GenomeNet

Database: UniProt
Entry: SCN60_DROME
LinkDB: SCN60_DROME
Original site: SCN60_DROME 
ID   SCN60_DROME             Reviewed;        2844 AA.
AC   Q9W0Y8; A0A0B4KF50; A9NIV8; Q27930; Q7JN09; Q7JN86; Q7JN87; Q7JN88;
AC   Q7JN89; Q7K324; Q8MMC7;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 6.
DT   23-MAY-2018, entry version 130.
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 [MRNA] (ISOFORM P), AND RNA EDITING OF POSITION
RP   2025.
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   [2]
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   [3] {ECO:0000305}
RP   GENOME REANNOTATION.
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   [4] {ECO:0000305, ECO:0000312|EMBL:CAA32567.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 84-924 AND 1736-2430.
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] {ECO:0000305, ECO:0000312|EMBL:CAA59129.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2181-2316.
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2164-2844 (ISOFORM G).
RC   STRAIN=Berkeley; TISSUE=Head {ECO:0000312|EMBL:AAL25396.1};
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   [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 2025.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=G {ECO:0000312|FlyBase:FBgn0085434}; Synonyms=H
CC       {ECO:0000312|FlyBase:FBgn0085434};
CC         IsoId=Q9W0Y8-1; Sequence=Displayed;
CC       Name=P {ECO:0000312|FlyBase:FBgn0085434};
CC         IsoId=Q9W0Y8-3; Sequence=VSP_059322, VSP_059323;
CC         Note=Ref.1 (ABF70206) sequence is in conflict in position:
CC         2347:S->N. Ref.1 (ABF70206) sequence is in conflict in position:
CC         2400:S->P. {ECO:0000305};
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=2025 {ECO:0000269|PubMed:12907802,
CC       ECO:0000269|Ref.1}; 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=CAA32567.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAA32568.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAA32569.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; DQ466888; ABF70206.1; -; mRNA.
DR   EMBL; AE013599; AAF47291.6; -; Genomic_DNA.
DR   EMBL; AE013599; AGB93705.1; -; Genomic_DNA.
DR   EMBL; X14394; CAA32567.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X14395; CAA32568.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X14396; CAA32569.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X14397; CAA32570.1; -; Genomic_DNA.
DR   EMBL; X14398; CAA32571.1; -; Genomic_DNA.
DR   EMBL; X84409; CAA59129.1; -; Genomic_DNA.
DR   EMBL; AY060357; AAL25396.1; ALT_SEQ; mRNA.
DR   PIR; S04029; A60165.
DR   RefSeq; NP_001189007.2; NM_001202078.3. [Q9W0Y8-1]
DR   RefSeq; NP_001261175.1; NM_001274246.2. [Q9W0Y8-3]
DR   RefSeq; NP_726495.3; NM_166696.5. [Q9W0Y8-1]
DR   UniGene; Dm.20002; -.
DR   ProteinModelPortal; Q9W0Y8; -.
DR   BioGrid; 63549; 22.
DR   IntAct; Q9W0Y8; 6.
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   EnsemblMetazoa; FBtr0333817; FBpp0305951; FBgn0085434. [Q9W0Y8-3]
DR   GeneID; 37981; -.
DR   KEGG; dme:Dmel_CG34405; -.
DR   CTD; 37981; -.
DR   FlyBase; FBgn0085434; NaCP60E.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128242; -.
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; baseline and 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:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; ISS:FlyBase.
DR   GO; GO:0006814; P:sodium ion transport; NAS:FlyBase.
DR   Gene3D; 1.20.120.350; -; 4.
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   InterPro; IPR027359; Volt_channel_dom_sf.
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   Alternative splicing; Cell membrane; Complete proteome;
KW   Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Olfaction; Reference proteome; Repeat; RNA editing;
KW   Sensory transduction; Sodium; Sodium channel; Sodium transport;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1   2844       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:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    146    151       Extracellular. {ECO:0000305}.
FT   TRANSMEM    152    172       Helical; Name=S2 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    173    183       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    184    202       Helical; Name=S3 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    203    208       Extracellular. {ECO:0000305}.
FT   TRANSMEM    209    228       Helical; Voltage-sensor; Name=S4 of
FT                                repeat I. {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    229    244       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    245    265       Helical; Name=S5 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
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:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    396    687       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    688    708       Helical; Name=S1 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    709    718       Extracellular. {ECO:0000305}.
FT   TRANSMEM    719    743       Helical; Name=S2 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    744    749       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    750    769       Helical; Name=S3 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
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|UniProtKB:D0E0C2}.
FT   TOPO_DOM    833    852       Extracellular. {ECO:0000305}.
FT   INTRAMEM    853    873       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    874    889       Extracellular. {ECO:0000305}.
