ID   CAC1A_MOUSE             Reviewed;        2368 AA.
AC   P97445; Q2TPN3;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   27-MAR-2024, entry version 206.
DE   RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha-1A;
DE   AltName: Full=Brain calcium channel I;
DE            Short=BI;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 4;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.1;
GN   Name=Cacna1a {ECO:0000312|MGI:MGI:109482};
GN   Synonyms=Caca1a, Cach4, Cacn3, Cacnl1a4, Ccha1a;
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=Swiss Webster; TISSUE=Brain;
RA   Richards K.S., Swensen A.M., Lipscombe D.;
RT   "Molecular identity of P-type calcium current in Purkinje neurons.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 49-2212, AND VARIANT TG LEU-649.
RC   STRAIN=DBA/2J;
RX   PubMed=8929530; DOI=10.1016/s0092-8674(00)81381-1;
RA   Fletcher C.F., Lutz C.M., O'Sullivan T.N., Shaughnessy J.D. Jr., Hawkes R.,
RA   Frankel W.N., Copeland N.G., Jenkins N.A.;
RT   "Absence epilepsy in tottering mutant mice is associated with calcium
RT   channel defects.";
RL   Cell 87:607-617(1996).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-792, 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   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-450; SER-453;
RP   SER-752; SER-755; SER-1038; SER-1042; SER-1051; THR-1935; SER-2016 AND
RP   SER-2071, AND 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).
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC       of calcium ions into excitable cells and are also involved in a variety
CC       of calcium-dependent processes, including muscle contraction, hormone
CC       or neurotransmitter release, gene expression, cell motility, cell
CC       division and cell death. The isoform alpha-1A gives rise to P and/or Q-
CC       type calcium currents. P/Q-type calcium channels belong to the 'high-
CC       voltage activated' (HVA) group and are specifically blocked by the
CC       spider omega-agatoxin-IVA (AC P54282) (By similarity). They are however
CC       insensitive to dihydropyridines (DHP). {ECO:0000250|UniProtKB:O00555,
CC       ECO:0000250|UniProtKB:P54282}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671,
CC         ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:O00555};
CC   -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit complexes,
CC       consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1
CC       ratio. The channel activity is directed by the pore-forming and
CC       voltage-sensitive alpha-1 subunit. In many cases, this subunit is
CC       sufficient to generate voltage-sensitive calcium channel activity. The
CC       auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge
CC       regulate the channel activity. Interacts with CABP1 (By
CC       similarity).Interacts with the spider omega-agatoxin-IVA (AC P30288)
CC       (By similarity). Interacts with TSPOAP1 (By similarity).
CC       {ECO:0000250|UniProtKB:O00555, ECO:0000250|UniProtKB:P54282}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O00555};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Brain specific; mainly found in the cerebellum,
CC       olfactory bulb, cerebral cortex, hippocampus, and inferior colliculus.
CC       In the hippocampus, expression occurs in pyramidal and granule neurons,
CC       as well as in interneurons. Purkinje cells contain predominantly P-type
CC       VSCC, the Q-type being a prominent calcium current in cerebellar
CC       granule cells.
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   -!- DISEASE: Note=Defects in Cacna1a are the cause of a delayed-onset,
CC       recessive neurological disorder seen in tottering (tg) mutants,
CC       resulting in ataxia, motor seizures and behavioral absence seizures
CC       resembling petit mal epilepsy (or absence epilepsy) in humans. There
CC       are two more alleles, leaner (tg(lA)), that is characterized by severe
CC       ataxia and frequent death past weaning, but no motor seizures; and
CC       rolling Nagoya (tg(rol)), that presents an intermediary phenotype, the
CC       ataxia being somewhat more severe that with tg, but without motors
CC       seizures. Selective degeneration of cerebellar Purkinje cells has been
CC       shown for all these types of mutants. Selective degeneration of
CC       cerebellar Purkinje cells has been shown for all these types of
CC       mutants. {ECO:0000269|PubMed:8929530}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. CACNA1A subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY714490; AAW56205.1; -; mRNA.
DR   EMBL; U76716; AAC52940.1; -; mRNA.
DR   CCDS; CCDS52618.1; -.
DR   RefSeq; NP_031604.3; NM_007578.3.
DR   AlphaFoldDB; P97445; -.
DR   SMR; P97445; -.
DR   BioGRID; 198430; 25.
DR   IntAct; P97445; 3.
DR   MINT; P97445; -.
DR   STRING; 10090.ENSMUSP00000112436; -.
DR   GlyCosmos; P97445; 2 sites, No reported glycans.
DR   GlyGen; P97445; 5 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P97445; -.
DR   PhosphoSitePlus; P97445; -.
DR   SwissPalm; P97445; -.
DR   EPD; P97445; -.
DR   MaxQB; P97445; -.
