GenomeNet

Database: UniProt
Entry: SCNAA_RAT
LinkDB: SCNAA_RAT
Original site: SCNAA_RAT 
ID   SCNAA_RAT               Reviewed;        1956 AA.
AC   Q62968; Q63554; Q6EWG6;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-SEP-2017, entry version 134.
DE   RecName: Full=Sodium channel protein type 10 subunit alpha;
DE   AltName: Full=Peripheral nerve sodium channel 3;
DE            Short=PN3;
DE   AltName: Full=Sensory neuron sodium channel;
DE   AltName: Full=Sodium channel protein type X subunit alpha;
DE   AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.8;
GN   Name=Scn10a; Synonyms=Sns;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION.
RC   TISSUE=Spinal ganglion;
RX   PubMed=8538791; DOI=10.1038/379257a0;
RA   Akopian A.N., Sivilotti L., Wood J.N.;
RT   "A tetrodotoxin-resistant voltage-gated sodium channel expressed by
RT   sensory neurons.";
RL   Nature 379:257-262(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion;
RX   PubMed=8626372; DOI=10.1074/jbc.271.11.5953;
RA   Sangameswaran L., Delgado S.G., Fish L.M., Koch B.D., Jakeman L.B.,
RA   Stewart G.R., Sze P., Hunter J.C., Eglen R.M., Herman R.C.;
RT   "Structure and function of a novel voltage-gated, tetrodotoxin-
RT   resistant sodium channel specific to sensory neurons.";
RL   J. Biol. Chem. 271:5953-5956(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1), AND INTERACTION WITH SCN1B; SCN2B AND
RP   SCN3B.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion;
RX   PubMed=15178439; DOI=10.1016/j.bbrc.2004.05.026;
RA   Vijayaragavan K., Powell A.J., Kinghorn I.J., Chahine M.;
RT   "Role of auxiliary beta1-, beta2-, and beta3-subunits and their
RT   interaction with Na(v)1.8 voltage-gated sodium channel.";
RL   Biochem. Biophys. Res. Commun. 319:531-540(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 963-1097 (ISOFORMS 1 AND 2).
RC   STRAIN=Wistar; TISSUE=Spinal ganglion, and Trigeminal ganglion;
RX   PubMed=15047701; DOI=10.1074/jbc.M401281200;
RA   Kerr N.C.H., Holmes F.E., Wynick D.;
RT   "Novel isoforms of the sodium channels Nav1.8 and Nav1.5 are produced
RT   by a conserved mechanism in mouse and rat.";
RL   J. Biol. Chem. 279:24826-24833(2004).
RN   [5]
RP   INDUCTION.
RX   PubMed=9450690; DOI=10.1016/S0169-328X(97)00239-8;
RA   Oaklander A.L., Belzberg A.J.;
RT   "Unilateral nerve injury down-regulates mRNA for Na+ channel SCN10A
RT   bilaterally in rat dorsal root ganglia.";
RL   Brain Res. Mol. Brain Res. 52:162-165(1997).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11487631;
RA   Benn S.C., Costigan M., Tate S., Fitzgerald M., Woolf C.J.;
RT   "Developmental expression of the TTX-resistant voltage-gated sodium
RT   channels Nav1.8 (SNS) and Nav1.9 (SNS2) in primary sensory neurons.";
RL   J. Neurosci. 21:6077-6085(2001).
RN   [7]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH S100A10.
RX   PubMed=12050667; DOI=10.1038/nature00781;
RA   Okuse K., Malik-Hall M., Baker M.D., Poon W.-Y.L., Kong H., Chao M.V.,
RA   Wood J.N.;
RT   "Annexin II light chain regulates sensory neuron-specific sodium
RT   channel expression.";
RL   Nature 417:653-656(2002).
RN   [8]
RP   INTERACTION WITH FSTL1; PRX; DYNLT1 AND PDZD2, AND IDENTIFICATION IN
RP   COMPLEXES WITH PRX; DYNLT1 AND PDZD2.
