ID M9MSE2_DROME Unreviewed; 2089 AA.
AC M9MSE2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN Name=para {ECO:0000313|EMBL:ADV37703.1,
GN ECO:0000313|FlyBase:FBgn0285944};
GN Synonyms=bas {ECO:0000313|EMBL:ADV37703.1}, bss
GN {ECO:0000313|EMBL:ADV37703.1}, Dmel\CG9907
GN {ECO:0000313|EMBL:ADV37703.1}, DmNa[[V]]
GN {ECO:0000313|EMBL:ADV37703.1}, DmNa[[v]]
GN {ECO:0000313|EMBL:ADV37703.1}, DmNa[[v]]1
GN {ECO:0000313|EMBL:ADV37703.1}, DmNav {ECO:0000313|EMBL:ADV37703.1},
GN DmNav1 {ECO:0000313|EMBL:ADV37703.1}, l(1)14Da
GN {ECO:0000313|EMBL:ADV37703.1}, l(1)ESHS48
GN {ECO:0000313|EMBL:ADV37703.1}, lincRNA.S9469
GN {ECO:0000313|EMBL:ADV37703.1}, Nav1 {ECO:0000313|EMBL:ADV37703.1}, Ocd
GN {ECO:0000313|EMBL:ADV37703.1}, olfD {ECO:0000313|EMBL:ADV37703.1}, par
GN {ECO:0000313|EMBL:ADV37703.1}, Para {ECO:0000313|EMBL:ADV37703.1}, sbl
GN {ECO:0000313|EMBL:ADV37703.1}, sbl-1 {ECO:0000313|EMBL:ADV37703.1},
GN Shu {ECO:0000313|EMBL:ADV37703.1}, Shudderer
GN {ECO:0000313|EMBL:ADV37703.1}, VSSC {ECO:0000313|EMBL:ADV37703.1};
GN ORFNames=CG9907 {ECO:0000313|EMBL:ADV37703.1,
GN ECO:0000313|FlyBase:FBgn0285944}, Dmel_CG9907
GN {ECO:0000313|EMBL:ADV37703.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:ADV37703.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:ADV37703.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A.,
RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|EMBL:ADV37703.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|EMBL:ADV37703.1, ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000313|EMBL:ADV37703.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:ADV37703.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:ADV37703.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:ADV37703.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:ADV37703.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
CC -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, the protein
CC forms a sodium-selective channel through which Na(+) ions may pass in
CC accordance with their electrochemical gradient.
CC {ECO:0000256|RuleBase:RU361132}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361132}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC {ECO:0000256|RuleBase:RU361132}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361132}.
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DR EMBL; AE014298; ADV37703.1; -; Genomic_DNA.
DR RefSeq; NP_001188621.1; NM_001201692.1.
DR SMR; M9MSE2; -.
DR EnsemblMetazoa; FBtr0303676; FBpp0292693; FBgn0285944.
DR GeneID; 32619; -.
DR AGR; FB:FBgn0285944; -.
DR CTD; 32619; -.
DR FlyBase; FBgn0285944; para.
DR VEuPathDB; VectorBase:FBgn0285944; -.
DR GeneTree; ENSGT00940000167131; -.
DR OrthoDB; 1110761at2759; -.
DR BioGRID-ORCS; 32619; 0 hits in 3 CRISPR screens.
DR ChiTaRS; para; fly.
DR GenomeRNAi; 32619; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0285944; Expressed in brain and 11 other cell types or tissues.
DR ExpressionAtlas; M9MSE2; baseline and differential.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc_dom.
DR InterPro; IPR024583; Na_trans_cytopl.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037:SF288; SODIUM CHANNEL PROTEIN; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR Pfam; PF11933; Na_trans_cytopl; 1.
DR PRINTS; PR00170; NACHANNEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|RuleBase:RU361132};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361132};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361132};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|RuleBase:RU361132};
KW Sodium channel {ECO:0000256|ARBA:ARBA00022461,
KW ECO:0000256|RuleBase:RU361132};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361132};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361132};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU361132}.
