SCN1A_RAT
ID SCN1A_RAT Reviewed; 2009 AA.
AC P04774;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 171.
DE RecName: Full=Sodium channel protein type 1 subunit alpha;
DE AltName: Full=Sodium channel protein brain I subunit alpha;
DE AltName: Full=Sodium channel protein type I subunit alpha;
DE AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.1;
GN Name=Scn1a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3754035; DOI=10.1038/320188a0;
RA Noda M., Ikeda T., Kayano T., Suzuki H., Takeshima H., Kurasaki M.,
RA Takahashi H., Numa S.;
RT "Existence of distinct sodium channel messenger RNAs in rat brain.";
RL Nature 320:188-192(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2442385; DOI=10.3109/10799898709054998;
RA Noda M., Numa S.;
RT "Structure and function of sodium channel.";
RL J. Recept. Res. 7:467-497(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 177-253.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=1658739; DOI=10.1093/nar/19.20.5673;
RA Sarao R., Gupta S.K., Auld V.J., Dunn R.J.;
RT "Developmentally regulated alternative RNA splicing of rat brain sodium
RT channel mRNAs.";
RL Nucleic Acids Res. 19:5673-5679(1991).
RN [4]
RP PHOSPHORYLATION AT SER-470; SER-551 AND SER-607.
RX PubMed=20131913; DOI=10.1021/pr901171q;
RA Berendt F.J., Park K.S., Trimmer J.S.;
RT "Multisite phosphorylation of voltage-gated sodium channel alpha subunits
RT from rat brain.";
RL J. Proteome Res. 9:1976-1984(2010).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; SER-525; SER-550;
RP SER-551 AND SER-730, 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., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP 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., Wickenden A.D.,
RA 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).
CC -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, the protein
CC forms a sodium-selective channel through which Na(+) ions may pass in
CC accordance with their electrochemical gradient. Plays a key role in
CC brain, probably by regulating the moment when neurotransmitters are
CC released in neurons. Involved in sensory perception of mechanical pain:
CC activation in somatosensory neurons induces pain without neurogenic
CC inflammation and produces hypersensitivity to mechanical, but not
CC thermal stimuli. {ECO:0000250|UniProtKB:A2APX8}.
CC -!- ACTIVITY REGULATION: Inactivation of this channel is specifically
CC inhibited by the spider toxins Hm1a and Hm1b (H.maculata, AC P60992 and
CC AC P0DOC5) in somatosensory neurons to elicit acute pain and mechanical
CC allodynia. {ECO:0000250|UniProtKB:A2APX8}.
CC -!- SUBUNIT: The voltage-sensitive sodium channel consists of an ion
CC conducting pore forming alpha-subunit regulated by one or more beta-1
CC (SCN1B), beta-2 (SCN2B), beta-3 (SCN3B) and/or beta-4 (SCN4B). Beta-1
CC (SCN1B) and beta-3 (SCN3B) are non-covalently associated with alpha,
CC while beta-2 (SCN2B) and beta-4 (SCN4B) are covalently linked by
CC disulfide bonds. Interacts with FGF13. Interacts with the conotoxin
CC GVIIJ (PubMed:24497506). {ECO:0000250|UniProtKB:P04775,
CC ECO:0000250|UniProtKB:P35498, ECO:0000269|PubMed:24497506}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35498};
CC Multi-pass membrane protein {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 charged
CC segment (S4). Segments S4 are probably the voltage-sensors and are
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000305}.
CC -!- DOMAIN: The S3b-S4 and S1-S2 loops of repeat IV are targeted by
CC H.maculata toxins Hm1a and Hm1b, leading to inhibit fast inactivation
CC of Nav1.1/SCN1A. Selectivity for H.maculata toxins Hm1a and Hm1b
CC depends on S1-S2 loops of repeat IV. {ECO:0000250|UniProtKB:A2APX8}.
CC -!- PTM: Phosphorylation at Ser-1516 by PKC in a highly conserved
CC cytoplasmic loop slows inactivation of the sodium channel and reduces
CC peak sodium currents. {ECO:0000250|UniProtKB:P04775}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.1/SCN1A subfamily. {ECO:0000305}.
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DR EMBL; X03638; CAA27286.1; -; mRNA.
DR EMBL; M22253; AAA79965.1; -; mRNA.
DR PIR; A25019; A25019.
DR RefSeq; NP_110502.1; NM_030875.1.
