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Database: UniProt
Entry: SCN3A_RAT
LinkDB: SCN3A_RAT
Original site: SCN3A_RAT 
ID   SCN3A_RAT               Reviewed;        1951 AA.
AC   P08104;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   18-JUL-2018, entry version 159.
DE   RecName: Full=Sodium channel protein type 3 subunit alpha;
DE   AltName: Full=Sodium channel protein brain III subunit alpha;
DE   AltName: Full=Sodium channel protein type III subunit alpha;
DE   AltName: Full=Voltage-gated sodium channel subtype III;
DE   AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.3;
GN   Name=Scn3a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
RX   PubMed=2449363; DOI=10.1016/0014-5793(88)80614-8;
RA   Kayano T., Noda M., Flockerzi V., Takahashi H., Numa S.;
RT   "Primary structure of rat brain sodium channel III deduced from the
RT   cDNA sequence.";
RL   FEBS Lett. 228:187-194(1988).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484; SER-485 AND
RP   SER-486, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3]
RP   SUBUNIT, AND INTERACTION WITH THE CONOTOXIN GVIIJ.
RX   PubMed=24497506; DOI=10.1073/pnas.1324189111;
RA   Gajewiak J., Azam L., Imperial J., Walewska A., Green B.R.,
RA   Bandyopadhyay P.K., Raghuraman S., Ueberheide B., Bern M., Zhou H.M.,
RA   Minassian N.A., Hagan R.H., Flinspach M., Liu Y., Bulaj G.,
RA   Wickenden A.D., Olivera B.M., Yoshikami D., Zhang M.M.;
RT   "A disulfide tether stabilizes the block of sodium channels by the
RT   conotoxin muO[section sign]-GVIIJ.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:2758-2763(2014).
RN   [4]
RP   SUBUNIT, INTERACTION WITH THE SPIDER RTX-VII TOXIN, AND MUTAGENESIS OF
RP   LYS-1503; TYR-1504; MET-1505; THR-1506; LEU-1507 AND GLU-1562.
RX   PubMed=25784299; DOI=10.1038/srep09241;
RA   Tang C., Zhou X., Zhang Y., Xiao Z., Hu Z., Zhang C., Huang Y.,
RA   Chen B., Liu Z., Liang S.;
RT   "Synergetic action of domain II and IV underlies persistent current
RT   generation in Nav1.3 as revealed by a tarantula toxin.";
RL   Sci. Rep. 5:9241-9241(2015).
RN   [5]
RP   SUBUNIT, INTERACTION WITH THE SPIDER BETA/DELTA-THERAPHOTOXIN-PRE1A,
RP   AND SITE SER-1510.
RX   PubMed=28428547; DOI=10.1038/s41598-017-01129-0;
RA   Wingerd J.S., Mozar C.A., Ussing C.A., Murali S.S., Chin Y.K.,
RA   Cristofori-Armstrong B., Durek T., Gilchrist J., Vaughan C.W.,
RA   Bosmans F., Adams D.J., Lewis R.J., Alewood P.F., Mobli M.,
RA   Christie M.J., Rash L.D.;
RT   "The tarantula toxin beta/delta-TRTX-Pre1a highlights the importance
RT   of the S1-S2 voltage-sensor region for sodium channel subtype
RT   selectivity.";
RL   Sci. Rep. 7:974-988(2017).
CC   -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability
CC       of excitable membranes. Assuming opened or closed conformations in
CC       response to the voltage difference across the membrane, forms a
CC       sodium-selective channel through which Na(+) ions may pass in
CC       accordance with their electrochemical gradient (By similarity).
CC       May contribute to the regulation of serotonin/5-hydroxytryptamine
CC       release by enterochromaffin cells (By similarity). In pancreatic
CC       endocrine cells, required for both glucagon and glucose-induced
CC       insulin secretion (By similarity). {ECO:0000250|UniProtKB:A2ASI5,
CC       ECO:0000250|UniProtKB:Q9NY46}.
CC   -!- SUBUNIT: Heterooligomer of a large alpha subunit and 2-3 smaller
CC       beta subunits. Heterooligomer with SCN2B or SCN4B; disulfide-
CC       linked. Interacts with NEDD4L (By similarity). Interacts with the
CC       conotoxin GVIIJ (PubMed:24497506). Interacts with the spider
CC       beta/delta-theraphotoxin-Pre1a (PubMed:25784299, PubMed:28428547).
CC       Interacts with the spider RTX-VII toxin (AC P0DL75)
CC       (PubMed:25784299). {ECO:0000250|UniProtKB:Q9NY46,
CC       ECO:0000269|PubMed:24497506, ECO:0000269|PubMed:25784299,
CC       ECO:0000269|PubMed:28428547}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:Q9NY46}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:D0E0C2}.
