY REGULATION.
RX PubMed=10938268; DOI=10.1074/jbc.m002252200;
RA Lewis R.J., Nielsen K.J., Craik D.J., Loughnan M.L., Adams D.A.,
RA Sharpe I.A., Luchian T., Adams D.J., Bond T., Thomas L., Jones A.,
RA Matheson J.-L., Drinkwater R., Andrews P.R., Alewood P.F.;
RT "Novel omega-conotoxins from Conus catus discriminate among neuronal
RT calcium channel subtypes.";
RL J. Biol. Chem. 275:35335-35344(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-746 AND SER-2253,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [7]
RP FUNCTION.
RX PubMed=23699505; DOI=10.1523/jneurosci.4288-12.2013;
RA Kim S.H., Ryan T.A.;
RT "Balance of calcineurin Aalpha and CDK5 activities sets release probability
RT at nerve terminals.";
RL J. Neurosci. 33:8937-8950(2013).
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 (PubMed:23699505).
CC {ECO:0000269|PubMed:23699505}.
CC -!- ACTIVITY REGULATION: Is specifically blocked by omega-conotoxin GVIA
CC (Probable) (PubMed:10938268). Is specifically blocked by omega-
CC conotoxin MVIIA (ziconotide) (By similarity). Is insensitive to
CC dihydropyridines (DHP). {ECO:0000250|UniProtKB:Q00975,
CC ECO:0000269|PubMed:10938268, ECO:0000305|PubMed:1317580}.
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. Interacts with FMR1 (via C-terminus); this interaction induces a
CC decrease in the number of presynaptic functional CACNA1B channels at
CC the cell surface. {ECO:0000250|UniProtKB:O55017}.
CC -!- INTERACTION:
CC Q02294; P21707: Syt1; NbExp=2; IntAct=EBI-540038, EBI-458098;
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=1;
CC Comment=2 isoforms may be produced.;
CC Name=1;
CC IsoId=Q02294-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Central nervous system.
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:0000269|PubMed:8125957}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1B subfamily. {ECO:0000305}.
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DR EMBL; M92905; AAA42014.1; -; mRNA.
DR PIR; B35901; B35901.
DR PDB; 4DEX; X-ray; 2.00 A; B=358-468.
DR PDBsum; 4DEX; -.
DR AlphaFoldDB; Q02294; -.
DR SMR; Q02294; -.
DR CORUM; Q02294; -.
DR IntAct; Q02294; 4.
DR MINT; Q02294; -.
DR STRING; 10116.ENSRNOP00000006162; -.
DR BindingDB; Q02294; -.
DR ChEMBL; CHEMBL5107; -.
DR DrugCentral; Q02294; -.
DR GuidetoPHARMACOLOGY; 533; -.
DR GlyGen; Q02294; 3 sites.
DR iPTMnet; Q02294; -.
DR PhosphoSitePlus; Q02294; -.
DR PaxDb; Q02294; -.
DR PRIDE; Q02294; -.
DR UCSC; RGD:628852; rat. [Q02294-1]
DR RGD; 628852; Cacna1b.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; Q02294; -.
DR PhylomeDB; Q02294; -.
DR Reactome; R-RNO-112308; Presynaptic depolarization and calcium channel opening.
DR PRO; PR:Q02294; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; EXP:SynGO.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; EXP:SynGO.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; ISO:RGD.
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:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:RGD.
DR GO; GO:0099635; F:voltage-gated calcium channel activity involved in positive regulation of presynaptic cytosolic calcium levels; EXP:SynGO.
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; IMP:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0007269; P:neurotransmitter secretion; ISO:RGD.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IMP:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:RGD.
DR GO; GO:0008016; P:regulation of heart contraction; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:1904645; P:response to amyloid-beta; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
DR GO; GO:0048265; P:response to pain; ISO:RGD.
DR GO; GO:0033574; P:response to testosterone; IMP:RGD.
