CAC1B_HUMAN
ID CAC1B_HUMAN Reviewed; 2339 AA.
AC Q00975; B1AQK5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 201.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1B-1 AND ALPHA-1B-2).
RC TISSUE=Brain;
RX PubMed=1321501; DOI=10.1126/science.1321501;
RA Williams M.E., Brust P.F., Feldman D.H., Patthi S., Simerson S.,
RA Maroufi A., McCue A.F., Velicelebi G., Ellis S.B., Harpold M.M.;
RT "Structure and functional expression of an omega-conotoxin-sensitive human
RT N-type calcium channel.";
RL Science 257:389-395(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94.
RC TISSUE=Lung fibroblast;
RX PubMed=9030575; DOI=10.1074/jbc.272.8.5098;
RA Kim D.S., Jung H.-H., Park S.-H., Chin H.;
RT "Isolation and characterization of the 5'-upstream region of the human N-
RT type calcium channel alpha1B subunit gene. Chromosomal localization and
RT promoter analysis.";
RL J. Biol. Chem. 272:5098-5104(1997).
RN [4]
RP VARIANT HIS-1389, AND CHARACTERIZATION OF VARIANT HIS-1389.
RX PubMed=25296916; DOI=10.1093/hmg/ddu513;
RA Groen J.L., Andrade A., Ritz K., Jalalzadeh H., Haagmans M., Bradley T.E.,
RA Jongejan A., Verbeek D.S., Nuernberg P., Denome S., Hennekam R.C.,
RA Lipscombe D., Baas F., Tijssen M.A.;
RT "CACNA1B mutation is linked to unique myoclonus-dystonia syndrome.";
RL Hum. Mol. Genet. 24:987-993(2015).
RN [5]
RP VARIANT HIS-1389.
RX PubMed=26157024; DOI=10.1093/hmg/ddv255;
RA Mencacci N.E., R'bibo L., Bandres-Ciga S., Carecchio M., Zorzi G.,
RA Nardocci N., Garavaglia B., Batla A., Bhatia K.P., Pittman A.M., Hardy J.,
RA Weissbach A., Klein C., Gasser T., Lohmann E., Wood N.W.;
RT "The CACNA1B R1389H variant is not associated with myoclonus-dystonia in a
RT large European multicentric cohort.";
RL Hum. Mol. Genet. 24:5326-5329(2015).
RN [6]
RP VARIANT NEDNEH 383-ARG--CYS-2339 DEL, INVOLVEMENT IN NEDNEH, AND TISSUE
RP SPECIFICITY.
RX PubMed=30982612; DOI=10.1016/j.ajhg.2019.03.005;
RG Deciphering Developmental Disorders Study;
RG UK10K Consortium;
RG NIHR BioResource;
RA Gorman K.M., Meyer E., Grozeva D., Spinelli E., McTague A.,
RA Sanchis-Juan A., Carss K.J., Bryant E., Reich A., Schneider A.L.,
RA Pressler R.M., Simpson M.A., Debelle G.D., Wassmer E., Morton J.,
RA Sieciechowicz D., Jan-Kamsteeg E., Paciorkowski A.R., King M.D.,
RA Cross J.H., Poduri A., Mefford H.C., Scheffer I.E., Haack T.B.,
RA McCullagh G., Millichap J.J., Carvill G.L., Clayton-Smith J., Maher E.R.,
RA Raymond F.L., Kurian M.A.;
RT "Bi-allelic loss-of-function CACNA1B mutations in progressive epilepsy-
RT dyskinesia.";
RL Am. J. Hum. Genet. 104:948-956(2019).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 86-1837 IN COMPLEX WITH
RP SUBUNITS ALPHA2DELTA-1 AND BETA3 IN PRESENCE AND ABSENCE OF THE
RP OMEGA-CONOTOXIN MVIIA, TOPOLOGY, DISULFIDE BONDS, SUBCELLULAR LOCATION,
RP GLYCOSYLATION AT ASN-256, PIP2-BINDING, SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=34234349; DOI=10.1038/s41586-021-03699-6;
RA Gao S., Yao X., Yan N.;
RT "Structure of human Cav2.2 channel blocked by the painkiller ziconotide.";
RL Nature 596:143-147(2021).
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) (PubMed:34234349). Is insensitive to dihydropyridines
CC (DHP). {ECO:0000250|UniProtKB:Q02294, ECO:0000305|PubMed:34234349}.