DR AlphaFoldDB; P04774; -.
DR BMRB; P04774; -.
DR SMR; P04774; -.
DR BioGRID; 249530; 3.
DR CORUM; P04774; -.
DR STRING; 10116.ENSRNOP00000008026; -.
DR BindingDB; P04774; -.
DR ChEMBL; CHEMBL4906; -.
DR DrugCentral; P04774; -.
DR GuidetoPHARMACOLOGY; 578; -.
DR GlyGen; P04774; 9 sites.
DR iPTMnet; P04774; -.
DR PhosphoSitePlus; P04774; -.
DR SwissPalm; P04774; -.
DR PaxDb; P04774; -.
DR PRIDE; P04774; -.
DR ABCD; P04774; 3 sequenced antibodies.
DR GeneID; 81574; -.
DR KEGG; rno:81574; -.
DR UCSC; RGD:69364; rat.
DR CTD; 6323; -.
DR RGD; 69364; Scn1a.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; P04774; -.
DR OrthoDB; 56920at2759; -.
DR PhylomeDB; P04774; -.
DR Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
DR PRO; PR:P04774; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0043194; C:axon initial segment; ISO:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0014704; C:intercalated disc; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0033268; C:node of Ranvier; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0034706; C:sodium channel complex; ISO:RGD.
DR GO; GO:0030315; C:T-tubule; ISO:RGD.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IDA:RGD.
DR GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
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:0001508; P:action potential; ISO:RGD.
DR GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:RGD.
DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0050884; P:neuromuscular process controlling posture; ISO:RGD.
DR GO; GO:0019228; P:neuronal action potential; IDA:RGD.
DR GO; GO:0019227; P:neuronal action potential propagation; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; ISO:RGD.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR008051; Na_channel_a1su.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc.
DR InterPro; IPR024583; Na_trans_cytopl.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR Pfam; PF11933; Na_trans_cytopl; 1.
DR PRINTS; PR00170; NACHANNEL.
DR PRINTS; PR01664; NACHANNEL1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Sodium;
KW Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
KW Transport; Voltage-gated channel.
FT CHAIN 1..2009
FT /note="Sodium channel protein type 1 subunit alpha"
FT /id="PRO_0000048490"
FT TOPO_DOM 1..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 129..147
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 148..154
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 176..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..207
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 208..213
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 214..230
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 231..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 250..269
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 270..367
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 368..392
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 393..399
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 400..420
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 421..768
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 769..787
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 788..798
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 799..818
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 819..832
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 833..852
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 853..854
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 855..872
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 873..888
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 889..907
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 908..936
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 937..957
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 958..970
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 971..991
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 992..1219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1220..1237
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1238..1250
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1251..1269
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1270..1283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1284..1302
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1303..1310
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1311..1329
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1330..1346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1347..1366
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1367..1418
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1419..1440
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1441..1457