RX   PubMed=12591166; DOI=10.1016/S0169-328X(02)00661-7;
RA   Malik-Hall M., Poon W.-Y.L., Baker M.D., Wood J.N., Okuse K.;
RT   "Sensory neuron proteins interact with the intracellular domains of
RT   sodium channel NaV1.8.";
RL   Brain Res. Mol. Brain Res. 110:298-304(2003).
RN   [9]
RP   FUNCTION IN PAIN.
RX   PubMed=12514212;
RA   Gold M.S., Weinreich D., Kim C.-S., Wang R., Treanor J., Porreca F.,
RA   Lai J.;
RT   "Redistribution of Na(V)1.8 in uninjured axons enables neuropathic
RT   pain.";
RL   J. Neurosci. 23:158-166(2003).
CC   -!- FUNCTION: Tetrodotoxin-resistant channel that mediates the
CC       voltage-dependent sodium ion permeability of excitable membranes.
CC       Assuming opened or closed conformations in response to the voltage
CC       difference across the membrane, the protein forms a sodium-
CC       selective channel through which sodium ions may pass in accordance
CC       with their electrochemical gradient. Plays a role in neuropathic
CC       pain mechanisms. {ECO:0000269|PubMed:12514212,
CC       ECO:0000269|PubMed:8538791, ECO:0000269|PubMed:8626372}.
CC   -!- SUBUNIT: The channel consists of an ion conducting pore forming
CC       alpha-subunit regulated by one or more associated auxiliary
CC       subunits SCN1B, SCN2B and SCN3B; electrophysiological properties
CC       may vary depending on the type of the associated beta subunits.
CC       Found in a number of complexes with PRX, DYNLT1 and PDZD2.
CC       Interacts with proteins such as FSTL1, PRX, DYNLT1, PDZD2, S100A10
CC       and many others. Interacts with NEDD4 and NEDD4L.
CC       {ECO:0000269|PubMed:12050667, ECO:0000269|PubMed:12591166,
CC       ECO:0000269|PubMed:15178439}.
CC   -!- INTERACTION:
CC       Q9Z336:Dynlt1; NbExp=2; IntAct=EBI-1800320, EBI-920359;
CC       Q63425:Prx; NbExp=2; IntAct=EBI-1800320, EBI-1800492;
CC       P05943:S100a10; NbExp=4; IntAct=EBI-1800320, EBI-1800351;
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:D0E0C2}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:D0E0C2}. Note=It can be translocated to the
CC       cell membrane through association with S100A10.
CC       {ECO:0000269|PubMed:12050667}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q62968-1; Sequence=Displayed;
CC       Name=2; Synonyms=Nav1.8c;
CC         IsoId=Q62968-2; Sequence=VSP_012258;
CC   -!- TISSUE SPECIFICITY: Expressed in dorsal root ganglia, trigeminal
CC       ganglia, nodose ganglia and sciatic nerve.
CC       {ECO:0000269|PubMed:11487631, ECO:0000269|PubMed:8538791,
CC       ECO:0000269|PubMed:8626372}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in dorsal root ganglia at 15 dpc
CC       onwards. {ECO:0000269|PubMed:11487631}.
CC   -!- INDUCTION: Down-regulated after axotomy in dorsal root ganglia.
CC       {ECO:0000269|PubMed:9450690}.
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: Ubiquitinated by NEDD4L; which promotes its endocytosis.
CC       {ECO:0000250}.
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   -!- PTM: Lacks the cysteine which covalently binds the conotoxin
CC       GVIIJ. This cysteine (position 815) is speculated in other sodium
CC       channel subunits alpha to be implied in covalent binding with the
CC       sodium channel subunit beta-2 or beta-4.
CC       {ECO:0000250|UniProtKB:P15389}.
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.8/SCN10A subfamily. {ECO:0000305}.
DR   EMBL; X92184; CAA63095.1; -; mRNA.
DR   EMBL; U53833; AAC52619.1; -; Genomic_DNA.
DR   EMBL; AJ623271; CAF25041.1; -; mRNA.