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   -!- PTM: May be ubiquitinated by NEDD4L; which would promote its
CC       endocytosis. {ECO:0000250|UniProtKB:Q9NY46}.
CC   -!- PTM: Phosphorylation at Ser-1452 by PKC in a highly conserved
CC       cytoplasmic loop slows inactivation of the sodium channel and
CC       reduces peak sodium currents. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.3/SCN3A subfamily. {ECO:0000305}.
DR   EMBL; Y00766; CAA68735.1; -; mRNA.
DR   PIR; S00320; S00320.
DR   RefSeq; NP_037251.1; NM_013119.1.
DR   UniGene; Rn.87394; -.
DR   PDB; 1QG9; NMR; -; A=156-176.
DR   PDBsum; 1QG9; -.
DR   ProteinModelPortal; P08104; -.
DR   SMR; P08104; -.
DR   BioGrid; 269080; 2.
DR   STRING; 10116.ENSRNOP00000006646; -.
DR   BindingDB; P08104; -.
DR   ChEMBL; CHEMBL4966; -.
DR   GuidetoPHARMACOLOGY; 580; -.
DR   TCDB; 1.A.1.10.1; the voltage-gated ion channel (vic) superfamily.
DR   iPTMnet; P08104; -.
DR   PhosphoSitePlus; P08104; -.
DR   SwissPalm; P08104; -.
DR   PaxDb; P08104; -.
DR   PRIDE; P08104; -.
DR   GeneID; 497770; -.
DR   KEGG; rno:497770; -.
DR   CTD; 6328; -.
DR   RGD; 3635; Scn3a.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   HOVERGEN; HBG053100; -.
DR   InParanoid; P08104; -.
DR   KO; K04836; -.
DR   PhylomeDB; P08104; -.
DR   EvolutionaryTrace; P08104; -.
DR   PRO; PR:P08104; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IDA:RGD.
DR   GO; GO:0005516; F:calmodulin binding; IDA:RGD.
DR   GO; GO:0031402; F:sodium ion binding; IDA:RGD.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:RGD.
DR   GO; GO:0071236; P:cellular response to antibiotic; IDA:RGD.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   GO; GO:0007399; P:nervous system development; IEP:RGD.
DR   GO; GO:0019228; P:neuronal action potential; IDA:RGD.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0046684; P:response to pyrethroid; IDA:RGD.
DR   GO; GO:0009611; P:response to wounding; IEP:RGD.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
DR   Gene3D; 1.20.120.350; -; 4.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   InterPro; IPR024583; Na_trans_cytopl.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   Pfam; PF11933; Na_trans_cytopl; 1.
DR   PRINTS; PR00170; NACHANNEL.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Complete proteome; Disulfide bond;
KW   Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Sodium; Sodium channel; Sodium transport;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
KW   Voltage-gated channel.
FT   CHAIN         1   1951       Sodium channel protein type 3 subunit
FT                                alpha.
FT                                /FTId=PRO_0000048494.
FT   TOPO_DOM      1    128       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    129    147       Helical; Name=S1 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    148    154       Extracellular. {ECO:0000305}.
FT   TRANSMEM    155    175       Helical; Name=S2 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    176    189       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    190    207       Helical; Name=S3 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    208    213       Extracellular. {ECO:0000305}.
FT   TRANSMEM    214    230       Helical; Name=S4 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    231    249       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    250    269       Helical; Name=S5 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    270    368       Extracellular. {ECO:0000305}.
FT   INTRAMEM    369    393       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    394    400       Extracellular. {ECO:0000305}.
FT   TRANSMEM    401    421       Helical; Name=S6 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    422    711       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    712    730       Helical; Name=S1 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    731    741       Extracellular. {ECO:0000305}.
FT   TRANSMEM    742    761       Helical; Name=S2 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    762    775       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    776    795       Helical; Name=S3 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    796    797       Extracellular. {ECO:0000305}.
FT   TRANSMEM    798    815       Helical; Name=S4 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    816    831       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    832    850       Helical; Name=S5 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    851    879       Extracellular. {ECO:0000305}.
FT   INTRAMEM    880    900       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    901    913       Extracellular. {ECO:0000305}.