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1458..1479
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1480..1542
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1543..1560
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1561..1571
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1572..1590
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1591..1602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1603..1620
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1621..1633
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1634..1650
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1651..1669
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1670..1687
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1688..1709
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1710..1732
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1733..1762
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1763..1785
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1786..2009
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 110..454
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 750..1022
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1200..1514
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1523..1821
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1915..1944
FT /note="IQ"
FT REGION 28..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1571
FT /note="S1-S2 loop of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:A2APX8"
FT REGION 1619..1636
FT /note="S3b-S4 loop of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:A2APX8"
FT REGION 1986..2009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1990..2009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20131913"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20131913,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20131913"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1516
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 277..345
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 919
FT /note="Interchain; with SCN2B or SCN4B"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 919
FT /note="Interchain; with the conotoxin GVIIJ (when the
FT channel is not linked to SCN2B or SCN4B; the bond to SCN2B
FT or SCN4B protects the channel from the inhibition by
FT toxin)"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 959..968
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
SQ SEQUENCE 2009 AA; 228770 MW; 6808466F6368373B CRC64;
MEQTVLVPPG PDSFNFFTRE SLAAIERRIA EEKAKNPKPD KKDDDENGPK PNSDLEAGKN
LPFIYGDIPP EMVSEPLEDL DPYYINKKTF IVLNKGKAIF RFSATSALYI LTPFNPLRKI
AIKILVHSLF SMLIMCTILT NCVFMTMSNP PDWTKNVEYT FTGIYTFESL IKIIARGFCL
EDFTFLRDPW NWLDFTVITF AYVTEFVDLG NVSALRTFRV LRALKTISVI PGLKTIVGAL
IQSVKKLSDV MILTVFCLSV FALIGLQLFM GNLRNKCVQW PPTNASLEEH SIEKNVTTDY
NGTLVNETVF EFDWKSYIQD SRYHYFLEGV LDALLCGNSS DAGQCPEGYM CVKAGRNPNY
GYTSFDTFSW AFLSLFRLMT QDFWENLYQL TLRAAGKTYM IFFVLVIFLG SFYLINLILA
VVAMAYEEQN QATLEEAEQK EAEFQQMLEQ LKKQQEAAQQ AAAATASEHS REPSAAGRLS
DSSSEASKLS SKSAKERRNR RKKRKQKEQS GGEEKDDDEF HKSESEDSIR RKGFRFSIEG
NRLTYEKRYS SPHQSLLSIR GSLFSPRRNS RTSLFSFRGR AKDVGSENDF ADDEHSTFED
NESRRDSLFV PRRHGERRNS NLSQTSRSSR MLAGLPANGK MHSTVDCNGV VSLVGGPSVP
TSPVGQLLPE VIIDKPATDD NGTTTETEMR KRRSSSFHVS MDFLEDPSQR QRAMSIASIL
TNTVEELEES RQKCPPCWYK FSNIFLIWDC SPYWLKVKHI VNLVVMDPFV DLAITICIVL
NTLFMAMEHY PMTEHFNHVL TVGNLVFTGI FTAEMFLKII AMDPYYYFQE GWNIFDGFIV
TLSLVELGLA NVEGLSVLRS FRLLRVFKLA KSWPTLNMLI KIIGNSVGAL GNLTLVLAII
VFIFAVVGMQ LFGKSYKDCV CKIATDCKLP RWHMNDFFHS FLIVFRVLCG EWIETMWDCM
EVAGQAMCLT VFMMVMVIRN LVVLNLFLAL LLSSFSADNL AATDDDNEMN NLQIAVDRMH
KGVAYVKRKI YEFIQQSFVR KQKILDEIKP LDDLNNRKDN CTSNHTTEIG KDLDCLKDVN
GTTSGIGTGS SVEKYIIDES DYMSFINNPS LTVTVPIAVG ESDFENLNTE DFSSESDLEE
SKEKLNESSS SSEGSTVDIG APAEEQPVME PEETLEPEAC FTEGCVQRFK CCQISVEEGR
GKQWWNLRRT CFRIVEHNWF ETFIVFMILL SSGALAFEDI YIDQRKTIKT MLEYADKVFT
YIFILEMLLK WVAYGYQTYF TNAWCWLDFL IVDVSLVSLT ANALGYSELG AIKSLRTLRA
LRPLRALSRF EGMRVVVNAL LGAIPSIMNV LLVCLIFWLI FSIMGVNLFA GKFYHCVNTT
TGDTFEITEV NNHSDCLKLI ERNETARWKN VKVNFDNVGF GYLSLLQVAT FKGWMDIMYA
AVDSRNVELQ PKYEESLYMY LYFVIFIIFG SFFTLNLFIG VIIDNFNQQK KKFGGQDIFM
TEEQKKYYNA MKKLGSKKPQ KPIPRPGNKF QGMVFDFVTR QVFDISIMIL ICLNMVTMMV
ETDDQSDYVT SILSRINLVF IVLFTGECVL KLISLRHYYF TIGWNIFDFV VVILSIVGMF
LAELIEKYFV SPTLFRVIRL ARIGRILRLI KGAKGIRTLL FALMMSLPAL FNIGLLLFLV
MFIYAIFGMS NFAYVKREVG IDDMFNFETF GNSMICLFQI TTSAGWDGLL APILNSKPPD
CDPNKVNPGS SVKGDCGNPS VGIFFFVSYI IISFLVVVNM YIAVILENFS VATEESAEPL
SEDDFEMFYE VWEKFDPDAT QFMEFEKLSQ FAAALEPPLN LPQPNKLQLI AMDLPMVSGD
RIHCLDILFA FTKRVLGESG EMDALRIQME ERFMASNPSK VSYQPITTTL KRKQEEVSAV
IIQRAYRRHL LKRTVKQASF TYNKNKLKGG ANLLVKEDMI IDRINENSIT EKTDLTMSTA
ACPPSYDRVT KPIVEKHEQE GKDEKAKGK