FT   TRANSMEM    890    910       Helical; Name=S6 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    911   1742       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1743   1763       Helical; Name=S1 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1764   1789       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1790   1810       Helical; Name=S2 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1811   1813       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1814   1834       Helical; Name=S3 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1835   1839       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1840   1861       Helical; Voltage-sensor; Name=S4 of
FT                                repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1862   1880       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1881   1902       Helical; Name=S5 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1903   1943       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1944   1965       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1966   1981       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1982   2002       Helical; Name=S6 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   2003   2069       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   2070   2090       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   2091   2095       Extracellular. {ECO:0000305}.
FT   TRANSMEM   2096   2116       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   2117   2132       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   2133   2153       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   2154   2162       Extracellular. {ECO:0000305}.
FT   TRANSMEM   2163   2184       Helical; Voltage-sensor; Name=S4 of
FT                                repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   2185   2199       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   2200   2220       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   2221   2236       Extracellular. {ECO:0000305}.
FT   INTRAMEM   2237   2259       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   2260   2288       Extracellular. {ECO:0000305}.
FT   TRANSMEM   2289   2309       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   2310   2844       Cytoplasmic. {ECO:0000305}.
FT   REPEAT      107    434       I. {ECO:0000305}.
FT   REPEAT      668   1130       II. {ECO:0000305}.
FT   REPEAT     1723   2040       III. {ECO:0000305}.
FT   REPEAT     2050   2311       IV. {ECO:0000305}.
FT   DOMAIN     2441   2470       IQ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00116}.
FT   CARBOHYD    282    282       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    293    293       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    311    311       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1778   1778       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1789   1789       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD   1930   1930       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   DISULFID    272    318       {ECO:0000250|UniProtKB:D0E0C2}.
FT   DISULFID    875    887       {ECO:0000250|UniProtKB:D0E0C2}.
FT   VAR_SEQ    2339   2407       DPHATQFIHFSQLSDFIASLDPPLGISKPNNVALVSFNLPI
FT                                SKGNKIHCLDILHALVKHVLGHVEETDN -> VFSSDSRPS
FT                                RRISPKAARQTIQRTLLTIPSDLLADTIHMPPNLYTSRNCP
FT                                ILLPLSIHHWASRSPIMSL (in isoform P).
FT                                /FTId=VSP_059322.
FT   VAR_SEQ    2408   2844       Missing (in isoform P).
FT                                /FTId=VSP_059323.
FT   VARIANT    2025   2025       M -> V (in RNA edited version).
FT                                {ECO:0000269|PubMed:12907802,
FT                                ECO:0000269|Ref.1}.
FT   CONFLICT      2      2       S -> G (in Ref. 1; 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. 1; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT    195    196       SG -> MR (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. 1; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT    487    487       H -> D (in Ref. 1; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT    535    535       N -> T (in Ref. 1; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT    601    601       Q -> R (in Ref. 1; 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. 1; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT    813    813       T -> R (in Ref. 4; CAA32568).
FT                                {ECO:0000305}.
FT   CONFLICT   1052   1052       P -> A (in Ref. 1; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT   1114   1114       R -> C (in Ref. 1; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT   1125   1125       L -> LRL (in Ref. 1; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT   1672   1672       Y -> C (in Ref. 1; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT   1736   1737       HW -> AL (in Ref. 4; CAA32569).
FT                                {ECO:0000305}.
FT   CONFLICT   1780   1780       T -> A (in Ref. 1; ABF70206).
FT                                {ECO:0000305}.
FT   CONFLICT   1960   1960       M -> N (in Ref. 4; CAA32569).
FT                                {ECO:0000305}.
FT   CONFLICT   1977   1977       Q -> R (in Ref. 4; CAA32569).
FT                                {ECO:0000305}.
FT   CONFLICT   2015   2016       KK -> RR (in Ref. 4; CAA32569).
FT                                {ECO:0000305}.
FT   CONFLICT   2018   2018       Y -> I (in Ref. 4; CAA32570).
FT                                {ECO:0000305}.
FT   CONFLICT   2133   2134       VF -> SV (in Ref. 4; CAA32571).
FT                                {ECO:0000305}.
FT   CONFLICT   2246   2246       R -> Q (in Ref. 4; CAA32571).
FT                                {ECO:0000305}.
FT   CONFLICT   2261   2263       Missing (in Ref. 5; CAA59129).
FT                                {ECO:0000305}.
FT   CONFLICT   2279   2279       C -> S (in Ref. 4; CAA32571).
FT                                {ECO:0000305}.
