ID M9MS75_DROME Unreviewed; 2110 AA. AC M9MS75; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 28-JUN-2023, entry version 74. DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132}; GN Name=para {ECO:0000313|EMBL:ADV37697.1, GN ECO:0000313|FlyBase:FBgn0285944}; GN Synonyms=bas {ECO:0000313|EMBL:ADV37697.1}, bss GN {ECO:0000313|EMBL:ADV37697.1}, Dmel\CG9907 GN {ECO:0000313|EMBL:ADV37697.1}, DmNa[[V]] GN {ECO:0000313|EMBL:ADV37697.1}, DmNa[[v]] GN {ECO:0000313|EMBL:ADV37697.1}, DmNa[[v]]1 GN {ECO:0000313|EMBL:ADV37697.1}, DmNav {ECO:0000313|EMBL:ADV37697.1}, GN DmNav1 {ECO:0000313|EMBL:ADV37697.1}, l(1)14Da GN {ECO:0000313|EMBL:ADV37697.1}, l(1)ESHS48 GN {ECO:0000313|EMBL:ADV37697.1}, lincRNA.S9469 GN {ECO:0000313|EMBL:ADV37697.1}, Nav1 {ECO:0000313|EMBL:ADV37697.1}, Ocd GN {ECO:0000313|EMBL:ADV37697.1}, olfD {ECO:0000313|EMBL:ADV37697.1}, par GN {ECO:0000313|EMBL:ADV37697.1}, Para {ECO:0000313|EMBL:ADV37697.1}, sbl GN {ECO:0000313|EMBL:ADV37697.1}, sbl-1 {ECO:0000313|EMBL:ADV37697.1}, GN Shu {ECO:0000313|EMBL:ADV37697.1}, Shudderer GN {ECO:0000313|EMBL:ADV37697.1}, VSSC {ECO:0000313|EMBL:ADV37697.1}; GN ORFNames=CG9907 {ECO:0000313|EMBL:ADV37697.1, GN ECO:0000313|FlyBase:FBgn0285944}, Dmel_CG9907 GN {ECO:0000313|EMBL:ADV37697.1}; 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:ADV37697.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:ADV37697.1, 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:ADV37697.1, 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:ADV37697.1, 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., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., Harris N.L., RA Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., RA 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:ADV37697.1, 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:ADV37697.1, 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:ADV37697.1, 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:ADV37697.1, 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:ADV37697.1, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014298; ADV37697.1; -; Genomic_DNA. DR RefSeq; NP_001188615.1; NM_001201686.1. DR SMR; M9MS75; -. DR EnsemblMetazoa; FBtr0303670; FBpp0292687; 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 tissues. DR ExpressionAtlas; M9MS75; 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:0005244; F:voltage-gated monoatomic ion channel activity; IEA:UniProtKB-KW. DR GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro. DR GO; GO:0034765; P:regulation of monoatomic ion transmembrane transport; IEA:UniProtKB-KW. 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 PARA; 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 1320..1342 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1348..1374 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1395..1426 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1513..1539 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1602..1620 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1632..1651 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1663..1682 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1726..1749 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT TRANSMEM 1812..1835 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361132" FT DOMAIN 1856..1891 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 1145..1219 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1980..2075 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 1145..1159 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1160..1174 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1175..1204 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1205..1219 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1980..2003 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 2110 AA; 236817 MW; 4A1F05C08F8EAD0A 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 GKGVCRCISA EHGDNELELG HDEILADGLI KKGIKEQTQL EVAIGDGMEF TIHGDMKNNK PKKSKYLNNA TDDDTASINS YGSHKNRPFK DESHKGSAET MEGEEKRDAS KEDLGLDEEL DEEGECEEGP LDGDIIIHAH DEDILDEYPA DCCPDSYYKK FPILAGDDDS PFWQGWGNLR LKTFQLIENK YFETAVITMI LMSSLALALE DVHLPQRPIL QDILYYMDRI FTVIFFLEML IKWLALGFKV YFTNAWCWLD FVIVMVSLIN FVASLVGAGG IQAFKTMRTL RALRPLRAMS RMQGMRVVVN ALVQAIPSIF NVLLVCLIFW LIFAIMGVQL FAGKYFKCED MNGTKLSHEI IPNRNACESE NYTWVNSAMN FDHVGNAYLC LFQVATFKGW IQIMNDAIDS REVDKQPIRE TNIYMYLYFV FFIIFGSFFT LNLFIGVIID NFNEQKKKAG GSLEMFMTED QKKYYNAMKK MGSKKPLKAI PRPRWRPQAI VFEIVTDKKF DIIIMLFIGL NMFTMTLDRY DASDTYNAVL DYLNAIFVVI FSSECLLKIF ALRYHYFIEP WNLFDVVVVI LSILGLVLSD IIEKYFVSPT LLRVVRVAKV GRVLRLVKGA KGIRTLLFAL AMSLPALFNI CLLLFLVMFI FAIFGMSFFM HVKEKSGIND VYNFKTFGQS MILLFQMSTS AGWDGVLDAI INEEACDPPD NDKGYPGNCG SATVGITFLL SYLVISFLIV INMYIAVILE NYSQATEDVQ EGLTDDDYDM YYEIWQQFDP EGTQYIRYDQ LSEFLDVLEP PLQIHKPNKY KIISMDIPIC RGDLMYCVDI LDALTKDFFA RKGNPIEETG EIGEIAARPD TEGYEPVSST LWRQREEYCA RLIQHAWRKH KARGEGGGSF EPDTDHGDGG DPDAGDPAPD EATDGDAPAG GDGSVNGTAE GAADADESNV NSPGEDAAAA AAAAAAAAAA GTTTAGSPGA GSAGRQTAVL VESDGFVTKN GHKVVIHSRS PSITSRTADV //