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 Q00975; P28702: RXRB; NbExp=3; IntAct=EBI-1055161, EBI-748576;
CC Q00975; P20650: Ppm1a; Xeno; NbExp=3; IntAct=EBI-1055161, EBI-7491743;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:34234349}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:34234349}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha-1B-1;
CC IsoId=Q00975-1; Sequence=Displayed;
CC Name=Alpha-1B-2;
CC IsoId=Q00975-2; Sequence=VSP_000882;
CC -!- TISSUE SPECIFICITY: Isoform Alpha-1b-1 and isoform Alpha-1b-2 are
CC expressed in the central nervous system, but not in skeletal muscle or
CC aorta. Expressed in the cerebral white matter, cortex, hippocampus,
CC basal ganglia, and cerebellum (PubMed:30982612).
CC {ECO:0000269|PubMed:30982612}.
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 -!- DISEASE: Neurodevelopmental disorder with seizures and non-epileptic
CC hyperkinetic movements (NEDNEH) [MIM:618497]: An autosomal recessive,
CC complex and progressive neurologic disorder characterized by severe
CC neurodevelopmental delay and developmental regression, epileptic
CC encephalopathy, postnatal microcephaly, hypotonia, and non-epileptic
CC hyperkinetic movement disorder, including myoclonus dystonia,
CC choreoathetosis, or generalized dyskinesia. Disease onset in infancy or
CC first years of life. {ECO:0000269|PubMed:30982612}. Note=The disease
CC may be caused by variants affecting the gene represented in this entry.
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; M94172; AAA51897.1; -; mRNA.
DR EMBL; M94173; AAA51898.1; -; mRNA.
DR EMBL; AL591424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL772363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U76666; AAC51138.1; -; Genomic_DNA.
DR CCDS; CCDS59522.1; -. [Q00975-1]
DR CCDS; CCDS59523.1; -. [Q00975-2]
DR PIR; A42566; A42566.
DR PIR; T45115; T45115.
DR RefSeq; NP_000709.1; NM_000718.3. [Q00975-1]
DR RefSeq; NP_001230741.1; NM_001243812.1. [Q00975-2]
DR PDB; 2LCM; NMR; -; A=1242-1269.
DR PDB; 7MIX; EM; 3.00 A; A=1-2339.
DR PDB; 7MIY; EM; 3.10 A; A=1-2339.
DR PDB; 7VFS; EM; 2.80 A; A=1-2339.
DR PDB; 7VFU; EM; 3.00 A; A=1-2339.
DR PDB; 7VFV; EM; 3.00 A; A=1-2339.
DR PDB; 7VFW; EM; 3.30 A; A=1-2339.
DR PDBsum; 2LCM; -.
DR PDBsum; 7MIX; -.
DR PDBsum; 7MIY; -.
DR PDBsum; 7VFS; -.
DR PDBsum; 7VFU; -.
DR PDBsum; 7VFV; -.
DR PDBsum; 7VFW; -.
DR AlphaFoldDB; Q00975; -.
DR SMR; Q00975; -.
DR BioGRID; 107228; 10.
DR IntAct; Q00975; 8.
DR MINT; Q00975; -.
DR STRING; 9606.ENSP00000360423; -.
DR BindingDB; Q00975; -.
DR ChEMBL; CHEMBL4478; -.
DR DrugBank; DB08838; Agmatine.
DR DrugBank; DB00381; Amlodipine.
DR DrugBank; DB09231; Benidipine.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB11148; Butamben.
DR DrugBank; DB09232; Cilnidipine.
DR DrugBank; DB05950; Contulakin-G.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB00153; Ergocalciferol.
DR DrugBank; DB00996; Gabapentin.
DR DrugBank; DB01202; Levetiracetam.
DR DrugBank; DB05885; Seletracetam.
DR DrugBank; DB00421; Spironolactone.
DR DrugBank; DB00661; Verapamil.
DR DrugBank; DB06283; Ziconotide.
DR DrugCentral; Q00975; -.
DR GuidetoPHARMACOLOGY; 533; -.
DR GlyGen; Q00975; 3 sites.
DR iPTMnet; Q00975; -.
DR PhosphoSitePlus; Q00975; -.
DR BioMuta; CACNA1B; -.
DR DMDM; 1705854; -.
DR jPOST; Q00975; -.
DR MassIVE; Q00975; -.
DR PaxDb; Q00975; -.
DR PeptideAtlas; Q00975; -.
DR PRIDE; Q00975; -.
DR ProteomicsDB; 57886; -. [Q00975-1]
DR ProteomicsDB; 57887; -. [Q00975-2]
DR Antibodypedia; 32538; 136 antibodies from 28 providers.