DR   PaxDb; 10090-ENSMUSP00000112436; -.
DR   PeptideAtlas; P97445; -.
DR   ProteomicsDB; 273878; -.
DR   Pumba; P97445; -.
DR   Antibodypedia; 26386; 114 antibodies from 22 providers.
DR   DNASU; 12286; -.
DR   Ensembl; ENSMUST00000121390.8; ENSMUSP00000112436.2; ENSMUSG00000034656.19.
DR   GeneID; 12286; -.
DR   KEGG; mmu:12286; -.
DR   UCSC; uc009mmn.2; mouse.
DR   AGR; MGI:109482; -.
DR   CTD; 773; -.
DR   MGI; MGI:109482; Cacna1a.
DR   VEuPathDB; HostDB:ENSMUSG00000034656; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   GeneTree; ENSGT00940000156518; -.
DR   HOGENOM; CLU_000540_1_0_1; -.
DR   InParanoid; P97445; -.
DR   OMA; KRMCQHR; -.
DR   OrthoDB; 1110761at2759; -.
DR   PhylomeDB; P97445; -.
DR   TreeFam; TF312805; -.
DR   Reactome; R-MMU-112308; Presynaptic depolarization and calcium channel opening.
DR   Reactome; R-MMU-422356; Regulation of insulin secretion.
DR   BioGRID-ORCS; 12286; 3 hits in 78 CRISPR screens.
DR   ChiTaRS; Cacna1a; mouse.
DR   PRO; PR:P97445; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; P97445; Protein.
DR   Bgee; ENSMUSG00000034656; Expressed in cerebellar cortex and 169 other cell types or tissues.
DR   ExpressionAtlas; P97445; baseline and differential.
DR   GO; GO:0042995; C:cell projection; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0043204; C:perikaryon; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0048787; C:presynaptic active zone membrane; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR   GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IMP:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:MGI.
DR   GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; IDA:SynGO.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0048266; P:behavioral response to pain; IMP: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; ISS:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IMP:MGI.
DR   GO; GO:0017156; P:calcium-ion regulated exocytosis; IMP:MGI.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI.
DR   GO; GO:0021953; P:central nervous system neuron differentiation; IMP:MGI.
DR   GO; GO:0021679; P:cerebellar molecular layer development; IMP:MGI.
DR   GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
DR   GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:MGI.
DR   GO; GO:0021590; P:cerebellum maturation; IMP:MGI.
DR   GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR   GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR   GO; GO:0014051; P:gamma-aminobutyric acid secretion; IMP:MGI.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0042446; P:hormone biosynthetic process; IMP:MGI.
DR   GO; GO:0030644; P:intracellular chloride ion homeostasis; IMP:MGI.
DR   GO; GO:0051899; P:membrane depolarization; IMP:MGI.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR   GO; GO:0050883; P:musculoskeletal movement, spinal reflex action; IMP:MGI.
DR   GO; GO:0032353; P:negative regulation of hormone biosynthetic process; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR   GO; GO:0050877; P:nervous system process; IMP:MGI.
DR   GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR   GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR   GO; GO:0070050; P:neuron cellular homeostasis; IMP:MGI.
DR   GO; GO:0007270; P:neuron-neuron synaptic transmission; IMP:MGI.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:MGI.
DR   GO; GO:0043113; P:receptor clustering; IMP:MGI.
DR   GO; GO:0014056; P:regulation of acetylcholine secretion, neurotransmission; IMP:MGI.
DR   GO; GO:0050770; P:regulation of axonogenesis; IMP:MGI.
DR   GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IDA:MGI.
DR   GO; GO:0010817; P:regulation of hormone levels; IMP:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR   GO; GO:0031335; P:regulation of sulfur amino acid metabolic process; IMP:MGI.
DR   GO; GO:1904645; P:response to amyloid-beta; ISO:MGI.
DR   GO; GO:0048265; P:response to pain; IMP:MGI.
DR   GO; GO:0060024; P:rhythmic synaptic transmission; IMP:MGI.
DR   GO; GO:0021522; P:spinal cord motor neuron differentiation; IMP:MGI.
DR   GO; GO:0007416; P:synapse assembly; IMP:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
DR   GO; GO:0021750; P:vestibular nucleus development; IMP: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; IPR005448; CACNA1A.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
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:SF3; VOLTAGE-DEPENDENT P_Q-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1A; 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; PR01632; PQVDCCALPHA1.
DR   SMART; SM01062; Ca_chan_IQ; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR   Genevisible; P97445; MM.
