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Database: UniProt
Entry: SCN60_DROME
LinkDB: SCN60_DROME
Original site: SCN60_DROME 
ID   SCN60_DROME             Reviewed;        2821 AA.
AC   Q9W0Y8; A9NIV8; Q27930; Q7JN09; Q7JN86; Q7JN87; Q7JN88; Q7JN89;
AC   Q7K324; Q8MMC7;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 5.
DT   25-OCT-2017, entry version 125.
DE   RecName: Full=Sodium channel protein 60E;
DE   AltName: Full=Drosophila ion channel 60;
DE   AltName: Full=Drosophila sodium channel 1;
DE   AltName: Full=Protein smell-impaired 60E;
DE   AltName: Full=Sodium channel 2;
DE            Short=DmNav2;
GN   Name=NaCP60E;
GN   Synonyms=DIC60 {ECO:0000312|EMBL:CAA59129.1},
GN   DSC1 {ECO:0000303|PubMed:8083728},
GN   smi60E {ECO:0000303|PubMed:12196396}; ORFNames=CG34405;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   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:0000305}
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-2349, AND RNA EDITING OF POSITION
RP   2002.
RA   Song W., Liu Z., Nomura Y., Dong K.;
RT   "Functional characterization of the DSC1 channel.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000305, ECO:0000312|EMBL:CAA32567.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 84-2407.
RX   PubMed=2444928; DOI=10.1093/nar/15.20.8569;
RA   Salkoff L., Butler A., Scavarda N., Wei A.;
RT   "Nucleotide sequence of the putative sodium channel gene from
RT   Drosophila: the four homologous domains.";
RL   Nucleic Acids Res. 15:8569-8572(1987).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2141-2821.
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6] {ECO:0000305, ECO:0000312|EMBL:CAA59129.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2158-2293.
RA   Okamoto H., Sakai K., Goto S., Takasu-Ishikawa E., Hotta Y.;
RT   "Isolation of Drosophila genomic clones homologous to the Eel sodium
RT   channel gene.";
RL   Proc. Jpn. Acad., B, Phys. Biol. Sci. 63:284-288(1987).
RN   [7] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RX   PubMed=8083728;
RA   Hong C.S., Ganetzky B.;
RT   "Spatial and temporal expression patterns of two sodium channel genes
RT   in Drosophila.";
RL   J. Neurosci. 14:5160-5169(1994).
RN   [8] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12196396;
RA   Kulkarni N.H., Yamamoto A.H., Robinson K.O., Mackay T.F.C.,
RA   Anholt R.R.;
RT   "The DSC1 channel, encoded by the smi60E locus, contributes to odor-
RT   guided behavior in Drosophila melanogaster.";
RL   Genetics 161:1507-1516(2002).
RN   [9] {ECO:0000305}
RP   RNA EDITING OF POSITION 2002.
RX   PubMed=12907802; DOI=10.1126/science.1086763;
RA   Hoopengardner B., Bhalla T., Staber C., Reenan R.;
RT   "Nervous system targets of RNA editing identified by comparative
RT   genomics.";
RL   Science 301:832-836(2003).
CC   -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability
CC       of excitable membranes. Plays a role in processing of olfactory
CC       information during the olfactory avoidance response.
CC       {ECO:0000269|PubMed:12196396}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12196396};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}.
CC   -!- TISSUE SPECIFICITY: In embryonic and larval stages, expression is
CC       limited to very few non-neuronal cells in either the CNS or PNS.
CC       In pupal and adult stages, expressed in cell bodies of the fly
CC       central nervous system, including optic lobes, central brain,
CC       subesophageal ganglion, thoracico-abdominal ganglion, major
CC       olfactory organs, the third antennal segment and the maxillary
CC       palps. {ECO:0000269|PubMed:12196396, ECO:0000269|PubMed:8083728}.
CC   -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC       hydrophobic segments (S1, S2, S3, S5, S6) and one positively
CC       charged segment (S4). Segments S4 are probably the voltage-sensors
CC       and are characterized by a series of positively charged amino
CC       acids at every third position. {ECO:0000305}.
CC   -!- RNA EDITING: Modified_positions=2002 {ECO:0000269|PubMed:12907802,
CC       ECO:0000269|Ref.3}; Note=Partially edited. Target of Adar.
