NALCN_RAT
ID NALCN_RAT Reviewed; 1738 AA.
AC Q6Q760; Q9Z165;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Sodium leak channel NALCN {ECO:0000305};
DE AltName: Full=Four domain-type voltage-gated ion channel alpha-1 subunit;
DE AltName: Full=Rb21-channel {ECO:0000303|PubMed:10094463};
DE AltName: Full=Sodium leak channel non-selective protein;
DE AltName: Full=Voltage gated channel-like protein 1;
GN Name=Nalcn; Synonyms=Nca, Rb21 {ECO:0000303|PubMed:10094463}, Vgcnl1;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10094463; DOI=10.1016/s0014-5793(99)00082-4;
RA Lee J.-H., Cribbs L.L., Perez-Reyes E.;
RT "Cloning of a novel four repeat protein related to voltage-gated sodium and
RT calcium channels.";
RL FEBS Lett. 445:231-236(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Hamming K.S., Snutch T.P.;
RT "Member of a novel family of four domain-type voltage-gated ion channel in
RT Rattus norvegicus.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=17448995; DOI=10.1016/j.cell.2007.02.041;
RA Lu B., Su Y., Das S., Liu J., Xia J., Ren D.;
RT "The neuronal channel NALCN contributes resting sodium permeability and is
RT required for normal respiratory rhythm.";
RL Cell 129:371-383(2007).
RN [4]
RP 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 [5] {ECO:0007744|PDB:7CU3}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.65 ANGSTROMS) IN COMPLEX WITH MOUSE
RP NALF1, DISULFIDE BOND, GLYCOSYLATION AT ASN-210; ASN-216 AND ASN-1064, AND
RP MUTAGENESIS OF GLU-1389 AND ASP-1390.
RX PubMed=33273469; DOI=10.1038/s41467-020-20002-9;
RA Kang Y., Wu J.X., Chen L.;
RT "Structure of voltage-modulated sodium-selective NALCN-FAM155A channel
RT complex.";
RL Nat. Commun. 11:6199-6199(2020).
CC -!- FUNCTION: Voltage-gated ion channel responsible for the resting Na(+)
CC permeability that controls neuronal excitability. NALCN channel
CC functions as a multi-protein complex, which consists at least of NALCN,
CC NALF1, UNC79 and UNC80. NALCN is the voltage-sensing, pore-forming
CC subunit of the NALCN channel complex. NALCN channel complex is
CC constitutively active and conducts monovalent cations but is blocked by
CC physiological concentrations of extracellular divalent cations (By
CC similarity). In addition to its role in regulating neuronal
CC excitability, is required for normal respiratory rhythm, systemic
CC osmoregulation by controlling the serum sodium concentration and in the
CC regulation of the intestinal pace-making activity in the interstitial
CC cells of Cajal. NALCN channel is also activated by neuropeptides such
CC as neurotensin and substance P (SP) through a SRC family kinases-
CC dependent pathway. In addition, NALCN activity is enhanced/modulated by
CC several GPCRs, such as CHRM3 (By similarity).
CC {ECO:0000250|UniProtKB:Q8BXR5, ECO:0000250|UniProtKB:Q8IZF0}.
CC -!- ACTIVITY REGULATION: Inhibited by low micromolar concentrations of
CC Gd(3+) and high micromolar concentrations of verapamil. Insensitive to
CC tetrodotoxin (TTX) and potentiated by low external Ca(2+)
CC concentration. {ECO:0000250|UniProtKB:Q8IZF0}.
CC -!- SUBUNIT: Found in a complex with NALCN, UNC79, UNC80 and NACL1; these
CC auxiliary subunits are indispensable for the function of NALCN channel
CC (By similarity). Interacts with UNC80; required for the NALCN
CC activation/inhibition by GPCRs in neurons. Found in a complex with
CC NALCN, UNC79 and UNC80; UNC80 bridges NALCN to UNC79. Interacts with
CC CHRM3 (By similarity). {ECO:0000250|UniProtKB:Q8BXR5,
CC ECO:0000250|UniProtKB:Q8IZF0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IZF0};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain, moderately in
CC the heart and weakly in the pancreas. {ECO:0000269|PubMed:10094463}.
