SCN2B_HUMAN
ID SCN2B_HUMAN Reviewed; 215 AA.
AC O60939; O75302; Q9UNN3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Sodium channel subunit beta-2;
DE Flags: Precursor;
GN Name=SCN2B; ORFNames=UNQ326/PRO386;
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].
RC TISSUE=Brain;
RX PubMed=9295116; DOI=10.1097/00001756-199708180-00025;
RA Eubanks J., Srinivasan J., Dinulos M.B., Disteche C.M., Catterall W.A.;
RT "Structure and chromosomal localization of the beta2 subunit of the human
RT brain sodium channel.";
RL NeuroReport 8:2775-2779(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=9887383; DOI=10.1038/sj.ejhg.5200220;
RA Bolino A., Seri M., Caroli F., Eubanks J., Srinivasan J., Mandich P.,
RA Schenone A., Quattrone A., Romeo G., Catterall W.A., Devoto M.;
RT "Exclusion of the SCN2B gene as candidate for CMT4B.";
RL Eur. J. Hum. Genet. 6:629-634(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Cruz J.S., Santana L.F., Frederick C.A., Isom L.L., Malhotra J.D.,
RA Mattei L.N., Kass R.S., Xia J., An R.-H., Lederer W.J.;
RT "Whether 'slip-mode conductance' occurs.";
RL Science 284:711-711(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Isom L.L., Mattei L.N., Ragsdale D.S.;
RT "Primary structure and functional expression of a beta 2 subunit of human
RT infant brain sodium channels.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=22992729; DOI=10.1074/jbc.m112.397646;
RA Chen C., Calhoun J.D., Zhang Y., Lopez-Santiago L., Zhou N., Davis T.H.,
RA Salzer J.L., Isom L.L.;
RT "Identification of the cysteine residue responsible for disulfide linkage
RT of Na+ channel alpha and beta2 subunits.";
RL J. Biol. Chem. 287:39061-39069(2012).
RN [8] {ECO:0000312|PDB:5FDY, ECO:0000312|PDB:5FEB}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 30-153, DISULFIDE BOND, AND
RP MUTAGENESIS OF CYS-55.
RX PubMed=26894959; DOI=10.7554/elife.10960;
RA Das S., Gilchrist J., Bosmans F., Van Petegem F.;
RT "Binary architecture of the Nav1.2-beta2 signaling complex.";
RL Elife 5:0-0(2016).
RN [9] {ECO:0000312|PDB:6J8G, ECO:0000312|PDB:6J8H, ECO:0000312|PDB:6J8I, ECO:0000312|PDB:6J8J}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.2 ANGSTROMS) IN COMPLEX WITH SCN9A;
RP SCN1B; PROTOTOXIN-II; TETRODOTOXIN; HUWENTOXIN-IV AND SAXITOXIN,
RP GLYCOSYLATION AT ASN-66, AND DISULFIDE BOND.
RX PubMed=30765606; DOI=10.1126/science.aaw2493;
RA Shen H., Liu D., Wu K., Lei J., Yan N.;
RT "Structures of human Nav1.7 channel in complex with auxiliary subunits and
RT animal toxins.";
RL Science 363:1303-1308(2019).
RN [10] {ECO:0000312|PDB:6J8E}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH SCN2A AND
RP MU-CONOTOXIN KIIIA, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=30765605; DOI=10.1126/science.aaw2999;
RA Pan X., Li Z., Huang X., Huang G., Gao S., Shen H., Liu L., Lei J., Yan N.;
RT "Molecular basis for pore blockade of human Na+ channel Nav1.2 by the mu-
RT conotoxin KIIIA.";
RL Science 363:1309-1313(2019).
RN [11]
RP VARIANTS ATFB14 GLN-28 AND TRP-28, AND CHARACTERIZATION OF VARIANTS ATFB14
RP GLN-28 AND TRP-28.
RX PubMed=19808477; DOI=10.1161/circep.108.779181;
RA Watanabe H., Darbar D., Kaiser D.W., Jiramongkolchai K., Chopra S.,
RA Donahue B.S., Kannankeril P.J., Roden D.M.;
RT "Mutations in sodium channel beta1- and beta2-subunits associated with
RT atrial fibrillation.";
RL Circ. Arrhythm. Electrophysiol. 2:268-275(2009).
RN [12]
RP VARIANT GLY-211, CHARACTERIZATION OF VARIANT GLY-211, AND POSSIBLE
RP INVOLVEMENT IN BRUGADA SYNDROME.