DR   PIR; S68453; S68453.
DR   RefSeq; NP_058943.1; NM_017247.1.
DR   UniGene; Rn.10246; -.
DR   ProteinModelPortal; Q62968; -.
DR   CORUM; Q62968; -.
DR   ELM; Q62968; -.
DR   IntAct; Q62968; 23.
DR   STRING; 10116.ENSRNOP00000047944; -.
DR   BindingDB; Q62968; -.
DR   ChEMBL; CHEMBL4017; -.
DR   GuidetoPHARMACOLOGY; 585; -.
DR   TCDB; 1.A.1.10.6; the voltage-gated ion channel (vic) superfamily.
DR   iPTMnet; Q62968; -.
DR   PhosphoSitePlus; Q62968; -.
DR   PaxDb; Q62968; -.
DR   PRIDE; Q62968; -.
DR   Ensembl; ENSRNOT00000046864; ENSRNOP00000047944; ENSRNOG00000032473. [Q62968-1]
DR   GeneID; 29571; -.
DR   KEGG; rno:29571; -.
DR   UCSC; RGD:3629; rat. [Q62968-1]
DR   CTD; 6336; -.
DR   RGD; 3629; Scn10a.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128242; -.
DR   HOGENOM; HOG000231755; -.
DR   HOVERGEN; HBG053100; -.
DR   InParanoid; Q62968; -.
DR   KO; K04842; -.
DR   OMA; WNIFDCI; -.
DR   OrthoDB; EOG091G00FK; -.
DR   PhylomeDB; Q62968; -.
DR   TreeFam; TF323985; -.
DR   PRO; PR:Q62968; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000032473; -.
DR   Genevisible; Q62968; RN.
DR   GO; GO:0071439; C:clathrin complex; IDA:RGD.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:Ensembl.
DR   GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:RGD.
DR   GO; GO:0086016; P:AV node cell action potential; IEA:Ensembl.
DR   GO; GO:0086043; P:bundle of His cell action potential; IEA:Ensembl.
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:0042475; P:odontogenesis of dentin-containing tooth; IEP:RGD.
DR   GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; IEA:Ensembl.
DR   GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:Ensembl.
DR   GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
DR   GO; GO:0006814; P:sodium ion transport; IDA:RGD.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR028809; Na_channel_a10su.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   PANTHER; PTHR10037:SF263; PTHR10037:SF263; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   PRINTS; PR00170; NACHANNEL.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Complete proteome;
KW   Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Phosphoprotein; Reference proteome; Repeat; Sodium; Sodium channel;
KW   Sodium transport; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation; Voltage-gated channel.
FT   CHAIN         1   1956       Sodium channel protein type 10 subunit
FT                                alpha.
FT                                /FTId=PRO_0000048509.
FT   TOPO_DOM      1    125       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    126    149       Helical; Name=S1 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    150    154       Extracellular. {ECO:0000305}.
FT   TRANSMEM    155    174       Helical; Name=S2 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    175    187       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    188    206       Helical; Name=S3 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    207    212       Extracellular. {ECO:0000305}.
FT   TRANSMEM    213    232       Helical; Voltage-sensor; Name=S4 of
FT                                repeat I. {ECO:0000255}.
FT   TOPO_DOM    233    248       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    249    272       Helical; Name=S5 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    273    340       Extracellular. {ECO:0000305}.
FT   INTRAMEM    341    365       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    366    372       Extracellular. {ECO:0000305}.
FT   TRANSMEM    373    398       Helical; Name=S6 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    399    658       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    659    683       Helical; Name=S1 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    684    694       Extracellular. {ECO:0000305}.
FT   TRANSMEM    695    718       Helical; Name=S2 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    719    726       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    727    746       Helical; Name=S3 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    747    752       Extracellular. {ECO:0000305}.
FT   TRANSMEM    753    772       Helical; Voltage-sensor; Name=S4 of
FT                                repeat II. {ECO:0000255}.
FT   TOPO_DOM    773    788       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    789    809       Helical; Name=S5 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    810    833       Extracellular. {ECO:0000305}.