DR DNASU; 774; -.
DR Ensembl; ENST00000277551.6; ENSP00000277551.2; ENSG00000148408.14. [Q00975-2]
DR Ensembl; ENST00000371372.6; ENSP00000360423.1; ENSG00000148408.14. [Q00975-1]
DR GeneID; 774; -.
DR KEGG; hsa:774; -.
DR MANE-Select; ENST00000371372.6; ENSP00000360423.1; NM_000718.4; NP_000709.1.
DR UCSC; uc064xny.1; human. [Q00975-1]
DR CTD; 774; -.
DR DisGeNET; 774; -.
DR GeneCards; CACNA1B; -.
DR HGNC; HGNC:1389; CACNA1B.
DR HPA; ENSG00000148408; Tissue enhanced (brain, pituitary gland, testis).
DR MalaCards; CACNA1B; -.
DR MIM; 601012; gene.
DR MIM; 618497; phenotype.
DR neXtProt; NX_Q00975; -.
DR OpenTargets; ENSG00000148408; -.
DR Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
DR PharmGKB; PA26008; -.
DR VEuPathDB; HostDB:ENSG00000148408; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000155275; -.
DR InParanoid; Q00975; -.
DR OMA; GTQCREY; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; Q00975; -.
DR PathwayCommons; Q00975; -.
DR Reactome; R-HSA-112308; Presynaptic depolarization and calcium channel opening.
DR SignaLink; Q00975; -.
DR SIGNOR; Q00975; -.
DR BioGRID-ORCS; 774; 9 hits in 1065 CRISPR screens.
DR ChiTaRS; CACNA1B; human.
DR GeneWiki; N-type_calcium_channel; -.
DR GenomeRNAi; 774; -.
DR Pharos; Q00975; Tclin.
DR PRO; PR:Q00975; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q00975; protein.
DR Bgee; ENSG00000148408; Expressed in middle temporal gyrus and 106 other tissues.
DR ExpressionAtlas; Q00975; baseline and differential.
DR Genevisible; Q00975; HS.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IBA:GO_Central.
DR GO; GO:0001540; F:amyloid-beta binding; IC:ARUK-UCL.
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; IMP:ARUK-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; TAS:ProtInc.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:ARUK-UCL.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:1904645; P:response to amyloid-beta; IDA:ARUK-UCL.
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; Disease variant; Disulfide bond; Epilepsy; Glycoprotein;
KW Intellectual disability; Ion channel; Ion transport; Membrane;
KW Metal-binding; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..2339
FT /note="Voltage-dependent N-type calcium channel subunit
FT alpha-1B"
FT /id="PRO_0000053921"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 91..114
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 115..131
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 132..152
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 153..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 164..182
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 183..187
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 188..211
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 212..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 222..244
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 245..331
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 332..356
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 357..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 483..501
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 502..511
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 512..534
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 535..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 545..566
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 567..573
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 574..586
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 587..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 605..630
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 631..682
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 683..709
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 710..1151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 1152..1170
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 1171..1178
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 1179..1203
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 1204..1217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 1218..1238
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 1239..1244
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 1245..1265
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 1266..1283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 1284..1303
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 1304..1390
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 1391..1416
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 1417..1471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 1472..1490
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 1491..1498
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 1499..1523
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 1524..1533
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 1534..1555
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 1556..1563
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 1564..1582
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 1583..1601
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 1602..1621
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 1622..1683
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TRANSMEM 1684..1707
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT TOPO_DOM 1708..2339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT REPEAT 82..359
FT /note="I"
FT REPEAT 468..712
FT /note="II"
FT REPEAT 1137..1419
FT /note="III"
FT REPEAT 1456..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 /evidence="ECO:0000250"