RX PubMed=23559163; DOI=10.1002/humu.22328;
RA Riuro H., Beltran-Alvarez P., Tarradas A., Selga E., Campuzano O.,
RA Verges M., Pagans S., Iglesias A., Brugada J., Brugada P., Vazquez F.M.,
RA Perez G.J., Scornik F.S., Brugada R.;
RT "A missense mutation in the sodium channel beta2 subunit reveals SCN2B as a
RT new candidate gene for Brugada syndrome.";
RL Hum. Mutat. 34:961-966(2013).
CC -!- FUNCTION: Crucial in the assembly, expression, and functional
CC modulation of the heterotrimeric complex of the sodium channel. The
CC subunit beta-2 causes an increase in the plasma membrane surface area
CC and in its folding into microvilli. Interacts with TNR may play a
CC crucial role in clustering and regulation of activity of sodium
CC channels at nodes of Ranvier (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The voltage-sensitive sodium channel consists of an ion
CC conducting pore forming alpha-subunit (SCN2A) regulated by one or more
CC beta subunits (SCN1B, SCN2B, SCN3B and SCN4B). SCN1B and SCN3B are non-
CC covalently associated with SCN2A. SCN2B and SCN4B are disulfide-linked
CC to SCN2A. {ECO:0000269|PubMed:30765605}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Brain specific.
CC -!- DISEASE: Atrial fibrillation, familial, 14 (ATFB14) [MIM:615378]: A
CC familial form of atrial fibrillation, a common sustained cardiac rhythm
CC disturbance. Atrial fibrillation is characterized by disorganized
CC atrial electrical activity and ineffective atrial contraction promoting
CC blood stasis in the atria and reduces ventricular filling. It can
CC result in palpitations, syncope, thromboembolic stroke, and congestive
CC heart failure. {ECO:0000269|PubMed:19808477}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Note=Genetic variations in SCN2B may be involved in Brugada
CC syndrome (PubMed:23559163). This tachyarrhythmia is characterized by
CC right bundle branch block and ST segment elevation on an
CC electrocardiogram (ECG). It can cause the ventricles to beat so fast
CC that the blood is prevented from circulating efficiently in the body.
CC When this situation occurs, the individual will faint and may die in a
CC few minutes if the heart is not reset. {ECO:0000269|PubMed:23559163}.
CC -!- SIMILARITY: Belongs to the sodium channel auxiliary subunit SCN2B (TC
CC 8.A.17) family. {ECO:0000305}.
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DR EMBL; AF007783; AAC26013.1; -; mRNA.
DR EMBL; AF049498; AAC05274.1; -; mRNA.
DR EMBL; AF049497; AAC05208.1; -; Genomic_DNA.
DR EMBL; AF049496; AAC05208.1; JOINED; Genomic_DNA.
DR EMBL; AF107028; AAD47196.1; -; mRNA.
DR EMBL; U87555; AAF21472.1; -; mRNA.
DR EMBL; AY358945; AAQ89304.1; -; mRNA.
DR EMBL; BC036793; AAH36793.1; -; mRNA.
DR CCDS; CCDS8390.1; -.
DR RefSeq; NP_004579.1; NM_004588.4.
DR PDB; 5FDY; X-ray; 1.85 A; A/B=30-153.
DR PDB; 5FEB; X-ray; 1.35 A; A=30-151.
DR PDB; 6J8E; EM; 3.00 A; C=27-148.
DR PDB; 6J8G; EM; 3.20 A; C=1-215.
DR PDB; 6J8H; EM; 3.20 A; C=1-215.
DR PDB; 6J8I; EM; 3.20 A; C=1-215.
DR PDB; 6J8J; EM; 3.20 A; C=1-215.
DR PDB; 6VRR; X-ray; 1.45 A; A=30-153.
DR PDB; 7W77; EM; 3.30 A; C=1-215.
DR PDB; 7W7F; EM; 3.35 A; C=1-215.
DR PDBsum; 5FDY; -.
DR PDBsum; 5FEB; -.
DR PDBsum; 6J8E; -.
DR PDBsum; 6J8G; -.
DR PDBsum; 6J8H; -.
DR PDBsum; 6J8I; -.
DR PDBsum; 6J8J; -.
DR PDBsum; 6VRR; -.
DR PDBsum; 7W77; -.
DR PDBsum; 7W7F; -.
DR AlphaFoldDB; O60939; -.
DR SMR; O60939; -.
DR BioGRID; 112232; 106.
DR CORUM; O60939; -.
DR IntAct; O60939; 58.
DR STRING; 9606.ENSP00000278947; -.
DR BindingDB; O60939; -.
DR ChEMBL; CHEMBL4630760; -.
