SCNBA_MOUSE
ID SCNBA_MOUSE Reviewed; 1765 AA.
AC Q9R053; E9QM88; Q9JMD4;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Sodium channel protein type 11 subunit alpha;
DE AltName: Full=NaN;
DE AltName: Full=Sensory neuron sodium channel 2;
DE AltName: Full=Sodium channel protein type XI subunit alpha;
DE AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.9;
GN Name=Scn11a; Synonyms=Nan, Nat, Sns2;
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=ICR; TISSUE=Trigeminal ganglion;
RX PubMed=10444332; DOI=10.1006/geno.1999.5890;
RA Dib-Hajj S.D., Tyrrell L., Escayg A., Wood P.M., Meisler M.H., Waxman S.G.;
RT "Coding sequence, genomic organization, and conserved chromosomal
RT localization of the mouse gene Scn11a encoding the sodium channel NaN.";
RL Genomics 59:309-318(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Testis;
RX PubMed=10623609; DOI=10.1006/bbrc.1999.1858;
RA Ogata K., Jeong S.-Y., Murakami H., Hashida H., Suzuki T., Masuda N.,
RA Hirai M., Isahara K., Uchiyama Y., Goto J., Kanazawa I.;
RT "Cloning and expression study of the mouse tetrodotoxin-resistant voltage-
RT gated sodium channel alpha subunit NaT/Scn11a.";
RL Biochem. Biophys. Res. Commun. 267:271-277(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP INDUCTION.
RX PubMed=14515348; DOI=10.1002/jnr.10768;
RA Klein J.P., Tendi E.A., Dib-Hajj S.D., Fields R.D., Waxman S.G.;
RT "Patterned electrical activity modulates sodium channel expression in
RT sensory neurons.";
RL J. Neurosci. Res. 74:192-198(2003).
RN [5]
RP REVIEW.
RX PubMed=12536125; DOI=10.1016/s0166-2236(02)00030-9;
RA Delmas P., Coste B.;
RT "Na+ channel Nav1.9: in search of a gating mechanism.";
RL Trends Neurosci. 26:55-57(2003).
CC -!- FUNCTION: This protein mediates the voltage-dependent sodium ion
CC permeability of excitable membranes. Assuming opened or closed
CC conformations in response to the voltage difference across the
CC membrane, the protein forms a sodium-selective channel through which
CC sodium ions may pass in accordance with their electrochemical gradient.
CC It is a tetrodotoxin-resistant sodium channel isoform. Also involved,
CC with the contribution of the receptor tyrosine kinase NTRK2, in rapid
CC BDNF-evoked neuronal depolarization (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The voltage-resistant sodium channel consists of an ion
CC conducting pore forming alpha-subunit regulated by one or more
CC auxiliary subunits SCN1B, SCN2B and SCN3B.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D0E0C2};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}.
CC -!- TISSUE SPECIFICITY: Expressed in the dorsal root ganglia (C-fiber
CC neurons), spinal cord, trigeminal ganglia, testis, ovary, uterus and
CC small intestine. {ECO:0000269|PubMed:10623609}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 15 dpc onwards.
CC {ECO:0000269|PubMed:10623609}.
CC -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged
CC segment (S4). Segments S4 are probably the voltage-sensors and are
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.9/SCN11A subfamily. {ECO:0000305}.
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DR EMBL; AF118044; AAD53403.1; -; mRNA.
DR EMBL; AB031389; BAA92154.1; -; mRNA.
DR EMBL; AC124662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS40804.1; -.
DR RefSeq; NP_036017.3; NM_011887.3.
DR AlphaFoldDB; Q9R053; -.
DR SMR; Q9R053; -.
DR BioGRID; 204861; 12.
DR STRING; 10090.ENSMUSP00000065466; -.
DR ChEMBL; CHEMBL4523482; -.
DR GlyGen; Q9R053; 11 sites.
DR iPTMnet; Q9R053; -.
DR PhosphoSitePlus; Q9R053; -.
DR PaxDb; Q9R053; -.
DR PRIDE; Q9R053; -.
DR ProteomicsDB; 253421; -.
DR Antibodypedia; 28814; 121 antibodies from 24 providers.
DR DNASU; 24046; -.
DR Ensembl; ENSMUST00000070617; ENSMUSP00000065466; ENSMUSG00000034115.
DR Ensembl; ENSMUST00000215718; ENSMUSP00000149420; ENSMUSG00000034115.
DR GeneID; 24046; -.