DR GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
DR Gene3D; 1.20.120.350; -; 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; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR PANTHER; PTHR10037:SF289; PTHR10037:SF289; 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 PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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..2336
FT /note="Voltage-dependent N-type calcium channel subunit
FT alpha-1B"
FT /id="PRO_0000053924"
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..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 484..502
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 503..512
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 513..535
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 536..545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 546..567
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 568..574
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 575..587
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 588..605
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 606..631
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 632..683
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 684..710
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 711..1149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1150..1168
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1169..1176
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1177..1201
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1202..1215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1216..1240
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1241..1246
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1247..1267
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1268..1285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1286..1305
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1306..1392
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1393..1418
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1419..1473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1474..1492
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1493..1500
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1501..1525
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1526..1535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1536..1557
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1558..1563
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1564..1582
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1583..1601
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1602..1621
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1622..1683
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TRANSMEM 1684..1707
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT TOPO_DOM 1708..2336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT REPEAT 82..359
FT /note="I"
FT REPEAT 469..713
FT /note="II"
FT REPEAT 1135..1421
FT /note="III"
FT REPEAT 1458..1711
FT /note="IV"
FT DOMAIN 1724..1759
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 REGION 800..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1981..2202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..945
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2014..2031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2047..2063
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2094..2117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2161..2202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 452..459
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 545
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 585
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 588
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 1737
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1743
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 1748
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT SITE 314
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 664
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1367
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1655
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT MOD_RES 22
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 1067
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 2065
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 2221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 2230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 2253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q00975"
FT CARBOHYD 1563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 1538
FT /note="N -> D (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 1579
FT /note="C -> L (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 364..403
FT /evidence="ECO:0007829|PDB:4DEX"
SQ SEQUENCE 2336 AA; 262256 MW; 8D50AF67834FD1BC CRC64;
MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA QRARTMALYN
PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD
GDKTPMSERL DDTEPYFIGI FCFEAGIKII ALGFVFHKGS YLRNGWNVMD FVVVLTEILA
TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII
GLEFYMGKFH KACFPNSTDA EPVGDFPCGK EAPARLCDSD TECREYWPGP NFGITNFDNI
LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA
KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDKNAEEK SPLDAVLKRA
ATKKSRNDLI HAEEGEDRFV DLCAAGSPFA RASLKSGKTE SSSYFRRKEK MFRFLIRRMV
KAQSFYWVVL CVVALNTLCV AMVHYNQPQR LTTALYFAEF VFLGLFLTEM SLKMYGLGPR
SYFRSSFNCF DFGVIVGSIF EVVWAAIKPG TSFGISVLRA LRLLRIFKVT KYWNSLRNLV
VSLLNSMKSI ISLLFLLFLF IVVFALLGMQ LFGGQFNFQD ETPTTNFDTF PAAILTVFQI
LTGEDWNAVM YHGIESQGGV SKGMFSSFYF IVLTLFGNYT LLNVFLAIAV DNLANAQELT
KDEEEMEEAA NQKLALQKAK EVAEVSPMSA ANISIAARQQ NSAKARSVWE QRASQLRLQN
LRASCEALYS EMDPEERLRY ASTRHVRPDM KTHMDRPLVV EPGRDGLRGP AGNKSKPEGT
EATEGADPPR RHHRHRDRDK TSASTPAGGE QDRTDCPKAE STETGAREER ARPRRSHSKE
APGADTQVRC ERSRRHHRRG SPEEATEREP RRHRAHRHAQ DSSKEGKEGT APVLVPKGER
RARHRGPRTG PRETENSEEP TRRHRAKHKV PPTLEPPERE VAEKESNVVE GDKETRNHQP
KEPRCDLEAI AVTGVGSLHM LPSTCLQKVD EQPEDADNQR NVTRMGSQPS DPSTTVHVPV
TLTGPPGEAT VVPSANTDLE GQAEGKKEAE ADDVLRRGPR PIVPYSSMFC LSPTNLLRRF
CHYIVTMRYF EMVILVVIAL SSIALAAEDP VRTDSFRNNA LKYMDYIFTG VFTFEMVIKM
IDLGLLLHPG AYFRDLWNIL DFIVVSGALV AFAFSSFMGG SKGKDINTIK SLRVLRVLRP
LKTIKRLPKL KAVFDCVVNS LKNVLNILIV YMLFMFIFAV IAVQLFKGKF FYCTDESKEL
ERDCRGQYLD YEKEEVEAQP RQWKKYDFHY DNVLWALLTL FTVSTGEGWP MVLKHSVDAT
YEEQGPSPGF RMELSIFYVV YFVVFPFFFV NIFVALIIIT FQEQGDKVMS ECSLEKNERA
CIDFAISAKP LTRYMPQNKQ SFQYKTWTFV VSPPFEYFIM AMIALNTVVL MMKFYDAPYE
YELMLKCLNI VFTSMFSLEC ILKIIAFGVL NYFRDAWNVF DFVTVLGSIT DILVTEIANN
FINLSFLRLF RAARLIKLCR QGYTIRILLW TFVQSFKALP YVCLLIAMLF FIYAIIGMQV
FGNIALDDGT SINRHNNFRT FLQALMLLFR SATGEAWHEI MLSCLGNRAC DPHANASECG
SDFAYFYFVS FIFLCSFLML NLFVAVIMDN FEYLTRDSSI LGPHHLDEFI RVWAEYDPAA
CGRISYNDMF EMLKHMSPPL GLGKKCPARV AYKRLVRMNM PISNEDMTVH FTSTLMALIR
TALEIKLAPA GTKQHQCDAE LRKEISSVWA NLPQKTLDLL VPPHKPDEMT VGKVYAALMI
FDFYKQNKTT RDQTHQAPGG LSQMGPVSLF HPLKATLEQT QPAVLRGARV FLRQKSATSL
SNGGAIQTQE SGIKESLSWG TQRTQDVLYE ARAPLERGHS AEIPVGQPGA LAVDVQMQNM
TLRGPDGEPQ PGLESQGRAA SMPRLAAETQ PAPNASPMKR SISTLAPRPH GTQLCNTVLD
RPPPSQVSHH HHHRCHRRRD KKQRSLEKGP SLSVDTEGAP STAAGSGLPH GEGSTGCRRE
RKQERGRSQE RRQPSSSSSE KQRFYSCDRF GSREPPQPKP SLSSHPISPT AALEPGPHPQ
GSGSVNGSPL MSTSGASTPG RGGRRQLPQT PLTPRPSITY KTANSSPVHF AEGQSGLPAF
SPGRLSRGLS EHNALLQKEP LSQPLASGSR IGSDPYLGQR LDSEASAHNL PEDTLTFEEA
VATNSGRSSR TSYVSSLTSQ SHPLRRVPNG YHCTLGLSTG VRARHSYHHP DQDHWC