PE   1: Evidence at protein level;
KW   Calcium; Calcium channel; Calcium transport; Cell membrane;
KW   Disease variant; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..2368
FT                   /note="Voltage-dependent P/Q-type calcium channel subunit
FT                   alpha-1A"
FT                   /id="PRO_0000053917"
FT   TOPO_DOM        1..100
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..119
FT                   /note="Helical; Name=S1 of repeat I"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..138
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..156
FT                   /note="Helical; Name=S2 of repeat I"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..168
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..184
FT                   /note="Helical; Name=S3 of repeat I"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..192
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..211
FT                   /note="Helical; Name=S4 of repeat I"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        212..230
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..250
FT                   /note="Helical; Name=S5 of repeat I"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..337
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..362
FT                   /note="Helical; Name=S6 of repeat I"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..489
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        490..509
FT                   /note="Helical; Name=S1 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        510..523
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        524..543
FT                   /note="Helical; Name=S2 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        544..551
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        552..570
FT                   /note="Helical; Name=S3 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        571..580
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        581..599
FT                   /note="Helical; Name=S4 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        600..618
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        619..638
FT                   /note="Helical; Name=S5 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        639..691
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        692..716
FT                   /note="Helical; Name=S6 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        717..1190
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1191..1214
FT                   /note="Helical; Name=S1 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1215..1231
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1232..1251
FT                   /note="Helical; Name=S2 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1252..1258
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1259..1282
FT                   /note="Helical; Name=S3 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1283..1293
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1294..1311
FT                   /note="Helical; Name=S4 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1312..1330
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1331..1350
FT                   /note="Helical; Name=S5 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1351..1437
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1438..1462
FT                   /note="Helical; Name=S6 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1463..1518
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1519..1537
FT                   /note="Helical; Name=S1 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1538..1551
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1552..1573
FT                   /note="Helical; Name=S2 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1574..1580
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1581..1600
FT                   /note="Helical; Name=S3 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1601..1607
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1608..1626
FT                   /note="Helical; Name=S4 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1627..1645
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1646..1665
FT                   /note="Helical; Name=S5 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1666..1737
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1738..1763
FT                   /note="Helical; Name=S6 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1764..2368
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          65..365
FT                   /note="I"
FT   REPEAT          475..719
FT                   /note="II"
FT   REPEAT          1182..1465
FT                   /note="III"
FT   REPEAT          1502..1765
FT                   /note="IV"
FT   REGION          385..402
FT                   /note="Binding to the beta subunit"
FT                   /evidence="ECO:0000250|UniProtKB:P27884"
FT   REGION          762..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          823..1117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1137..1170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1940..2368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        828..842
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..864
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..991
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        994..1011
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1052..1081
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1092..1112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1144..1164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1947..1962
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1981..1995
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2007..2021