CC -!- DOMAIN: Contains 24 transmembrane helices (TM) that form four
CC homologous functional repeats connected by intracellular linkers. Each
CC of the four internal repeats contains five hydrophobic transmembrane
CC segments (S1, S2, S3, S5, S6) and one positively charged transmembrane
CC segment (S4). S4 segments represent the voltage-sensor. S4
CC transmembrane segments lack some of the charged residues (K and R)
CC found at every third position in the S4s of the NaV, CaV, and KV
CC channels. Pore-forming loops (P loops) between S5 and S6 of each domain
CC form an EEKE sodium- ion selectivity filter a mixture between the EEEE
CC found in the CaVs and the DEKA of NaVs. Voltage-sensing domains (VSDs),
CC formed by S1 to S4 of each domain, detect changes in membrane potential
CC and induce the opening or closing of the ion-conducting pore domain,
CC formed by S5 and S6. {ECO:0000250|UniProtKB:Q8BXR5}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000250|UniProtKB:Q8BXR5}.
CC -!- SIMILARITY: Belongs to the NALCN family. {ECO:0000305}.
CC -!- CAUTION: NALCN was also originally reported to be a voltage-
CC independent, cation-nonselective channel which is permeable to sodium,
CC potassium and calcium ions (PubMed:17448995). However, NALCN is
CC recently reported to be selective only for monovalent cations and to be
CC blocked by extracellular divalent cations (By similarity). Futhemore,
CC coexpression of NALCN, UNC79, UNC80, and NALF1 results in voltage-
CC dependent NALCN currents (By similarity).
CC {ECO:0000250|UniProtKB:Q8IZF0, ECO:0000269|PubMed:17448995}.
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DR EMBL; AF078779; AAC68885.1; -; mRNA.
DR EMBL; AY555273; AAS65873.1; -; mRNA.
DR PIR; T17101; T17101.
DR RefSeq; NP_705894.1; NM_153630.1.
DR PDB; 7CU3; EM; 2.65 A; A=1-1738.
DR PDBsum; 7CU3; -.
DR AlphaFoldDB; Q6Q760; -.
DR SMR; Q6Q760; -.
DR STRING; 10116.ENSRNOP00000054214; -.
DR iPTMnet; Q6Q760; -.
DR PhosphoSitePlus; Q6Q760; -.
DR PaxDb; Q6Q760; -.
DR PRIDE; Q6Q760; -.
DR ABCD; Q6Q760; 1 sequenced antibody.
DR GeneID; 266760; -.
DR KEGG; rno:266760; -.
DR CTD; 259232; -.
DR RGD; 628710; Nalcn.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; Q6Q760; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; Q6Q760; -.
DR PRO; PR:Q6Q760; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005261; F:cation channel activity; ISS:UniProtKB.
DR GO; GO:0022840; F:leak channel activity; ISS:UniProtKB.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; ISS:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IBA:GO_Central.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0060075; P:regulation of resting membrane potential; ISS:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISS:UniProtKB.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR028823; NALCN.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR46141; PTHR46141; 1.