FT   TRANSMEM    914    934       Helical; Name=S6 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    935   1158       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1159   1176       Helical; Name=S1 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1177   1189       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1190   1208       Helical; Name=S2 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1209   1222       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1223   1241       Helical; Name=S3 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1242   1249       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1250   1268       Helical; Name=S4 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1269   1285       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1286   1305       Helical; Name=S5 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1306   1354       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1355   1376       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1377   1393       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1394   1415       Helical; Name=S6 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1416   1478       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1479   1496       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1497   1507       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1508   1526       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1527   1538       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1539   1556       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1557   1569       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1570   1586       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1587   1605       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1606   1623       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1624   1645       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1646   1668       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1669   1698       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1699   1721       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1722   1951       Cytoplasmic. {ECO:0000305}.
FT   REPEAT      110    455       I. {ECO:0000305}.
FT   REPEAT      693    965       II. {ECO:0000305}.
FT   REPEAT     1139   1450       III. {ECO:0000305}.
FT   REPEAT     1459   1757       IV. {ECO:0000305}.
FT   DOMAIN     1851   1880       IQ.
FT   SITE       1503   1503       Important residue that permits the spider
FT                                RTX-VII toxin to inhibit fast
FT                                inactivation of the channel.
FT                                {ECO:0000269|PubMed:25784299}.
FT   SITE       1506   1506       Important residue that permits the spider
FT                                RTX-VII toxin to inhibit fast
FT                                inactivation of the channel.
FT                                {ECO:0000269|PubMed:25784299}.
FT   SITE       1507   1507       Important residue that permits the spider
FT                                RTX-VII toxin to inhibit fast
FT                                inactivation of the channel.
FT                                {ECO:0000269|PubMed:25784299}.
FT   SITE       1510   1510       Key residue that permits the spider
FT                                beta/delta-theraphotoxin-Pre1a to inhibit
FT                                fast inactivation of the channel.
FT                                {ECO:0000269|PubMed:28428547}.
FT   SITE       1562   1562       Important residue that permits the spider
FT                                RTX-VII toxin to inhibit fast
FT                                inactivation of the channel.
FT                                {ECO:0000269|PubMed:25784299}.
FT   MOD_RES     484    484       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     485    485       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     486    486       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    1452   1452       Phosphoserine; by PKC.
FT                                {ECO:0000250|UniProtKB:Q14524}.
FT   CARBOHYD    211    211       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    290    290       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    296    296       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    302    302       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    307    307       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    339    339       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1317   1317       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1331   1331       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    277    346       {ECO:0000250|UniProtKB:D0E0C2}.
FT   DISULFID    862    862       Interchain; with SCN2B or SCN4B.
FT                                {ECO:0000250|UniProtKB:P04775}.
FT   DISULFID    862    862       Interchain; with the conotoxin GVIIJ
FT                                (when the channel is not linked to SCN2B
FT                                or SCN4B; the bond to SCN2B or SCN4B
FT                                protects the channel from the inhibition
FT                                by toxin).
FT                                {ECO:0000250|UniProtKB:P04775}.
FT   DISULFID    902    911       {ECO:0000250|UniProtKB:D0E0C2}.
FT   MUTAGEN    1503   1503       K->P: 6-fold decrease in activity of the
FT                                spider RTX-VII toxin.
FT                                {ECO:0000269|PubMed:25784299}.
FT   MUTAGEN    1504   1504       Y->E: 2-fold decrease in activity of the
FT                                spider RTX-VII toxin.
FT                                {ECO:0000269|PubMed:25784299}.
FT   MUTAGEN    1505   1505       M->K: 4.5-fold decrease in activity of
FT                                the spider RTX-VII toxin.
FT                                {ECO:0000269|PubMed:25784299}.
FT   MUTAGEN    1506   1506       T->I: 10-fold decrease in activity of the
FT                                spider RTX-VII toxin.
FT                                {ECO:0000269|PubMed:25784299}.
FT   MUTAGEN    1507   1507       L->N: 12-fold decrease in activity of the
FT                                spider RTX-VII toxin.
FT                                {ECO:0000269|PubMed:25784299}.
FT   MUTAGEN    1562   1562       E->Q: 5.5-fold decrease in activity of
FT                                the spider RTX-VII toxin.
FT                                {ECO:0000269|PubMed:25784299}.
FT   MUTAGEN    1562   1562       E->R: 20-fold decrease in activity of the
FT                                spider RTX-VII toxin.
FT                                {ECO:0000269|PubMed:25784299}.
FT   HELIX       161    174       {ECO:0000244|PDB:1QG9}.