DR KEGG; mmu:24046; -.
DR UCSC; uc009sbk.1; mouse.
DR CTD; 11280; -.
DR MGI; MGI:1345149; Scn11a.
DR VEuPathDB; HostDB:ENSMUSG00000034115; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000161553; -.
DR HOGENOM; CLU_000540_5_0_1; -.
DR InParanoid; Q9R053; -.
DR OMA; VEIDMFP; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; Q9R053; -.
DR TreeFam; TF323985; -.
DR Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR BioGRID-ORCS; 24046; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q9R053; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9R053; protein.
DR Bgee; ENSMUSG00000034115; Expressed in lumbar dorsal root ganglion and 46 other tissues.
DR Genevisible; Q9R053; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0044299; C:C-fiber; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IDA:MGI.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IDA:MGI.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR028821; Na_channel_a11su.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR PANTHER; PTHR10037:SF210; PTHR10037:SF210; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR PRINTS; PR00170; NACHANNEL.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Reference proteome; Repeat; Sodium; Sodium channel;
KW Sodium transport; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..1765
FT /note="Sodium channel protein type 11 subunit alpha"
FT /id="PRO_0000048511"
FT TOPO_DOM 1..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 127..148
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250"
FT TOPO_DOM 149..159
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 160..179
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250"
FT TOPO_DOM 180..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..211
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250"
FT TOPO_DOM 212..219
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 220..239
FT /note="Helical; Voltage-sensor; Name=S4 of repeat I"
FT /evidence="ECO:0000250"
FT TOPO_DOM 240..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 256..269
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250"
FT TOPO_DOM 270..342
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 343..367
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 368..374
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 375..400
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250"
FT TOPO_DOM 401..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 571..594
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250"
FT TOPO_DOM 595..605
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 606..629
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250"
FT TOPO_DOM 630..637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 638..659
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250"
FT TOPO_DOM 660..664
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 665..684
FT /note="Helical; Voltage-sensor; Name=S4 of repeat II"
FT /evidence="ECO:0000250"
FT TOPO_DOM 685..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 700..722
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250"
FT TOPO_DOM 723..742
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 743..763
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 764..773
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 774..799
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250"
FT TOPO_DOM 800..1030
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1031..1053
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1054..1067
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1068..1093
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1094..1099
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1100..1117
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1118
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1119..1140
FT /note="Helical; Voltage-sensor; Name=S4 of repeat III"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1141..1159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1160..1181
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1182..1224
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1225..1246
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1247..1262
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1263..1289
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1290..1342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1343..1366
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1367..1377