CC       {ECO:0000269|PubMed:12907802};
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       NaCP60E subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL25396.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=ABF70206.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=CAA32567.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAA32568.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AE013599; AAF47291.5; -; Genomic_DNA.
DR   EMBL; DQ466888; ABF70206.1; ALT_SEQ; mRNA.
DR   EMBL; X14394; CAA32567.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X14395; CAA32568.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X14396; CAA32569.1; -; Genomic_DNA.
DR   EMBL; X14397; CAA32570.1; -; Genomic_DNA.
DR   EMBL; X14398; CAA32571.1; -; Genomic_DNA.
DR   EMBL; AY060357; AAL25396.1; ALT_SEQ; mRNA.
DR   EMBL; X84409; CAA59129.1; -; Genomic_DNA.
DR   PIR; S04029; A60165.
DR   RefSeq; NP_001189007.2; NM_001202078.3.
DR   RefSeq; NP_726495.3; NM_166696.5.
DR   UniGene; Dm.20002; -.
DR   ProteinModelPortal; Q9W0Y8; -.
DR   BioGrid; 63549; 22.
DR   IntAct; Q9W0Y8; 6.
DR   MINT; MINT-282473; -.
DR   STRING; 7227.FBpp0303273; -.
DR   TCDB; 1.A.1.10.13; the voltage-gated ion channel (vic) superfamily.
DR   PaxDb; Q9W0Y8; -.
DR   PRIDE; Q9W0Y8; -.
DR   GeneID; 37981; -.
DR   KEGG; dme:Dmel_CG34405; -.
DR   CTD; 37981; -.
DR   FlyBase; FBgn0085434; NaCP60E.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   InParanoid; Q9W0Y8; -.
DR   KO; K21862; -.
DR   OrthoDB; EOG091G01WJ; -.
DR   ChiTaRS; NaCP60E; fly.
DR   GenomeRNAi; 37981; -.
DR   PRO; PR:Q9W0Y8; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   ExpressionAtlas; Q9W0Y8; differential.
DR   GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR   GO; GO:0022843; F:voltage-gated cation channel activity; IDA:FlyBase.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; ISS:FlyBase.
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:0042048; P:olfactory behavior; IMP:FlyBase.
DR   GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR   GO; GO:0030431; P:sleep; IEP:FlyBase.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; ISS:FlyBase.
DR   GO; GO:0006814; P:sodium ion transport; NAS:FlyBase.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001696; Na_channel_asu.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00170; NACHANNEL.
DR   PROSITE; PS50096; IQ; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Olfaction; Reference proteome;
KW   Repeat; RNA editing; Sensory transduction; Sodium; Sodium channel;
KW   Sodium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1   2821       Sodium channel protein 60E.
FT                                /FTId=PRO_0000291840.
FT   TOPO_DOM      1    121       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    122    145       Helical; Name=S1 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    146    151       Extracellular. {ECO:0000305}.
FT   TRANSMEM    152    172       Helical; Name=S2 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    173    183       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    184    202       Helical; Name=S3 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    203    208       Extracellular. {ECO:0000305}.
FT   TRANSMEM    209    228       Helical; Voltage-sensor; Name=S4 of
FT                                repeat I. {ECO:0000255}.
FT   TOPO_DOM    229    244       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    245    265       Helical; Name=S5 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    266    340       Extracellular. {ECO:0000305}.
FT   INTRAMEM    341    365       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    366    374       Extracellular. {ECO:0000305}.
FT   TRANSMEM    375    395       Helical; Name=S6 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    396    687       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    688    708       Helical; Name=S1 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    709    718       Extracellular. {ECO:0000305}.
FT   TRANSMEM    719    743       Helical; Name=S2 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    744    749       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    750    769       Helical; Name=S3 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    770    775       Extracellular. {ECO:0000305}.
FT   TRANSMEM    776    795       Helical; Voltage-sensor; Name=S4 of
FT                                repeat II. {ECO:0000250}.
FT   TOPO_DOM    796    810       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    811    832       Helical; Name=S5 of repeat II.
FT                                {ECO:0000250}.
FT   TOPO_DOM    833    852       Extracellular. {ECO:0000305}.
FT   INTRAMEM    853    873       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    874    882       Extracellular. {ECO:0000305}.
FT   TRANSMEM    883    903       Helical; Name=S6 of repeat II.
FT                                {ECO:0000250}.