SQ   SEQUENCE   1951 AA;  221387 MW;  74E5E851524BD10E CRC64;
     MAQALLVPPG PESFRLFTRE SLAAIEKRAA EEKAKKPKKE QDIDDENKPK PNSDLEAGKN
     LPFIYGDIPP EMVSEPLEDL DPYYVSKKTF VVLNKGKAIF RFSATSALYI LTPLNPVRKI
     AIKILVHSLF SMLIMCTILT NCVFMTLSNP PDWTKNVEYT FTGIYTFESL IKILARGFCL
     EDFTFLRDPW NWLDFSVIVM AYVTEFVDLG NVSALRTFRV LRALKTISVI PGLKTIVGAL
     IQSVKKLSDV MILTVFCLSV FALIGLQLFM GNLRNKCSQW PPSDSAFETN TTSYFNGTMD
     SNGTFVNVTM STFNWKDYIA DDSHFYVLDG QKDPLLCGNG SDAGQCPEGY ICVKAGRNPN
     YGYTSFDTFS WAFLSLFRLM TQDYWENLYQ LTLRAAGKTY MIFFVLVIFL GSFYLVNLIL
     AVVAMAYEEQ NQATLEEAEQ KEAEFQQMLE QLKKQQEEAQ AVAAASAASR DFSGIGGLGE
     LLESSSEASK LSSKSAKEWR NRRKKRRQRE HLEGNHRADG DRFPKSESED SVKRRSFLLS
     LDGNPLTGDK KLCSPHQSLL SIRGSLFSPR RNSKTSIFSF RGRAKDVGSE NDFADDEHST
     FEDSESRRDS LFVPHRPGER RNSNGTTTET EVRKRRLSSY QISMEMLEDS SGRQRSMSIA
     SILTNTMEEL EESRQKCPPC WYRFANVFLI WDCCDAWLKV KHLVNLIVMD PFVDLAITIC
     IVLNTLFMAM EHYPMTQQFS SVLTVGNLVF TGIFTAEMVL KIIAMDPYYY FQEGWNIFDG
     IIVSLSLMEL GLANVEGLSV LRSFRLLRVF KLAKSWPTLN MLIKIIGNSV GALGNLTLVL
     AIIVFIFAVV GMQLFGKSYK ECVCKINVDC KLPRWHMNDF FHSFLIVFRV LCGEWIETMW
     DCMEVAGQTM CLIVFMLVMV IGNLVVLNLF LALLLSSFSS DNLAATDDDN EMNNLQIAVG
     RMQKGIDFVK NKIRECFRKA FFRKPKVIEI QEGNKIDSCM SNNTGIEISK ELNYLKDGNG
     TTSGVGTGSS VEKYVIDEND YMSFINNPSL TVTVPIAVGE SDFENLNTEE FSSESELEES
     KEKLNATSSS EGSTVDVAPP REGEQAEIEP EEDLKPEACF TEGCIKKFPF CQVSTEEGKG
     KIWWNLRKTC YSIVEHNWFE TFIVFMILLS SGALAFEDIY IEQRKTIKTM LEYADKVFTY
     IFILEMLLKW VAYGFQTYFT NAWCWLDFLI VDVSLVSLVA NALGYSELGA IKSLRTLRAL
     RPLRALSRFE GMRVVVNALV GAIPSIMNVL LVCLIFWLIF SIMGVNLFAG KFYHCVNTTT
     GNMFEIKEVN NFSDCQALGK QARWKNVKVN FDNVGAGYLA LLQVATFKGW MDIMYAAVDS
     RDVKLQPIYE ENLYMYLYFV IFIIFGSFFT LNLFIGVIID NFNQQKKKFG GQDIFMTEEQ
     KKYYNAMKKL GSKKPQKPIP RPANKFQGMV FDFVTRQVFD ISIMILICLN MVTMMVETDD
     QSKYMTLVLS RINLVFIVLF TGEFLLKLIS LRYYYFTIGW NIFDFVVVIL SIVGMFLAEL
     IEKYFVSPTL FRVIRLARIG RILRLIKGAK GIRTLLFALM MSLPALFNIG LLLFLVMFIY
     AIFGMSNFAY VKKEAGIDDM FNFETFGNSM ICLFQITTSA GWDGLLAPIL NSAPPDCDPD
     AIHPGSSVKG DCGNPSVGIF FFVSYIIISF LVVVNMYIAV ILENFSVATE ESAEPLSEDD
     FEMFYEVWEK FDPDATQFIE FCKLSDFAAA LDPPLLIAKP NKVQLIAMDL PMVSGDRIHC
     LDILFAFTKR VLGESGEMDA LRIQMEDRFM ASNPSKVSYE PITTTLKRKQ EEVSAAIIQR
     NYRCYLLKQR LKNISSKYDK ETIKGRIDLP IKGDMVIDKL NGNSTPEKTD GSSSTTSPPS
     YDSVTKPDKE KFEKDKPEKE IKGKEVRENQ K
//
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