DR ChEMBL; CHEMBL4630762; -.
DR ChEMBL; CHEMBL4630763; -.
DR ChEMBL; CHEMBL4630765; -.
DR DrugBank; DB05541; Brivaracetam.
DR DrugBank; DB00907; Cocaine.
DR DrugBank; DB13269; Dichlorobenzyl alcohol.
DR DrugBank; DB13961; Fish oil.
DR DrugBank; DB00776; Oxcarbazepine.
DR DrugBank; DB00243; Ranolazine.
DR DrugBank; DB00313; Valproic acid.
DR DrugBank; DB00909; Zonisamide.
DR DrugCentral; O60939; -.
DR TCDB; 8.A.17.2.1; the na(+) channel auxiliary subunit Beta1-Beta4 (sca-Beta) family.
DR GlyGen; O60939; 3 sites.
DR iPTMnet; O60939; -.
DR PhosphoSitePlus; O60939; -.
DR BioMuta; SCN2B; -.
DR MassIVE; O60939; -.
DR PaxDb; O60939; -.
DR PeptideAtlas; O60939; -.
DR PRIDE; O60939; -.
DR ProteomicsDB; 49682; -.
DR Antibodypedia; 2511; 310 antibodies from 33 providers.
DR DNASU; 6327; -.
DR Ensembl; ENST00000278947.6; ENSP00000278947.5; ENSG00000149575.9.
DR GeneID; 6327; -.
DR KEGG; hsa:6327; -.
DR MANE-Select; ENST00000278947.6; ENSP00000278947.5; NM_004588.5; NP_004579.1.
DR CTD; 6327; -.
DR DisGeNET; 6327; -.
DR GeneCards; SCN2B; -.
DR GeneReviews; SCN2B; -.
DR HGNC; HGNC:10589; SCN2B.
DR HPA; ENSG00000149575; Tissue enhanced (brain, heart muscle).
DR MalaCards; SCN2B; -.
DR MIM; 601327; gene.
DR MIM; 615378; phenotype.
DR neXtProt; NX_O60939; -.
DR OpenTargets; ENSG00000149575; -.
DR Orphanet; 130; Brugada syndrome.
DR Orphanet; 334; Familial atrial fibrillation.
DR PharmGKB; PA303; -.
DR VEuPathDB; HostDB:ENSG00000149575; -.
DR eggNOG; ENOG502R29H; Eukaryota.
DR GeneTree; ENSGT01030000234556; -.
DR HOGENOM; CLU_090350_0_0_1; -.
DR InParanoid; O60939; -.
DR OMA; NCYVTNP; -.
DR OrthoDB; 1380581at2759; -.
DR PhylomeDB; O60939; -.
DR TreeFam; TF331728; -.
DR PathwayCommons; O60939; -.
DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
DR Reactome; R-HSA-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR SignaLink; O60939; -.
DR BioGRID-ORCS; 6327; 8 hits in 1074 CRISPR screens.
DR ChiTaRS; SCN2B; human.
DR GeneWiki; SCN2B; -.
DR GenomeRNAi; 6327; -.
DR Pharos; O60939; Tbio.
DR PRO; PR:O60939; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O60939; protein.
DR Bgee; ENSG00000149575; Expressed in middle temporal gyrus and 142 other tissues.
DR ExpressionAtlas; O60939; baseline and differential.
DR Genevisible; O60939; HS.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IDA:BHF-UCL.
DR GO; GO:0017080; F:sodium channel regulator activity; IDA:BHF-UCL.
DR GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; IEA:Ensembl.
DR GO; GO:0086006; F:voltage-gated sodium channel activity involved in cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IMP:BHF-UCL.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; IMP:BHF-UCL.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0046684; P:response to pyrethroid; IEA:Ensembl.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IDA:BHF-UCL.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000920; Myelin_P0-rel.
DR InterPro; IPR029873; SCN2B.
DR PANTHER; PTHR13869; PTHR13869; 1.
DR PANTHER; PTHR13869:SF3; PTHR13869:SF3; 1.
DR Pfam; PF07686; V-set; 1.