FT   TOPO_DOM    904   1719       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1720   1740       Helical; Name=S1 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1741   1766       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1767   1787       Helical; Name=S2 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1788   1790       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1791   1811       Helical; Name=S3 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1812   1816       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1817   1838       Helical; Voltage-sensor; Name=S4 of
FT                                repeat III. {ECO:0000255}.
FT   TOPO_DOM   1839   1857       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1858   1879       Helical; Name=S5 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1880   1920       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1921   1942       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1943   1958       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1959   1979       Helical; Name=S6 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1980   2046       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   2047   2067       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   2068   2072       Extracellular. {ECO:0000305}.
FT   TRANSMEM   2073   2093       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   2094   2109       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   2110   2130       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   2131   2139       Extracellular. {ECO:0000305}.
FT   TRANSMEM   2140   2161       Helical; Voltage-sensor; Name=S4 of
FT                                repeat IV. {ECO:0000255}.
FT   TOPO_DOM   2162   2176       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   2177   2197       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   2198   2213       Extracellular. {ECO:0000305}.
FT   INTRAMEM   2214   2236       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   2237   2265       Extracellular. {ECO:0000305}.
FT   TRANSMEM   2266   2286       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   2287   2821       Cytoplasmic. {ECO:0000305}.
FT   REPEAT      107    434       I. {ECO:0000305}.
FT   REPEAT      668   1107       II. {ECO:0000305}.
FT   REPEAT     1700   2017       III. {ECO:0000305}.
FT   REPEAT     2027   2288       IV. {ECO:0000305}.
FT   DOMAIN     2418   2447       IQ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00116}.
FT   CARBOHYD    282    282       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    293    293       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    311    311       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1755   1755       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1766   1766       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    272    318       {ECO:0000250|UniProtKB:D0E0C2}.
FT   DISULFID    875    887       {ECO:0000250|UniProtKB:D0E0C2}.
FT   VARIANT    2002   2002       M -> V (in RNA edited version).
FT   CONFLICT      2      2       S -> G (in Ref. 3; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT     85     85       F -> V (in Ref. 4; CAA32567).
FT                                {ECO:0000305}.
FT   CONFLICT     93     93       R -> Q (in Ref. 3; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT    195    196       SG -> MR (in Ref. 4; CAA32567).
FT                                {ECO:0000305}.
FT   CONFLICT    233    234       NA -> RP (in Ref. 4; CAA32567).
FT                                {ECO:0000305}.
FT   CONFLICT    239    240       FR -> VA (in Ref. 4; CAA32567).
FT                                {ECO:0000305}.
FT   CONFLICT    253    253       L -> V (in Ref. 4; CAA32567).
FT                                {ECO:0000305}.
FT   CONFLICT    478    478       G -> S (in Ref. 3; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT    487    487       H -> D (in Ref. 3; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT    535    535       N -> T (in Ref. 3; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT    601    601       Q -> R (in Ref. 3; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT    785    785       V -> A (in Ref. 4; CAA32568).
FT                                {ECO:0000305}.
FT   CONFLICT    790    790       Q -> K (in Ref. 4; CAA32568).
FT                                {ECO:0000305}.
FT   CONFLICT    807    807       G -> R (in Ref. 3; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT    813    813       T -> R (in Ref. 4; CAA32568).
FT                                {ECO:0000305}.
FT   CONFLICT    901    901       M -> MVLNLFLALLLNSFNSEELKSKKE (in Ref. 3;
FT                                ABF70206). {ECO:0000305}.
FT   CONFLICT   1029   1029       P -> A (in Ref. 3; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT   1091   1091       R -> C (in Ref. 3; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT   1101   1101       E -> ELR (in Ref. 3; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT   1649   1649       Y -> C (in Ref. 3; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT   1713   1714       HW -> AL (in Ref. 4; CAA32569).
FT                                {ECO:0000305}.
FT   CONFLICT   1757   1757       T -> A (in Ref. 3; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT   1882   1895       FKCVNEMGELLPIT -> LSALINIINHFIFQ (in Ref.
FT                                4; CAA32569). {ECO:0000305}.
FT   CONFLICT   1937   1937       M -> N (in Ref. 4; CAA32569).
FT                                {ECO:0000305}.
FT   CONFLICT   1954   1954       Q -> R (in Ref. 4; CAA32569).