DR Pfam; PF00520; Ion_trans; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Coiled coil; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1738
FT /note="Sodium leak channel NALCN"
FT /id="PRO_0000314012"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 37..57
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 58..65
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 66..90
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 91..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 107..129
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 130..137
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 138..158
FT /note="Helical; Voltage-sensor; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 159..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 174..199
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 200..269
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT INTRAMEM 270..289
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 290..294
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 295..322
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 323..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 383..403
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 404..416
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 417..439
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 440..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 448..468
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 469..472
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 473..492
FT /note="Helical; Voltage-sensor; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 493..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 503..530
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 531..543
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT INTRAMEM 544..563
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 564..569
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 570..599
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 600..886
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 887..906
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 907..915
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 916..939
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 940..947
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 948..972
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 973..980
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 981..1003
FT /note="Helical; Voltage-sensor; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 1004..1015
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 1016..1039
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 1040..1104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 1105..1124
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 1125..1129
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 1130..1159
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 1160..1210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 1211..1227
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 1228..1236
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 1237..1260
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 1261..1271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 1272..1293
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 1294..1296
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 1297..1318
FT /note="Helical; Voltage-sensor; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 1319..1331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 1332..1357
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 1358..1378
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT INTRAMEM 1379..1398
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 1399..1420
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TRANSMEM 1421..1447
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT TOPO_DOM 1448..1738
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8IZF0"
FT REGION 762..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1611..1679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 795..830
FT /evidence="ECO:0000255"
FT COMPBIAS 772..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1611..1653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:33273469,
FT ECO:0007744|PDB:7CU3"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:33273469,
FT ECO:0007744|PDB:7CU3"
FT CARBOHYD 1064
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:33273469,
FT ECO:0007744|PDB:7CU3"
FT DISULFID 207..239
FT /evidence="ECO:0000269|PubMed:33273469,
FT ECO:0007744|PDB:7CU3"
FT DISULFID 229..245
FT /evidence="ECO:0000269|PubMed:33273469,
FT ECO:0007744|PDB:7CU3"
FT DISULFID 1046..1057
FT /evidence="ECO:0000269|PubMed:33273469,
FT ECO:0007744|PDB:7CU3"
FT DISULFID 1405..1417
FT /evidence="ECO:0000269|PubMed:33273469,
FT ECO:0007744|PDB:7CU3"
FT MUTAGEN 1389
FT /note="E->A: Affects ion seletivity."
FT /evidence="ECO:0000269|PubMed:33273469"
FT MUTAGEN 1390
FT /note="D->A: Affects ion seletivity."
FT /evidence="ECO:0000269|PubMed:33273469"
FT CONFLICT 52
FT /note="P -> S (in Ref. 1; AAC68885)"
FT /evidence="ECO:0000305"
FT CONFLICT 748
FT /note="T -> A (in Ref. 1; AAC68885)"
FT /evidence="ECO:0000305"
FT CONFLICT 1480..1485
FT /note="KREGVI -> NERCD (in Ref. 1; AAC68885)"
FT /evidence="ECO:0000305"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 36..54
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 65..90
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 108..129
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 164..199
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:7CU3"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 266..277
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 282..292
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 295..308
FT /evidence="ECO:0007829|PDB:7CU3"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 312..335
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 377..382