FT   INTRAMEM    834    854       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    855    863       Extracellular. {ECO:0000305}.
FT   TRANSMEM    864    889       Helical; Name=S6 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    890   1148       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1149   1172       Helical; Name=S1 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1173   1185       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1186   1211       Helical; Name=S2 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1212   1217       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1218   1239       Helical; Name=S3 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1240   1243       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1244   1265       Helical; Voltage-sensor; Name=S4 of
FT                                repeat III. {ECO:0000255}.
FT   TOPO_DOM   1266   1284       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1285   1312       Helical; Name=S5 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1313   1354       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1355   1376       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1377   1392       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1393   1419       Helical; Name=S6 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1420   1472       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1473   1496       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1497   1507       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1508   1531       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1532   1537       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1538   1561       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1562   1573       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1574   1595       Helical; Voltage-sensor; Name=S4 of
FT                                repeat IV. {ECO:0000255}.
FT   TOPO_DOM   1596   1610       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1611   1633       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1634   1647       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1648   1670       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1671   1698       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1699   1723       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1724   1956       Cytoplasmic. {ECO:0000305}.
FT   REPEAT      116    404       I. {ECO:0000305}.
FT   REPEAT      646    910       II. {ECO:0000305}.
FT   REPEAT     1141   1450       III. {ECO:0000305}.
FT   REPEAT     1459   1758       IV. {ECO:0000305}.
FT   DOMAIN     1852   1881       IQ.
FT   MOD_RES     440    440       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14524}.
FT   MOD_RES     443    443       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14524}.
FT   MOD_RES     466    466       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14524}.
FT   MOD_RES     478    478       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14524}.
FT   MOD_RES     611    611       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14524}.
FT   MOD_RES     614    614       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14524}.
FT   MOD_RES    1452   1452       Phosphoserine; by PKC. {ECO:0000250}.
FT   CARBOHYD    279    279       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    288    288       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    311    311       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    334    334       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1323   1323       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1329   1329       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1337   1337       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1687   1687       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    276    318       {ECO:0000250|UniProtKB:D0E0C2}.
FT   DISULFID    856    865       {ECO:0000250|UniProtKB:D0E0C2}.
FT   VAR_SEQ    1030   1030       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15047701}.
FT                                /FTId=VSP_012258.
FT   CONFLICT     59     59       A -> D (in Ref. 1; CAA63095).
FT                                {ECO:0000305}.
FT   CONFLICT    432    432       A -> E (in Ref. 1; CAA63095).
FT                                {ECO:0000305}.
FT   CONFLICT    520    520       T -> TP (in Ref. 1; CAA63095).
FT                                {ECO:0000305}.
FT   CONFLICT    587    587       D -> H (in Ref. 1; CAA63095).
FT                                {ECO:0000305}.
FT   CONFLICT    757    757       F -> L (in Ref. 1; CAA63095).
FT                                {ECO:0000305}.
FT   CONFLICT    938    938       R -> H (in Ref. 1; CAA63095).
FT                                {ECO:0000305}.