FT                                {ECO:0000305}.
FT   CONFLICT   1992   1993       KK -> RR (in Ref. 4; CAA32569).
FT                                {ECO:0000305}.
FT   CONFLICT   1995   1995       Y -> I (in Ref. 4; CAA32570).
FT                                {ECO:0000305}.
FT   CONFLICT   2110   2111       VF -> SV (in Ref. 4; CAA32571).
FT                                {ECO:0000305}.
FT   CONFLICT   2223   2223       R -> Q (in Ref. 4; CAA32571).
FT                                {ECO:0000305}.
FT   CONFLICT   2238   2240       Missing (in Ref. 6; CAA59129).
FT                                {ECO:0000305}.
FT   CONFLICT   2256   2256       C -> S (in Ref. 4; CAA32571).
FT                                {ECO:0000305}.
FT   CONFLICT   2332   2332       I -> V (in Ref. 3; ABF70206 and 5;
FT                                AAL25396). {ECO:0000305}.
FT   CONFLICT   2341   2341       I -> T (in Ref. 3; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT   2362   2362       I -> M (in Ref. 5; AAL25396).
FT                                {ECO:0000305}.
FT   CONFLICT   2368   2369       LH -> FD (in Ref. 4; CAA32571).
FT                                {ECO:0000305}.
FT   CONFLICT   2384   2389       NFKQLQ -> DFGQLR (in Ref. 5; AAL25396).
FT                                {ECO:0000305}.
FT   CONFLICT   2433   2433       L -> LYLGVTNPIVSLH (in Ref. 5; AAL25396).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2821 AA;  318625 MW;  B817FB1372E68AEF CRC64;
     MSDDQATFND EKAVAKHQVV AYTQRSQVKH ENRHIQLVRE YGFHPRTKAS VEDGDVLPRK
     FEPFPEHMYG KPLEEIDTFI YEETFCVVSK RFRKNYIHRF TGTKSLFLFY PWSPARRVCV
     YIATNQFFDY CVMATILFNC IFLAMTETVE EAEYIFLAIY SIEMVIKIIA KGFLLNKYTY
     LRNPWNWLDF VVITSGYATI GMEVGNLAGL RTFRVLRALK TVSIMPGLKT IINALLHSFR
     QLAEVMTLTI FCLMVFALFA LQVYMGELRN KCVRQVPTDW TNVSHTDWQI WVNDTDNWLY
     DEDELPVLCG NLTGARHCPF EYVCLCVGEN PNHGYTNFDN FMWSMLTTFQ LITLDYWENV
     YNMVLATCGP MSVSFFTVVV FFGSFYLINL MLAVVALSYE EEAEITNEER KKDLLDHRDD
     STFSFDPSVL NVKKLNKNNK KKIDSRKGVL LASYSKKKTR RKKTKGGKEG GTNGNGNGSN
     GDDNKSHSAT PSPGPSPRHS ATERPSALTM QAQKQYQQME QQHKLAKSGS GGSNNPMAPT
     PKGRISFQDS GMGVKNPNML YPSDYKGQLI ANSGQPSSNS SGVNRESSQD DSGVVDDHEE
     QDTTNDMGHV STVELALSPR EVRLIKCNGN IARIKNHNVY ALHQEFSSEV VVIDDLPDRN
     CDRCVHWCTD YESWLQFQNC LYKVVRDPLF ELAITLCIVL NTAFLAMEHH GMSESFRNAL
     DVGNKVFTSI FTFECIVKLM ALSKDFFLCG WNIFDLLIVT ASLLDIIFEL VDGLSVLRGL
     RLLRVLKLAQ SWTTMKVLLS IIISTIGALG NLTLILVIVI YIFAVIGMQL FSKDYTPEKF