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2086..2105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2156..2173
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2174..2210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2211..2245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2351..2368
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         320
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   BINDING         670
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   BINDING         1411
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P07293"
FT   SITE            1600
FT                   /note="Binds to omega-Aga-IVA"
FT                   /evidence="ECO:0000250|UniProtKB:P27884"
FT   MOD_RES         411
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         450
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         453
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         752
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         755
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         792
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087"
FT   MOD_RES         1038
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1042
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1051
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1935
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1998
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P54282"
FT   MOD_RES         2016
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2028
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P54282"
FT   MOD_RES         2030
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P54282"
FT   MOD_RES         2071
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2091
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P54282"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1607
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         649
FT                   /note="P -> L (in tg)"
FT                   /evidence="ECO:0000269|PubMed:8929530"
FT   CONFLICT        79
FT                   /note="S -> P (in Ref. 2; AAC52940)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82
FT                   /note="L -> F (in Ref. 2; AAC52940)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        884
FT                   /note="P -> L (in Ref. 2; AAC52940)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        888
FT                   /note="E -> D (in Ref. 1; AAW56205)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1083
FT                   /note="N -> D (in Ref. 2; AAC52940)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1349
FT                   /note="L -> F (in Ref. 2; AAC52940)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1373
FT                   /note="L -> F (in Ref. 2; AAC52940)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2161
FT                   /note="P -> PH (in Ref. 1; AAW56205)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2368 AA;  267647 MW;  E7B573BA005E5CB1 CRC64;
     MARFGDEMPG RYGAGGGGSG PAAGVVVGAA GGRGAGGSRQ GGQPGAQRMY KQSMAQRART
     MALYNPIPVR QNCLTVNRSL FLFSEDNVVR KYAKKITEWP PFEYMILATI IANCIVLALE
     QHLPDDDKTP MSERLDDTEP YFIGIFCFEA GIKIVALGFA FHKGSYLRNG WNVMDFVVVL
     TGILATVGTE FDLRTLRAVR VLRPLKLVSG IPSLQVVLKS IMKAMIPLLQ IGLLLFFAIL
     IFAIIGLEFY MGKFHTTCFE EGTDDIQGES PAPCGTEEPA RTCPNGTKCQ PYWEGPNNGI
     TQFDNILFAV LTVFQCITME GWTDLLYNSN DASGNTWNWL YFIPLIIIGS FFMLNLVLGV
     LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYMEWISK AEEVILAEDE TDVEQRHPFD
     GALRRATLKK SKTDLLNPEE AEDQLADIAS VGSPFARASI KSAKLENSTF FHKKERRMRF
     YIRRMVKTQA FYWTVLSLVA LNTLCVAIVH YNQPEWLSDF LYYAEFIFLG LFMSEMFIKM
     YGLGTRPYFH SSFNCFDCGV IIGSIFEVIW AVIKPGTSFG ISVLRALRLL RIFKVTKYWA
     SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFDEGTPP TNFDTFPAAI
     MTVFQILTGE DWNEVMYDGI KSQGGVQGGM VFSIYFIVLT LFGNYTLLNV FLAIAVDNLA
     NAQELTKDEQ EEEEAANQKL ALQKAKEVAE VSPLSAANMS IAVKEQQKNQ KPTKSVWEQR
     TSEMRKQNLL ASREALYGDA AERWPTPYAR PLRPDVKTHL DRPLVVDPQE NRNNNTNKSR
     APEALRPTAR PRESARDPDA RRAWPGSPER APGREGPYGR ESEPQQREHA PPREHAPWDA
     DTERAKAGDA PRRHTHRPVA EGEPRRHRAR RRPGDEPDDR PERRPRPRDA TRPARAADGE
     GDDGERKRRH RHGPPAHDDR ERRHRRRKEN QGSGVPVSGP NLSTTRPIQQ DLGRQDLPLA
     EDLDNMKNNK LATGEPASPH DSLGHSGLPP SPAKIGNSTN PGPALATNPQ NAASRRTPNN
     PGNPSNPGPP KTPENSLIVT NPSSTQPNSA KTARKPEHMA VEIPPACPPL NHTVVQVNKN
     ANPDPLPKKE EEKKEEEEAD PGEDGPKPMP PYSSMFILST TNPLRRLCHY ILNLRYFEMC
     ILMVIAMSSI ALAAEDPVQP NAPRNNVLRY FDYVFTGVFT FEMVIKMIDL GLVLHQGAYF
     RDLWNILDFI VVSGALVAFA FTGNSKGKDI NTIKSLRVLR VLRPLKTIKR LPKLKAVFDC
     VVNSLKNVFN ILIVYMLFMF IFAVVAVQLF KGKFFHCTDE SKEFERDCRG KYLLYEKNEV
     KARDREWKKY EFHYDNVLWA LLTLFTVSTG EGWPQVLKHS VDATFENQGP SPGYRMEMSI
     FYVVYFVVFP FFFVNIFVAL IIITFQEQGD KMMEEYSLEK NERACIDFAI SAKPLTRHMP
     QNKQSFQYRM WQFVVSPPFE YTIMAMIALN TIVLMMKFYG ASVAYENALR VFNIVFTSLF
     SLECVLKVMA FGILNYFRDA WNIFDFVTVL GSITDILVTE FGNNFINLSF LRLFRAARLI
     KLLRQGYTIR ILLWTFVQSF KALPYVCLLI AMLFFIYAII GMQVFGNIGI DGEDEDSDED
     EFQITEHNNF RTFFQALMLL FRSATGEAWH NIMLSCLSGK PCDKNSGILT ADCGNEFAYF
     YFVSFIFLCS FLMLNLFVAV IMDNFEYLTR DSSILGPHHL DEYVRVWAEY DPAACGRIHY
     KDMYSLLRVI SPPLGLGKKC PHRVACKRLL RMDLPVADDN TVHFNSTLMA LIRTALDIKI
     AKGGADKQQM DAELRKEMMA IWPNLSQKTL DLLVTPHKST DLTVGKIYAA MMIMEYYRQS
     KAKKLQAMRE EQNRTPLMFQ RMEPPSPTQE GGPSQNALPS TQLDPGGGLM AHEGGMKESP
     SWVTQRAQEM FQKTGTWSPE RGPPIDMPNS QPNSQSVEMR EMGTDGYSDS EHYLPMEGQT
     RAASMPRLPA ENQRRRGRPR GNDLSTISDT SPMKRSASVL GPKARRLDDY SLERVPPEEN
     QRYHQRRRDR GHRTSERSLG RYTDVDTGLG TDLSMTTQSG DLPSKDRDQD RGRPKDRKHR
     PHHHHHHHHH HPPAPDRDRY AQERPDTGRA RAREQRWSRS PSEGREHTTH RQGSSSVSGS
     PAPSTSGTST PRRGRRQLPQ TPCTPRPLVS YSPAPRRPAA RRMAGPAAPP GGSPRGCRRA
     PRWPAHAPEG PRPRGADYTE PDSPREPPGG AHDPAPRSPR TPRAAGCASP RHGRRLPNGY
     YAGHGAPRPR TARRGAHDAY SESEDDWC
//