ID M9MSE7_DROME Unreviewed; 2113 AA.
AC M9MSE7;
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:ADV37718.1,
GN ECO:0000313|FlyBase:FBgn0285944};
GN Synonyms=bas {ECO:0000313|EMBL:ADV37718.1}, bss
GN {ECO:0000313|EMBL:ADV37718.1}, Dmel\CG9907
GN {ECO:0000313|EMBL:ADV37718.1}, DmNa[[V]]
GN {ECO:0000313|EMBL:ADV37718.1}, DmNa[[v]]
GN {ECO:0000313|EMBL:ADV37718.1}, DmNa[[v]]1
GN {ECO:0000313|EMBL:ADV37718.1}, DmNav {ECO:0000313|EMBL:ADV37718.1},
GN DmNav1 {ECO:0000313|EMBL:ADV37718.1}, l(1)14Da
GN {ECO:0000313|EMBL:ADV37718.1}, l(1)ESHS48
GN {ECO:0000313|EMBL:ADV37718.1}, lincRNA.S9469
GN {ECO:0000313|EMBL:ADV37718.1}, Nav1 {ECO:0000313|EMBL:ADV37718.1}, Ocd
GN {ECO:0000313|EMBL:ADV37718.1}, olfD {ECO:0000313|EMBL:ADV37718.1}, par
GN {ECO:0000313|EMBL:ADV37718.1}, Para {ECO:0000313|EMBL:ADV37718.1}, sbl
GN {ECO:0000313|EMBL:ADV37718.1}, sbl-1 {ECO:0000313|EMBL:ADV37718.1},
GN Shu {ECO:0000313|EMBL:ADV37718.1}, Shudderer
GN {ECO:0000313|EMBL:ADV37718.1}, VSSC {ECO:0000313|EMBL:ADV37718.1};
GN ORFNames=CG9907 {ECO:0000313|EMBL:ADV37718.1,
GN ECO:0000313|FlyBase:FBgn0285944}, Dmel_CG9907
GN {ECO:0000313|EMBL:ADV37718.1};
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:ADV37718.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:ADV37718.1, 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:ADV37718.1, 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:ADV37718.1, 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:ADV37718.1, 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:ADV37718.1, 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:ADV37718.1, 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:ADV37718.1, 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:ADV37718.1, 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; ADV37718.1; -; Genomic_DNA.
DR RefSeq; NP_001188636.1; NM_001201707.1.
DR SMR; M9MSE7; -.
DR EnsemblMetazoa; FBtr0303691; FBpp0292708; 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; M9MSE7; 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 803..826
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 847..864
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 876..900
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 931..953
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1011..1032
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1323..1345
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1351..1377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1398..1429
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1516..1542
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1605..1623
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1635..1654
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1666..1685
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1729..1752
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1815..1838
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 1859..1894
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 553..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1983..2078
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 553..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1222
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1983..2006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2113 AA; 237430 MW; 640A19E218C16593 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 VSVIQRQPAP
TTAHQATKVR KVSTTSLSLP GSPFNIRRGS RSSHKYTIRN GRGRFGIPGS DRKPLVLSTY
QDAQQHLPYA DDSNAVTPMS EENGAIIVPV YYGNLGSRHS SYTSHQSRIS YTSHGDLLGG
MAVMGVSTMT KESKLRNRNT RNQSVGATNG GTTCLDTNHK LDHRDYEIGL ECTDEAGKIK
HHDNPFIEPV QTQTVVDMKD VMVLNDIIEQ AAGRHSRASD RGEDDDEDGP TFKDKALEVI
LKGIDVFCVW DCCWVWLKFQ EWVSLIVFDP FVELFITLCI VVNTMFMAMD HHDMNKEMER
VLKSGNYFFT ATFAIEATMK LMAMSPKYYF QEGWNIFDFI IVALSLLELG LEGVQGLSVL
RSFRLLRVFK LAKSWPTLNL LISIMGRTMG ALGNLTFVLC IIIFIFAVMG MQLFGKNYHD
HKDRFPDGDL PRWNFTDFMH SFMIVFRVLC GEWIESMWDC MYVGDVSCIP FFLATVVIGN
LVVLNLFLAL LLSNFGSSSL SAPTADNDTN KIAEAFNRIG RFKSWVKRNI ADCFKLIRNK
LTNQISDQPS GERTNQISWI WSEEHGDNEL ELGHDEILAD GLIKKGIKEQ TQLEVAIGDG
MEFTIHGDMK NNKPKKSKYL NNATDDDTAS INSYGSHKNR PFKDESHKGS AETMEGEEKR
DASKEDLGLD EELDEEGECE EGPLDGDIII HAHDEDILDE YPADCCPDSY YKKFPILAGD
DDSPFWQGWG NLRLKTFQLI ENKYFETAVI TMILMSSLAL ALEDVHLPQR PILQDILYYM
DRIFTVIFFL EMLIKWLALG FKVYFTNAWC WLDFVIVMVS LINFVASLVG AGGIQAFKTM
RTLRALRPLR AMSRMQGMRV VVNALVQAIP SIFNVLLVCL IFWLIFAIMG VQLFAGKYFK
CEDMNGTKLS HEIIPNRNAC ESENYTWVNS AMNFDHVGNA YLCLFQVATF KGWIQIMNDA
IDSREVDKQP IRETNIYMYL YFVFFIIFGS FFTLNLFIGV IIDNFNEQKK KAGGSLEMFM
TEDQKKYYNA MKKMGSKKPL KAIPRPRWRP QAIVFEIVTD KKFDIIIMLF IGLNMFTMTL
DRYDASDTYN AVLDYLNAIF VVIFSSECLL KIFALRYHYF IEPWNLFDVV VVILSILGLV
LSDIIEKYFV SPTLLRVVRV AKVGRVLRLV KGAKGIRTLL FALAMSLPAL FNICLLLFLV
MFIFAIFGMS FFMHVKEKSG INDVYNFKTF GQSMILLFQM STSAGWDGVL DAIINEEACD
PPDNDKGYPG NCGSATVGIT FLLSYLVISF LIVINMYIAV ILENYSQATE DVQEGLTDDD
YDMYYEIWQQ FDPEGTQYIR YDQLSEFLDV LEPPLQIHKP NKYKIISMDI PICRGDLMYC
VDILDALTKD FFARKGNPIE ETGEIGEIAA RPDTEGYEPV SSTLWRQREE YCARLIQHAW
RKHKARGEGG GSFEPDTDHG DGGDPDAGDP APDEATDGDA PAGGDGSVNG TAEGAADADE
SNVNSPGEDA AAAAAAAAAA AAAGTTTAGS PGAGSAGRQT AVLVESDGFV TKNGHKVVIH
SRSPSITSRT ADV
//