     DPDPVPRWNF NDFFHSFMMI FRILCGEWIE PLWDCMRAEE EQGASTCFAI FLPTLVMGNF
     MEVGEESKLA RSIERVRDLI RKKRQERKDR KERKFAEKFQ QIVLDAQQAH AQTLSHQAAV
     GLERGDKPGV LAETKFHRLS YQESMNRPVS GSDFGFQIPL HDGLHTIVDG LEYDDTGDLP
     EQIQLQAHPL PPTSDSMPPT YESAMMATTG GSFSSVNGNG TCQNLTPFVQ AERRLQHQIS
     SGVSTQQYDS REEATYTESI ELLGQYNSTD TDPYANDQRS GCGSFNRGDS LQDNSSRRYG
     SEEHDEAFLK YQKSLLTRSP SYRKSLDRLS QSSGQSQRSL LKSEEAEMRR HSSGQSLNSM
     SIEQDELLSQ QGNLREELLN CDQKELFQFL QEEEELQKGT KLRRISNVMR SRRPSSQMGQ
     PENETMVEHS EFDNIIQSFE KELEEIKRST TSLERKLSNL SEPSPAADEA TKAIMEHIAI
     ITGASERSAA DEVVLPLNPY DSYDLSSVPR RSQSVSAAAQ RQSVKLKRRS LEKQRKIDED
     FSISNEIRKI CDQIHAPFVA MEAMAVAATS ASQAQPNQSP FLRRKVDPFT VQFDRFKRLS
     LIERVEEVPE EEKPISTLRI ESEKMPRKFL HGPDQLRLDS LSLKSTNSYE NLLIQKQKLG
     MATPPAVPAT PPTSLKSSIE PPTLAQISSL KTTPPLAALT EHQQHFHATS IQAAPTPAHT
     HAHSQAHAHS MAGQRRRMEH PQSTLDKAAS FQSARTESHS SGAADASSAL ALAMAQKTEQ
     SQSTAPDATQ KPSAFTRLTE KPWHCLVSYV DDLTVGGRRN SQGAYNDPMT FPSYGATKAA
     KVPDDCFPQK CYDHFYFRCP WFMSCMDTQS AKHWTRVRTA VLTVVDTPAF EWFVLVLIFA
     SSITLCFEDI NLDKNKTLKR VLYWINFSFC LIFVVEMILK WLALGFSKYF TSFWTILDFI
     IVFVSVFSLL IEENENLKVL RSLRTLRALR PLRAISRWQG MRIVVNALMY AIPSIFNVLL
     VCLVFWLIFS IMGVQFFGGK FFKCVNEMGE LLPITEVNDK WDCIEQNYTW INSKITFDHV
     GMGYLALLQV ATFEGWMEVM ADAVDARGVD LQPQREANLY AYIYFVIFIV CGSFFTLNLF
     IGVIIDNFNM LKKKYEGGVL EMFLTESQKH YYTAMKKLGR KKPQKVIKRP INHFLAMFYD
     LSNSRRFEIA IFVLIFLNML TMGIEHYDQP HAVFFILEVS NAFFTTVFGL EAIVKIVGLR
     YHYFTVPWNV FDFLLVLASI FGILMEDIMI DLPISPTLLR VVRVFRIGRI LRLIKAAKGI
     RKLLFALVVS LPALFNIGAL LGLITFIYAI LGMSLFGNVK LQGALDDMVN FQTFGRSMQL
     LFRLMTSAGW NDVLESLMIQ PPDCDPFIHG HTNGNCGHPL LAITYFTSFI IISYMIVINM
     YIAIILENFN QAHQEEEIGI VEDDLEMFYI RWSKYDPHAT QFIHFSQLSD FIASLDPPLG
     ISKPNNVALV SFNLPISKGN KIHCLDILHA LVKHVLGHVE ETDNFKQLQE QMDVKFKKQF
     PTRKELEIVS STRIWKRQEK AAKTIQTGWK EYLRRKREKE RSNSGDSATQ TSSPGGWQSK
     LSALNFFHLQ VSRRGTACSS RASSRKSSRA SDASDLSELA GPWLNLPLML VSGADEVVKD
     IKQQNDELGK RGSIFVEAPR ASRRRSFYNF FLRHQDAVDD SLTSPSVHRK TAMNNTTNTT
     SNSASTSGTA SSTATAPATG CGPAATSASD SDRHQAVGGG SAPSRKRASS FIRKKPPLER
     GLSAQSALRV NKNAFVSEAS APEVIVTRPS PEQQTHPHSL SLRPDNATLV HVLVHRESEE
     YKEEDESSPS VSGNGNGFGV GLDMLSKQPP PQIRITTGSV ESSMDTCAMP TVQIMVDSPK
     DPPRGDFSSA PIDDVGAPID VNVQGDTSQV FYDYNPEKAT DDQGNGQDET AQFESLPDRQ
     R
//
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