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1378..1401
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1402..1407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1408..1431
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1432..1440
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1441..1463
FT /note="Helical; Voltage-sensor; Name=S4 of repeat IV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1464..1478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1479..1501
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1502..1515
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1516..1538
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1539..1559
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1560..1584
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1585..1765
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 115..406
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 557..821
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1023..1320
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1329..1619
FT /note="IV"
FT /evidence="ECO:0000305"
FT REGION 470..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 283..320
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 765..775
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT CONFLICT 400
FT /note="A -> G (in Ref. 2; BAA92154)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="R -> K (in Ref. 2; BAA92154)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="N -> K (in Ref. 2; BAA92154)"
FT /evidence="ECO:0000305"
FT CONFLICT 738
FT /note="W -> R (in Ref. 2; BAA92154)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="N -> T (in Ref. 2; BAA92154)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="E -> D (in Ref. 2; BAA92154)"
FT /evidence="ECO:0000305"
FT CONFLICT 843
FT /note="C -> R (in Ref. 2; BAA92154)"
FT /evidence="ECO:0000305"
FT CONFLICT 1023..1024
FT /note="NL -> IF (in Ref. 2; BAA92154)"
FT /evidence="ECO:0000305"
FT CONFLICT 1054
FT /note="F -> L (in Ref. 2; BAA92154)"
FT /evidence="ECO:0000305"
FT CONFLICT 1113
FT /note="G -> V (in Ref. 1; AAD53403 and 2; BAA92154)"
FT /evidence="ECO:0000305"
FT CONFLICT 1212
FT /note="Y -> H (in Ref. 2; BAA92154)"
FT /evidence="ECO:0000305"
FT CONFLICT 1376
FT /note="K -> Q (in Ref. 2; BAA92154)"
FT /evidence="ECO:0000305"
FT CONFLICT 1496
FT /note="N -> S (in Ref. 2; BAA92154)"
FT /evidence="ECO:0000305"
FT CONFLICT 1572
FT /note="F -> L (in Ref. 2; BAA92154)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1765 AA; 201385 MW; 0A17EA3B9D86FB9C CRC64;
MEERYYPVIF PDERNFRPFT FDSLAAIEKR ITIQKEKKKS KDKAATEPQP RPQLDLKASR
KLPKLYGDVP PDLIAKPLED LDPFYKDHKT FMVLNKKRTI YRFSAKRALF ILGPFNPIRS
FMIRISVHSV FSMFIICTVI INCMFMANNS SVDSRPSSNI PEYVFIGIYV LEAVIKILAR
GFIVDEFSYL RDPWNWLDFI VIGTAIAPCF LGNKVNNLST LRTFRVLRAL KAISVISGLK
VIVGALLRSV KKLVDVMVLT LFCLSIFALV GQQLFMGILS QKCIKDDCGP NAFSNKDCFV
KENDSEDFIM CGNWLGRRSC PDGSTCNKTT FNPDYNYTNF DSFGWSFLAM FRVMTQDSWE
KLYRQILRTS GIYFVFFFVV VIFLGSFYLL NLTLAVVTMA YEEQNRNVAA ETEAKEKMFQ
EAQQLLREEK EALVAMGIDR TSLNSLQASS FSPKKRKFFG SKTRKSFFMR GSKTARASAS
DSEDDASKNP QLLEQTKRLS QNLPVELFDE HVDPLHRQRA LSAVSILTIT MQEQEKSQEP
CFPCGKNLAS KYLVWECSPP WLCIKKVLQT IMTDPFTELA ITICIIVNTV FLAMEHHNMD
NSLKDILKIG NWVFTGIFIA EMCLKIIALD PYHYFRHGWN IFDSIVALVS LADVLFHKLS
KNLSFLASLR VLRVFKLAKS WPTLNTLIKI IGHSVGALGN LTVVLTIVVF IFSVVGMRLF
GAKFNKTCST SPESLRRWHM GDFYHSFLVV FRILCGEWIE NMWECMQEME GSPLCVIVFV
LIMVVGKLVV LNLFIALLLN SFSNEEKDGN PEGETRKTKV QLALDRFSRA FYFMARALQN
FCCKRCRRQN SPKPNEATES FAGESRDTAT LDTRSWKEYD SEMTLYTGQA GAPLAPLAKE
EDDMECCGEC DASPTSQPSE EAQACDLPLK TKRLPSPDDH GVEMEVFSEE DPNLTIQSAR
KKSDAASMLS ECSTIDLNDI FRNLQKTVSP QKQPDRCFPK GLSCIFLCCK TIKKKSPWVL
WWNLRKTCYQ IVKHSWFESF IIFVILLSSG ALIFEDVNLP SRPQVEKLLK CTDNIFTFIF
LLEMILKWVA FGFRKYFTSA WCWLDFLIVV VSGLSLTNLP NLKSFRNLRA LRPLRALSQF
EGMKVVVNAL MSAIPAILNV LLVCLIFWLI FCILGVNFFS GKFGRCINGT DINKYFNASN
VPNQSQCLVS NYTWKVPNVN FDNVGNAYLA LLQVATYKGW LDIMNAAVDS RGKDEQPAFE
ANLYAYLYFV VFIIFGSFFT LNLFIGVIID NFNQQQKKLG GQDIFMTEEQ KKYYNAMKKL
GTKKPQKPIP RPLNKCQAFV FDLVTSQVFD VIILGLIVTN MIIMMAESEG QPNEVKKIFD
ILNIVFVVIF TVECLIKVFA LRQHYFTNGW NLFDCVVVVL SIISTLVSGL ENSNVFPPTL
FRIVRLARIG RILRLVRAAR GIRTLLFALM MSLPSLFNIG LLLFLVMFIY AIFGMNWFSK
VKRGSGIDDI FNFDTFSGSM LCLFQITTSA GWDALLNPML ESKASCNSSS QESCQQPQIA
IVYFVSYIII SFLIVVNMYI AVILENFNTA TEESEDPLGE DDFEIFYEIW EKFDPEATQF
IQYSSLSDFA DALPEPLRVA KPNRFQFLMM DLPMVMGDRL HCMDVLFAFT TRVLGNSSGL
DTMKAMMEEK FMEANPFKKL YEPIVTTTKR KEEEECAAVI QRAYRRHMEK MIKLKLKGRS
SSSLQVFCNG DLSSLDVPKI KVHCD