FT TRANSMEM 145..172
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 250..268
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 274..296
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 406..428
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 779..802
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 823..840
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 852..876
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 907..929
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 987..1008
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1299..1321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1327..1353
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1374..1405
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1492..1518
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1581..1599
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1611..1630
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1642..1661
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1705..1728
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1791..1814
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 1835..1870
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 35..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1959..2054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 432..482
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 35..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1198
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1959..1982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2089 AA; 234776 MW; 448E7AB916EB01CB CRC64;
MTEDSDSISE EERSLFRPFT RESLVQIEQR IAAEHEKQKE LERKRAEGEV PQYGRKKKQK
EIRYDDEDED EGPQPDPTLE QGVPIPVRLQ GSFPPELAST PLEDIDPYYS NVLTFVVVSK
GKDIFRFSAS KAMWMLDPFN PIRRVAIYIL VHPLFSLFII TTILVNCILM IMPTTPTVES
TEVIFTGIYT FESAVKVMAR GFILCPFTYL RDAWNWLDFV VIALAYVTMG IDLGNLAALR
TFRVLRALKT VAIVPGLKTI VGAVIESVKN LRDVIILTMF SLSVFALMGL QIYMGVLTQK
CIKKFPLDGS WGNLTDENWD YHNRNSSNWY SEDEGISFPL CGNISGAGQC DDDYVCLQGF
GPNPNYGYTS FDSFGWAFLS AFRLMTQDFW EDLYQLVLRA AGPWHMLFFI VIIFLGSFYL
VNLILAIVAM SYDELQKKAE EEEAAEEEAI REAEEAAAAK AAKLEERANA QAQAAADAAA
AEEAALHPEM AKSPTYSCIS YELFVGGEKG NDDNNKEKMS IRSVEVESES TSLSLPGSPF
NIRRGSRSSH KYTIRNGRGR FGIPGSDRKP LVLSTYQDAQ QHLPYADDSN AVTPMSEENG
AIIVPVYYGN LGSRHSSYTS HQSRISYTSH GDLLGGMAVM GVSTMTKESK LRNRNTRNQS
VGATNGGTTC LDTNHKLDHR DYEIGLECTD EAGKIKHHDN PFIEPVQTQT VVDMKDVMVL
NDIIEQAAGR HSRASDRGED DDEDGPTFKD KALEVILKGI DVFCVWDCCW VWLKFQEWVS
LIVFDPFVEL FITLCIVVNT MFMAMDHHDM NKEMERVLKS GNYFFTATFA IEATMKLMAM
SPKYYFQEGW NIFDFIIVAL SLLELGLEGV QGLSVLRSFR LLRVFKLAKS WPTLNLLISI
MGRTVGALGN LTFVLCIIIF IFAVMGMQLF GKNYTDHKDR FPDGDLPRWN FTDFMHSFMI
VFRVLCGEWI ESMWDCMYVG DVSCIPFFLA TVVIGNLVVL NLFLALLLSN FGSSSLSAPT
ADNDTNKIAE AFNRIGRFKS WVKRNIADCF KLIRNKLTNQ ISDQPSGERT NQISWIWSEE
HGDNELELGH DEILADGLIK KGIKEQTQLE VAIGDGMEFT IHGDMKNNKP KKSKYLNNAT
DDDTASINSY GSHKNRPFKD ESHKGSAETM EGEEKRDASK EDLGLDEELD EEGECEEGPL
DGDIIIHAHD EDILDEYPAD CCPDSYYKKF PILAGDDDSP FWQGWGNLRL KTFQLIENKY
FETAVITMIL MSSLALALED VHLPQRPILQ DILYYMDRIF TVIFFLEMLI KWLALGFKVY
FTNAWCWLDF VIVMVSLINF VASLVGAGGI QAFKTMRTLR ALRPLRAMSR MQGMRVVVNA
LVQAIPSIFN VLLVCLIFWL IFAIMGVQLF AGKYFKCEDM NGTKLSHEII PNRNACESEN
YTWVNSAMNF DHVGNAYLCL FQVATFKGWI QIMNDAIDSR EVDKQPIRET NIYMYLYFVF
FIIFGSFFTL NLFIGVIIDN FNEQKKKAGG SLEMFMTEDQ KKYYNAMKKM GSKKPLKAIP
RPRWRPQAIV FEIVTDKKFD IIIMLFIGLN MFTMTLDRYD ASDTYNAVLD YLNAIFVVIF
SSECLLKIFA LRYHYFIEPW NLFDVVVVIL SILGLVLSDI IEKYFVSPTL LRVVRVAKVG
RVLRLVKGAK GIRTLLFALA MSLPALFNIC LLLFLVMFIF AIFGMSFFMH VKEKSGINDV
YNFKTFGQSM ILLFQMSTSA GWDGVLDAII NEEACDPPDN DKGYPGNCGS ATVGITFLLS
YLVISFLIVI NMYIAVILEN YSQATEDVQE GLTDDDYDMY YEIWQQFDPE GTQYIRYDQL
SEFLDVLEPP LQIHKPNKYK IISMDIPICR GDLMYCVDIL DALTKDFFAR KGNPIEETGE
IGEIAARPDT EGYEPVSSTL WRQREEYCAR LIQHAWRKHK ARGEGGGSFE PDTDHGDGGD
PDAGDPAPDE ATDGDAPAGG DGSVNGTAEG AADADESNVN SPGEDAAAAA AAAAAAAAAG
TTTAGSPGAG SAGRQTAVLV ESDGFVTKNG HKVVIHSRSP SITSRTADV
//