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 384..402
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 417..440
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 442..446
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 451..465
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 475..480
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 481..488
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 490..500
FT /evidence="ECO:0007829|PDB:7CU3"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 506..528
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 540..552
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 556..567
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 572..602
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 606..614
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 753..763
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 847..853
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 876..882
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 887..903
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 908..910
FT /evidence="ECO:0007829|PDB:7CU3"
FT TURN 912..914
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 916..940
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 942..945
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 949..952
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 953..971
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 981..989
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 990..995
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 996..999
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1001..1011
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1014..1039
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 1045..1048
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 1059..1065
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 1082..1087
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1101..1112
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1117..1127
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1130..1132
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1133..1143
FT /evidence="ECO:0007829|PDB:7CU3"
FT TURN 1144..1146
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1147..1162
FT /evidence="ECO:0007829|PDB:7CU3"
FT TURN 1163..1166
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1170..1182
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1198..1207
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1210..1225
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1238..1262
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1265..1268
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1272..1293
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1297..1313
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1314..1317
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1319..1334
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1336..1357
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 1367..1370
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1375..1386
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1391..1397
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1412..1414
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1420..1436
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1439..1453
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 1459..1461
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1464..1477
FT /evidence="ECO:0007829|PDB:7CU3"
FT STRAND 1478..1480
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1488..1496
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1499..1501
FT /evidence="ECO:0007829|PDB:7CU3"
FT TURN 1505..1507
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1509..1521
FT /evidence="ECO:0007829|PDB:7CU3"
FT TURN 1522..1524
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1532..1540
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1544..1547
FT /evidence="ECO:0007829|PDB:7CU3"
FT HELIX 1550..1577
FT /evidence="ECO:0007829|PDB:7CU3"
SQ SEQUENCE 1738 AA; 200491 MW; 9920B25C43193C75 CRC64;
MLKRKQSSRV EAQPVTDFGP DESLSDNADI LWINKPWVHS LLRICAIISV IPVCMNTPMT
FEHYPPLQYV TFTLDTLLMF LYTAEMIAKM HIRGIVKGDS SYVKDRWCVF DGFMVFCLWV
SLVLQVFEIA DIVDQMSPWG MLRIPRPLIM IRAFRIYFRF ELPRTRITNI LKRSGEQIWS
VSIFLLFFLL LYGILGVQMF GTFTYHCVVN DTKPGNVTWN SLAIPDTHCS PELEEGYQCP
PGFKCMDLED LGLSRQELGY SGFNEIGTSI FTVYEASSQE GWVFLMYRAI DSFPRWRSYF
YFITLIFFLA WLVKNVFIAV IIETFAEIRV QFQQMWGTRS STTSTATTQM FHEDAAGGWQ
LVAVDVNKPQ GRAPACLQKM MRSSVFHMFI LSMVTVDVIV AASNYYKGEN FRRQYDEFYL
AEVAFTVLFD LEALLKIWCL GFTGYISSSL HKFELLLVIG TTLHVYPDLY HSQFTYFQVL
RVVRLIKISP ALEDFVYKIF GPGKKLGSLV VFTASLLIVM SAISLQMFCF VEELDRFTTF
PRAFMSMFQI LTQEGWVDVM DQTLNAVGHM WAPLVAIYFI LYHLFATLIL LSLFVAVILD
NLELDEDLKK LKQLKQSEAN ADTKEKLPLR LRIFEKFPNR PQMVKISKLP SDFTVPKIRE
SFMKQFIDRQ QQDTCCLFRI LPSTSSSSCD NPKRPTVEDN KYIDQKLRKS VFSIRARNLL
EKETAVTKIL RACTRQRMLS GSFEGQPTKE RSILSVQHHI RQERRSLRHG SNSQRISRGK
SLETLTQDHS NTVRYRNAQR EDSEIKMIQE KKEQAEMKRK VQEEELRENH PYFDKPLFIV
GREHRFRNFC RVVVRARFNA SKTDPVTGAV KNTKYHQLYD LLGLVTYLDW VMITVTICSC
ISMMFESPFR RVMHAPTLQI AEYVFVIFMS IELNLKIMAD GLFFTPTAVI RDFGGVMDIF
IYLVSLIFLC WMPQNVPAES GAQLLMVLRC LRPLRIFKLV PQMRKVVREL FSGFKEIFLV
SILLLTLMLV FASFGVQLFA GKLAKCNDPN IIRREDCNGI FRINVSVSKN LNLKLRPGEK
KPGFWVPRVW ANPRNFNFDN VGNAMLALFE VLSLKGWVEV RDVIIHRVGP IHGIYIHVFV
FLGCMIGLTL FVGVVIANFN ENKGTALLTV DQRRWEDLKS RLKIAQPLHL PPRPDNDGFR
AKMYDITQHP FFKRTIALLV LAQSVLLSVK WDVEDPVTVP LATMSVVFTF IFVLEVTMKI
IAMSPAGFWQ SRRNRYDLLV TSLGVVWVVL HFALLNAYTY MMGACVIVFR FFSICGKHVT
LKMLLLTVVV SMYKSFFIIV GMFLLLLCYA FAGVVLFGTV KYGENINRHA NFSSAGKAIT
VLFRIVTGED WNKIMHDCMV QPPFCTPDEF TYWATDCGNY AGALMYFCSF YVIIAYIMLN
LLVAIIVENF SLFYSTEEDQ LLSYNDLRHF QIIWNMVDDK REGVIPTFRV KFLLRLLRGR
LEVDLDKDKL LFKHMCYEME RLHNGGDVTF HDVLSMLSYR SVDIRKSLQL EELLAREQLE
YTIEEEVAKQ TIRMWLKKCL KRIRAKQQQS CSIIHSLRES QQQELSRFLN PPSIETTQPS
EDTNANSQDH NTQPESSSQQ QLLSPTLSDR GGSRQDAADT GKPQRKIGQW RLPSAPKPIS
HSVSSVNLRF GGRTTMKSVV CKMNPMPDTA SCGSEVKKWW TRQLTVESDE SGDDLLDI