FT   CONFLICT   1896   1896       V -> I (in Ref. 1; CAA63095).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1956 AA;  219733 MW;  8FC58EDAD263AC67 CRC64;
     MELPFASVGT TNFRRFTPES LAEIEKQIAA HRAAKKARTK HRGQEDKGEK PRPQLDLKAC
     NQLPKFYGEL PAELVGEPLE DLDPFYSTHR TFMVLNKSRT ISRFSATWAL WLFSPFNLIR
     RTAIKVSVHS WFSIFITITI LVNCVCMTRT DLPEKVEYVF TVIYTFEALI KILARGFCLN
     EFTYLRDPWN WLDFSVITLA YVGAAIDLRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI
     HSVRKLADVT ILTVFCLSVF ALVGLQLFKG NLKNKCIRNG TDPHKADNLS SEMAEYIFIK
     PGTTDPLLCG NGSDAGHCPG GYVCLKTPDN PDFNYTSFDS FAWAFLSLFR LMTQDSWERL
     YQQTLRASGK MYMVFFVLVI FLGSFYLVNL ILAVVTMAYE EQSQATIAEI EAKEKKFQEA
     LEVLQKEQEV LAALGIDTTS LQSHSGSPLA SKNANERRPR VKSRVSEGST DDNRSPQSDP
     YNQRRMSFLG LSSGRRRASH GSVFHFRAPS QDISFPDGIT DDGVFHGDQE SRRGSILLGR
     GAGQTGPLPR SPLPQSPNPG RRHGEEGQLG VPTGELTAGA PEGPALDTTG QKSFLSAGYL
     NEPFRAQRAM SVVSIMTSVI EELEESKLKC PPCLISFAQK YLIWECCPKW RKFKMALFEL
     VTDPFAELTI TLCIVVNTVF MAMEHYPMTD AFDAMLQAGN IVFTVFFTME MAFKIIAFDP
     YYYFQKKWNI FDCVIVTVSL LELSASKKGS LSVLRTFRLL RVFKLAKSWP TLNTLIKIIG
     NSVGALGNLT FILAIIVFIF ALVGKQLLSE DYGCRKDGVS VWNGEKLRWH MCDFFHSFLV
     VFRILCGEWI ENMWVCMEVS QKSICLILFL TVMVLGNLVV LNLFIALLLN SFSADNLTAP
     EDDGEVNNLQ LALARIQVLG HRASRAIASY ISSHCRFRWP KVETQLGMKP PLTSSEAKNH
     IATDAVSAAV GNLTKPALSS PKENHGDFIT DPNVWVSVPI AEGESDLDEL EEDMEQASQS
     SWQEEDPKGQ QEQLPQVQKC ENHQAARSPA SMMSSEDLAP YLGESWKRKD SPQVPAEGVD
     DTSSSEGSTV DCPDPEEILR KIPELADDLD EPDDCFTEGC TRRCPCCNVN TSKSPWATGW
     QVRKTCYRIV EHSWFESFII FMILLSSGAL AFEDNYLEEK PRVKSVLEYT DRVFTFIFVF
     EMLLKWVAYG FKKYFTNAWC WLDFLIVNIS LTSLIAKILE YSDVASIKAL RTLRALRPLR
     ALSRFEGMRV VVDALVGAIP SIMNVLLVCL IFWLIFSIMG VNLFAGKFSK CVDTRNNPFS
     NVNSTMVNNK SECHNQNSTG HFFWVNVKVN FDNVAMGYLA LLQVATFKGW MDIMYAAVDS
     GEINSQPNWE NNLYMYLYFV VFIIFGGFFT LNLFVGVIID NFNQQKKKLG GQDIFMTEEQ
     KKYYNAMKKL GSKKPQKPIP RPLNKYQGFV FDIVTRQAFD IIIMVLICLN MITMMVETDE
     QGEEKTKVLG RINQFFVAVF TGECVMKMFA LRQYYFTNGW NVFDFIVVIL SIGSLLFSAI
     LKSLENYFSP TLFRVIRLAR IGRILRLIRA AKGIRTLLFA LMMSLPALFN IGLLLFLVMF
     IYSIFGMASF ANVVDEAGID DMFNFKTFGN SMLCLFQITT SAGWDGLLSP ILNTGPPYCD
     PNLPNSNGSR GNCGSPAVGI IFFTTYIIIS FLIVVNMYIA VILENFNVAT EESTEPLSED
     DFDMFYETWE KFDPEATQFI AFSALSDFAD TLSGPLRIPK PNQNILIQMD LPLVPGDKIH
     CLDILFAFTK NVLGESGELD SLKTNMEEKF MATNLSKASY EPIATTLRWK QEDLSATVIQ
     KAYRSYMLHR SLTLSNTLHV PRAEEDGVSL PGEGYVTFMA NSGLPDKSET ASATSFPPSY
     DSVTRGLSDR ANINPSSSMQ NEDEVAAKEG NSPGPQ
//
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