FT REGION 816..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1916..1968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1981..2206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1916..1945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2014..2045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2048..2064
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2096..2120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2147..2206
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:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
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:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
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:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
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 MOD_RES 22
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 1069
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 2066
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 2224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 2233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT MOD_RES 2256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55017"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
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 VAR_SEQ 2164..2339
FT /note="GSGSVNGSPLLSTSGASTPGRGGRRQLPQTPLTPRPSITYKTANSSPIHFAG
FT AQTSLPAFSPGRLSRGLSEHNALLQRDPLSQPLAPGSRIGSDPYLGQRLDSEASVHALP
FT EDTLTFEEAVATNSGRSSRTSYVSSLTSQSHPLRRVPNGYHCTLGLSSGGRARHSYHHP
FT DQDHWC -> AGSAVGFPNTTPCCRETPSASPWPLALELALTLTWGSVWTVRPLSTPCL
FT RTLSLSRRLWPPTRAAPPGLPTCPP (in isoform Alpha-1B-2)"
FT /evidence="ECO:0000303|PubMed:1321501"
FT /id="VSP_000882"
FT VARIANT 167
FT /note="N -> K (in dbSNP:rs4422842)"
FT /id="VAR_048741"
FT VARIANT 383..2339
FT /note="Missing (in NEDNEH)"
FT /evidence="ECO:0000269|PubMed:30982612"
FT /id="VAR_083051"
FT VARIANT 862
FT /note="A -> S (in dbSNP:rs7873074)"
FT /id="VAR_061100"
FT VARIANT 996
FT /note="T -> A (in dbSNP:rs11137342)"
FT /id="VAR_061101"
FT VARIANT 1389
FT /note="R -> H (found in a family with myoclonus and
FT dystonia; also found in a sporadic case; unknown
FT pathological significance; single-channel currents of the
FT mutant are smaller than wild-type, likely due to channel
FT stabilization in the lower current amplitude open state;
FT voltage-dependent activation and inactivation as well as
FT ion selectivity are unchanged; dbSNP:rs184841813)"
FT /evidence="ECO:0000269|PubMed:25296916"
FT /id="VAR_073432"
FT VARIANT 1436
FT /note="E -> K (in dbSNP:rs1322525317)"
FT /id="VAR_048742"
FT VARIANT 1500
FT /note="E -> K (in dbSNP:rs12377346)"
FT /id="VAR_048743"
FT TURN 84..92
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 95..114
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 134..150
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:7VFU"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 165..179
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:7MIY"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 223..245
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:7VFU"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 300..311
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 316..326
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 333..343
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 345..363
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 366..405
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 463..479
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 482..500
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 508..536
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 538..541
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 545..566
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 575..588
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 592..604
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 606..631
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 632..635
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 637..640
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 649..661
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 662..664
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 665..674
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 679..681
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 683..685
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 686..694
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 697..741
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 748..755
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 756..761
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 767..781
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1141..1147
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1152..1168
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1178..1205
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1207..1213
FT /evidence="ECO:0007829|PDB:7VFU"
FT HELIX 1218..1235
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1238..1240
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 1245..1252
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1253..1260
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1261..1264
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1266..1281
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1283..1304
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1309..1313
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 1319..1321
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1324..1328
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1330..1333
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1335..1338
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1341..1343
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1351..1363
