ID M9MSP9_DROME Unreviewed; 2062 AA.
AC M9MSP9;
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:ADV37726.1,
GN ECO:0000313|FlyBase:FBgn0285944};
GN Synonyms=bas {ECO:0000313|EMBL:ADV37726.1}, bss
GN {ECO:0000313|EMBL:ADV37726.1}, Dmel\CG9907
GN {ECO:0000313|EMBL:ADV37726.1}, DmNa[[V]]
GN {ECO:0000313|EMBL:ADV37726.1}, DmNa[[v]]
GN {ECO:0000313|EMBL:ADV37726.1}, DmNa[[v]]1
GN {ECO:0000313|EMBL:ADV37726.1}, DmNav {ECO:0000313|EMBL:ADV37726.1},
GN DmNav1 {ECO:0000313|EMBL:ADV37726.1}, l(1)14Da
GN {ECO:0000313|EMBL:ADV37726.1}, l(1)ESHS48
GN {ECO:0000313|EMBL:ADV37726.1}, lincRNA.S9469
GN {ECO:0000313|EMBL:ADV37726.1}, Nav1 {ECO:0000313|EMBL:ADV37726.1}, Ocd
GN {ECO:0000313|EMBL:ADV37726.1}, olfD {ECO:0000313|EMBL:ADV37726.1}, par
GN {ECO:0000313|EMBL:ADV37726.1}, Para {ECO:0000313|EMBL:ADV37726.1}, sbl
GN {ECO:0000313|EMBL:ADV37726.1}, sbl-1 {ECO:0000313|EMBL:ADV37726.1},
GN Shu {ECO:0000313|EMBL:ADV37726.1}, Shudderer
GN {ECO:0000313|EMBL:ADV37726.1}, VSSC {ECO:0000313|EMBL:ADV37726.1};
GN ORFNames=CG9907 {ECO:0000313|EMBL:ADV37726.1,
GN ECO:0000313|FlyBase:FBgn0285944}, Dmel_CG9907
GN {ECO:0000313|EMBL:ADV37726.1};
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:ADV37726.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:ADV37726.1, 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:ADV37726.1, 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:ADV37726.1, 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:ADV37726.1, 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:ADV37726.1, 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:ADV37726.1, 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:ADV37726.1, 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:ADV37726.1, 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; ADV37726.1; -; Genomic_DNA.
DR RefSeq; NP_001188644.1; NM_001201715.1.
DR SMR; M9MSP9; -.
DR EnsemblMetazoa; FBtr0303699; FBpp0292716; 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; M9MSP9; 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 134..161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 205..227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 239..257
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 263..285
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 395..417
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 755..778
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 799..816
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 828..852
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 883..905
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 963..984
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1272..1294
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1300..1326
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1347..1378
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1465..1491
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1554..1572