FT   CONFLICT   2391   2392       LH -> FD (in Ref. 4; CAA32571).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2844 AA;  321257 MW;  2D329637EE0C6777 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
     MVLNLFLALL LNSFNSEELK SKKEEVGEES KLARSIERVR DLIRKKRQER KDRKERKFAE
     KFQQIVLDAQ QAHAQTLSHQ AAVGLERGDK PGVLAETKFH RLSYQESMNR PVSGSDFGFQ
     IPLHDGLHTI VDGLEYDDTG DLPEQIQLQA HPLPPTSDSM PPTYESAMMA TTGGSFSSVN
     GNGTCQNLTP FVQAERRLQH QISSGVSTQQ YDSREEATYT ESIELLGQYN STDTDPYAND
     QRSGCGSFNR GDSLQDNSSR RYGSEEHDEA FLKYQKSLLT RSPSYRKSLD RLSQSSGQSQ
     RSLLKSEEAE MRRHSSGQSL NSMSIEQDEL LSQQGNLREE LLNCDQKELF QFLQEEEELQ
     KGTKLRRISN VMRSRRPSSQ MGQPENETMV EHSEFDNIIQ SFEKELEEIK RSTTSLERKL
     SNLSEPSPAA DEATKAIMEH IAIITGASER SAADEVVLPL NPYDSYDLSS VPRRSQSVSA
     AAQRQSVKLK RRSLEKQRKI DEDFSISNEI RKICDQIHAP FVAMEAMAVA ATSASQAQPN
     QSPFLRRKVD PFTVQFDRFK RLSLIERVEE VPEEEKPIST LRIESEKMPR KFLHGPDQLR
     LDSLSLKSTN SYENLLIQKQ KLGMATPPAV PATPPTSLKS SIEPPTLAQI SSLKTTPPLA
     ALTEHQQHFH ATSIQAAPTP AHTHAHSQAH AHSMAGQRRR MEHPQSTLDK AASFQSARTE
     SHSSGAADAS SALALAMAQK TEQSQSTAPD ATQKPSAFTR LTEKPWHCLV SYVDDLTVGG
     RRNSQGAYND PMTFPSYGAT KAAKVPDDCF PQKCYDHFYF RCPWFMSCMD TQSAKHWTRV
     RTAVLTVVDT PAFEWFVLVL IFASSITLCF EDINLDKNKT LKRVLYWINF SFCLIFVVEM
     ILKWLALGFS KYFTSFWTIL DFIIVFVSVF SLLIEENENL KVLRSLRTLR ALRPLRAISR
     WQGMRIVVNA LMYAIPSIFN VLLVCLVFWL IFSIMGVQFF GGKFFKCVNE MGELLPITEV
     NDKWDCIEQN YTWINSKITF DHVGMGYLAL LQVATFEGWM EVMADAVDAR GVDLQPQREA
     NLYAYIYFVI FIVCGSFFTL NLFIGVIIDN FNMLKKKYEG GVLEMFLTES QKHYYTAMKK
     LGRKKPQKVI KRPINHFLAM FYDLSNSRRF EIAIFVLIFL NMLTMGIEHY DQPHAVFFIL
     EVSNAFFTTV FGLEAIVKIV GLRYHYFTVP WNVFDFLLVL ASIFGILMED IMIDLPISPT
     LLRVVRVFRI GRILRLIKAA KGIRKLLFAL VVSLPALFNI GALLGLITFI YAILGMSLFG
     NVKLQGALDD MVNFQTFGRS MQLLFRLMTS AGWNDVLESL MIQPPDCDPF IHGHTNGNCG
     HPLLAITYFT SFIIISYMIV INMYIAIILE NFNQAHQEEE IGIVEDDLEM FYIRWSKYDP
     HATQFIHFSQ LSDFIASLDP PLGISKPNNV ALVSFNLPIS KGNKIHCLDI LHALVKHVLG
     HVEETDNFKQ LQEQMDVKFK KQFPTRKELE IVSSTRIWKR QEKAAKTIQT GWKEYLRRKR
     EKERSNSGDS ATQTSSPGGW QSKLSALNFF HLQVSRRGTA CSSRASSRKS SRASDASDLS
     ELAGPWLNLP LMLVSGADEV VKDIKQQNDE LGKRGSIFVE APRASRRRSF YNFFLRHQDA
     VDDSLTSPSV HRKTAMNNTT NTTSNSASTS GTASSTATAP ATGCGPAATS ASDSDRHQAV
     GGGSAPSRKR ASSFIRKKPP LERGLSAQSA LRVNKNAFVS EASAPEVIVT RPSPEQQTHP
     HSLSLRPDNA TLVHVLVHRE SEEYKEEDES SPSVSGNGNG FGVGLDMLSK QPPPQIRITT
     GSVESSMDTC AMPTVQIMVD SPKDPPRGDF SSAPIDDVGA PIDVNVQGDT SQVFYDYNPE
     KATDDQGNGQ DETAQFESLP DRQR
//
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