DR PRINTS; PR00213; MYELINP0.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Atrial fibrillation; Brugada syndrome; Disease variant;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Signal;
KW Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..215
FT /note="Sodium channel subunit beta-2"
FT /id="PRO_0000014931"
FT TOPO_DOM 30..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..154
FT /note="Ig-like C2-type"
FT REGION 187..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 56
FT /note="Binds SCN2A"
FT /evidence="ECO:0000305|PubMed:30765605"
FT SITE 135
FT /note="Binds SCN2A"
FT /evidence="ECO:0000305|PubMed:30765605"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54900"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54900"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30765606,
FT ECO:0007744|PDB:6J8G, ECO:0007744|PDB:6J8H,
FT ECO:0007744|PDB:6J8I, ECO:0007744|PDB:6J8J"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..127
FT /evidence="ECO:0000269|PubMed:22992729,
FT ECO:0000269|PubMed:26894959, ECO:0000269|PubMed:30765605,
FT ECO:0000269|PubMed:30765606, ECO:0007744|PDB:5FDY,
FT ECO:0007744|PDB:5FEB, ECO:0007744|PDB:6J8E,
FT ECO:0007744|PDB:6J8G, ECO:0007744|PDB:6J8H,
FT ECO:0007744|PDB:6J8I, ECO:0007744|PDB:6J8J"
FT DISULFID 55
FT /note="Interchain; with alpha subunit"
FT /evidence="ECO:0000269|PubMed:22992729,
FT ECO:0000269|PubMed:26894959, ECO:0000269|PubMed:30765605,
FT ECO:0000269|PubMed:30765606, ECO:0007744|PDB:6J8E,
FT ECO:0007744|PDB:6J8G, ECO:0007744|PDB:6J8H,
FT ECO:0007744|PDB:6J8I, ECO:0007744|PDB:6J8J"
FT DISULFID 72..75
FT /evidence="ECO:0000269|PubMed:26894959,
FT ECO:0000269|PubMed:30765605, ECO:0000269|PubMed:30765606,
FT ECO:0007744|PDB:5FDY, ECO:0007744|PDB:5FEB,
FT ECO:0007744|PDB:6J8E, ECO:0007744|PDB:6J8G,
FT ECO:0007744|PDB:6J8H, ECO:0007744|PDB:6J8I,
FT ECO:0007744|PDB:6J8J"
FT VARIANT 28
FT /note="R -> Q (in ATFB14; the mutant results in reduced
FT sodium currents and altered channel gating when coexpressed
FT with SCN5A in a heterologous expression system;
FT dbSNP:rs72544145)"
FT /evidence="ECO:0000269|PubMed:19808477"
FT /id="VAR_070229"
FT VARIANT 28
FT /note="R -> W (in ATFB14; the mutant results in reduced
FT sodium currents and altered channel gating when coexpressed
FT with SCN5A in a heterologous expression system;
FT dbSNP:rs17121819)"
FT /evidence="ECO:0000269|PubMed:19808477"
FT /id="VAR_029131"
FT VARIANT 47
FT /note="R -> H (in dbSNP:rs17121818)"
FT /id="VAR_029132"
FT VARIANT 211
FT /note="D -> G (found in a patient with Brugada syndrome;
FT unknown pathological significance; induces a reduction in
FT sodium current density most likely by decreasing SCN5A
FT protein cell surface expression; dbSNP:rs587777023)"
FT /evidence="ECO:0000269|PubMed:23559163"
FT /id="VAR_070230"
FT MUTAGEN 55
FT /note="C->A,S: Does not bind alpha subunit. Loss of ability
FT to protect alpha subunit from inhibition by the spider
FT protoxin-II."
FT /evidence="ECO:0000269|PubMed:26894959"
FT CONFLICT 2
FT /note="H -> Q (in Ref. 1; AAC26013)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="P -> L (in Ref. 1; AAC26013)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="T -> N (in Ref. 1; AAC26013)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="L -> Q (in Ref. 1; AAC26013)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="T -> S (in Ref. 1; AAC26013)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="S -> F (in Ref. 3; AAD47196)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..179
FT /note="MV -> TA (in Ref. 1; AAC26013)"
FT /evidence="ECO:0000305"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:6J8G"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:5FEB"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:5FEB"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:6J8G"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:5FEB"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:5FEB"
FT STRAND 77..89
FT /evidence="ECO:0007829|PDB:5FEB"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5FEB"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5FEB"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:5FEB"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5FEB"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:5FEB"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:5FEB"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:5FEB"
SQ SEQUENCE 215 AA; 24326 MW; 94A30A60A32683F3 CRC64;
MHRDAWLPRP AFSLTGLSLF FSLVPPGRSM EVTVPATLNV LNGSDARLPC TFNSCYTVNH
KQFSLNWTYQ ECNNCSEEMF LQFRMKIINL KLERFQDRVE FSGNPSKYDV SVMLRNVQPE
DEGIYNCYIM NPPDRHRGHG KIHLQVLMEE PPERDSTVAV IVGASVGGFL AVVILVLMVV
KCVRRKKEQK LSTDDLKTEE EGKTDGEGNP DDGAK