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 1364..1366
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1367..1375
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 1386..1389
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1390..1392
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1393..1402
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 1403..1405
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1406..1417
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1435..1443
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1457..1459
FT /evidence="ECO:0007829|PDB:7VFU"
FT HELIX 1460..1469
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1471..1489
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1499..1524
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1527..1531
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1533..1535
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1536..1555
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1556..1558
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1559..1561
FT /evidence="ECO:0007829|PDB:7MIY"
FT HELIX 1562..1564
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1566..1568
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1569..1573
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1574..1576
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1577..1581
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1583..1597
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1602..1621
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1630..1636
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1638..1640
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1641..1652
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1657..1663
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1665..1670
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1672..1675
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 1677..1679
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1683..1709
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1711..1714
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1718..1720
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1723..1731
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 1734..1736
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 1748..1754
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 1758..1761
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 1763..1765
FT /evidence="ECO:0007829|PDB:7MIY"
FT HELIX 1767..1775
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 1776..1778
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 1781..1783
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 1793..1802
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1807..1810
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 1813..1827
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1834..1836
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 1837..1844
FT /evidence="ECO:0007829|PDB:7VFS"
FT CONFLICT Q00975-2:2215
FT /note="L -> R (in Ref. 1; AAA51898)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2339 AA; 262496 MW; 17A45C6D1E76B39D CRC64;
MVRFGDELGG RYGGPGGGER ARGGGAGGAG GPGPGGLQPG QRVLYKQSIA QRARTMALYN
PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD
GDKTPMSERL DDTEPYFIGI FCFEAGIKII ALGFVFHKGS YLRNGWNVMD FVVVLTGILA
TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII
GLEFYMGKFH KACFPNSTDA EPVGDFPCGK EAPARLCEGD TECREYWPGP NFGITNFDNI
LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA
KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDRNAEEK SPLDVLKRAA
TKKSRNDLIH AEEGEDRFAD LCAVGSPFAR ASLKSGKTES SSYFRRKEKM FRFFIRRMVK
AQSFYWVVLC VVALNTLCVA MVHYNQPRRL TTTLYFAEFV FLGLFLTEMS LKMYGLGPRS
YFRSSFNCFD FGVIVGSVFE VVWAAIKPGS SFGISVLRAL RLLRIFKVTK YWSSLRNLVV
SLLNSMKSII SLLFLLFLFI VVFALLGMQL FGGQFNFQDE TPTTNFDTFP AAILTVFQIL
TGEDWNAVMY HGIESQGGVS KGMFSSFYFI VLTLFGNYTL LNVFLAIAVD NLANAQELTK
DEEEMEEAAN QKLALQKAKE VAEVSPMSAA NISIAARQQN SAKARSVWEQ RASQLRLQNL
RASCEALYSE MDPEERLRFA TTRHLRPDMK THLDRPLVVE LGRDGARGPV GGKARPEAAE
APEGVDPPRR HHRHRDKDKT PAAGDQDRAE APKAESGEPG AREERPRPHR SHSKEAAGPP
EARSERGRGP GPEGGRRHHR RGSPEEAAER EPRRHRAHRH QDPSKECAGA KGERRARHRG
GPRAGPREAE SGEEPARRHR ARHKAQPAHE AVEKETTEKE ATEKEAEIVE ADKEKELRNH
QPREPHCDLE TSGTVTVGPM HTLPSTCLQK VEEQPEDADN QRNVTRMGSQ PPDPNTIVHI
PVMLTGPLGE ATVVPSGNVD LESQAEGKKE VEADDVMRSG PRPIVPYSSM FCLSPTNLLR
RFCHYIVTMR YFEVVILVVI ALSSIALAAE DPVRTDSPRN NALKYLDYIF TGVFTFEMVI
KMIDLGLLLH PGAYFRDLWN ILDFIVVSGA LVAFAFSGSK GKDINTIKSL RVLRVLRPLK
TIKRLPKLKA VFDCVVNSLK NVLNILIVYM LFMFIFAVIA VQLFKGKFFY CTDESKELER
DCRGQYLDYE KEEVEAQPRQ WKKYDFHYDN VLWALLTLFT VSTGEGWPMV LKHSVDATYE
EQGPSPGYRM ELSIFYVVYF VVFPFFFVNI FVALIIITFQ EQGDKVMSEC SLEKNERACI
DFAISAKPLT RYMPQNRQSF QYKTWTFVVS PPFEYFIMAM IALNTVVLMM KFYDAPYEYE
LMLKCLNIVF TSMFSMECVL KIIAFGVLNY FRDAWNVFDF VTVLGSITDI LVTEIAETNN
FINLSFLRLF RAARLIKLLR QGYTIRILLW TFVQSFKALP YVCLLIAMLF FIYAIIGMQV
FGNIALDDDT SINRHNNFRT FLQALMLLFR SATGEAWHEI MLSCLSNQAC DEQANATECG
SDFAYFYFVS FIFLCSFLML NLFVAVIMDN FEYLTRDSSI LGPHHLDEFI RVWAEYDPAA
CGRISYNDMF EMLKHMSPPL GLGKKCPARV AYKRLVRMNM PISNEDMTVH FTSTLMALIR
TALEIKLAPA GTKQHQCDAE LRKEISVVWA NLPQKTLDLL VPPHKPDEMT VGKVYAALMI
FDFYKQNKTT RDQMQQAPGG LSQMGPVSLF HPLKATLEQT QPAVLRGARV FLRQKSSTSL
SNGGAIQNQE SGIKESVSWG TQRTQDAPHE ARPPLERGHS TEIPVGRSGA LAVDVQMQSI
TRRGPDGEPQ PGLESQGRAA SMPRLAAETQ PVTDASPMKR SISTLAQRPR GTHLCSTTPD
RPPPSQASSH HHHHRCHRRR DRKQRSLEKG PSLSADMDGA PSSAVGPGLP PGEGPTGCRR
ERERRQERGR SQERRQPSSS SSEKQRFYSC DRFGGREPPK PKPSLSSHPT SPTAGQEPGP
HPQGSGSVNG SPLLSTSGAS TPGRGGRRQL PQTPLTPRPS ITYKTANSSP IHFAGAQTSL
PAFSPGRLSR GLSEHNALLQ RDPLSQPLAP GSRIGSDPYL GQRLDSEASV HALPEDTLTF
EEAVATNSGR SSRTSYVSSL TSQSHPLRRV PNGYHCTLGL SSGGRARHSY HHPDQDHWC