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1584..1603
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1615..1634
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1678..1701
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1764..1787
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 1808..1843
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 35..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1932..2027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 421..471
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 35..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1932..1955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2062 AA; 231550 MW; 43C3A192EF72694E CRC64;
MTEDSDSISE EERSLFRPFT RESLVQIEQR IAAEHEKQKE LERKRAEGEV IRYDDEDEDE
GPQPDPTLEQ GVPIPVRLQG SFPPELASTP LEDIDPYYSN VLTFVVVSKG KDIFRFSASK
AMWMLDPFNP IRRVAIYILV HPLFSLFIIT TILVNCILMI MPTTPTVEST EVIFTGIYTF
ESAVKVMARG FILCPFTYLR DAWNWLDFVV IALAYVTMGI DLGNLAALRT FRVLRALKTV
AIVPGLKTIV GAVIESVKNL RDVIILTMFS LSVFALMGLQ IYMGVLTQKC IKKFPLDGSW
GNLTDENWDY HNRNSSNWYS EDEGISFPLC GNISGAGQCD DDYVCLQGFG PNPNYGYTSF
DSFGWAFLSA FRLMTQDFWE DLYQLVLRAA GPWHMLFFIV IIFLGSFYLV NLILAIVAMS
YDELQKKAEE EEAAEEEAIR EAEEAAAAKA AKLEERANAQ AQAAADAAAA EEAALHPEMA
KSPTYSCISY ELFVGGEKGN DDNNKEKMSI RSVEVESESY TIRNGRGRFG IPGSDRKPLV
LSTYQDAQQH LPYADDSNAV TPMSEENGAI IVPVYYGNLG SRHSSYTSHQ SRISYTSHGD
LLGGMAVMGV STMTKESKLR NRNTRNQSVG ATNGGTTCLD TNHKLDHRDY EIGLECTDEA
GKIKHHDNPF IEPVQTQTVV DMKDVMVLND IIEQAAGRHS RASDRGVSVY YFPTEDDDED
GPTFKDKALE VILKGIDVFC VWDCCWVWLK FQEWVSLIVF DPFVELFITL CIVVNTMFMA
MDHHDMNKEM ERVLKSGNYF FTATFAIEAT MKLMAMSPKY YFQEGWNIFD FIIVALSLLE
LGLEGVQGLS VLRSFRLLRV FKLAKSWPTL NLLISIMGRT MGALGNLTFV LCIIIFIFAV
MGMQLFGKNY HDHKDRFPDG DLPRWNFTDF MHSFMIVFRV LCGEWIESMW DCMYVGDVSC
IPFFLATVVI GNLVVLNLFL ALLLSNFGSS SLSAPTADND TNKIAEAFNR IGRFKSWVKR
NIADCFKLIR NKLTNQISDQ PSGKGVCRCI SAEHGDNELE LGHDEILADG LIKKGIKEQT
QLEVAIGDGM EFTIHGDMKN NKPKKSKYLN NATDDDTASI NSYGSHKNRP FKDESHKGSA
ETMEGEEKRD ASKEDLGLDE ELDEEGECEE GPLDGDIIIH AHDEDILDEY PADCCPDSYY
KKFPILAGDD DSPFWQGWGN LRLKTFQLIE NKYFETAVIT MILMSSLALA LEDVHLPQRP
ILQDILYYMD RIFTVIFFLE MLIKWLALGF KVYFTNAWCW LDFVIVMVSL INFVASLVGA
GGIQAFKTMR TLRALRPLRA MSRMQGMRVV VNALVQAIPS IFNVLLVCLI FWLIFAIMGV
QLFAGKYFKC EDMNGTKLSH EIIPNRNACE SENYTWVNSA MNFDHVGNAY LCLFQVATFK
GWIQIMNDAI DSREVDKQPI RETNIYMYLY FVFFIIFGSF FTLNLFIGVI IDNFNEQKKK
AGGSLEMFMT EDQKKYYNAM KKMGSKKPLK AIPRPRWRPQ AIVFEIVTDK KFDIIIMLFI
GLNMFTMTLD RYDASDTYNA VLDYLNAIFV VIFSSECLLK IFALRYHYFI EPWNLFDVVV
VILSILGLVL SDIIEKYFVS PTLLRVVRVA KVGRVLRLVK GAKGIRTLLF ALAMSLPALF
NICLLLFLVM FIFAIFGMSF FMHVKEKSGI NDVYNFKTFG QSMILLFQMS TSAGWDGVLD
AIINEEACDP PDNDKGYPGN CGSATVGITF LLSYLVISFL IVINMYIAVI LENYSQATED
VQEGLTDDDY DMYYEIWQQF DPEGTQYIRY DQLSEFLDVL EPPLQIHKPN KYKIISMDIP
ICRGDLMYCV DILDALTKDF FARKGNPIEE TGEIGEIAAR PDTEGYEPVS STLWRQREEY
CARLIQHAWR KHKARGEGGG SFEPDTDHGD GGDPDAGDPA PDEATDGDAP AGGDGSVNGT
AEGAADADES NVNSPGEDAA AAAAAAAAAA AAGTTTAGSP GAGSAGRQTA VLVESDGFVT
KNGHKVVIHS RSPSITSRTA DV
//