SCN9A_RAT
ID SCN9A_RAT Reviewed; 1984 AA.
AC O08562;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Sodium channel protein type 9 subunit alpha {ECO:0000250|UniProtKB:Q15858};
DE AltName: Full=Peripheral sodium channel 1;
DE Short=PN1 {ECO:0000303|PubMed:9037087};
DE AltName: Full=Sodium channel protein type IX subunit alpha;
DE AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.7;
GN Name=Scn9a {ECO:0000312|RGD:69368};
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], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=9037087; DOI=10.1073/pnas.94.4.1527;
RA Toledo-Aral J.J., Moss B.L., He Z.J., Koszowski A.G., Whisenand T.,
RA Levinson S.R., Wolf J.J., Silos-Santiago I., Halegoua S., Mandel G.;
RT "Identification of PN1, a predominant voltage-dependent sodium channel
RT expressed principally in peripheral neurons.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1527-1532(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Spinal ganglion;
RX PubMed=9169448; DOI=10.1074/jbc.272.23.14805;
RA Sangameswaran L., Fish L.M., Koch B.D., Rabert D.K., Delgado S.G.,
RA Ilnicka M., Jakeman L.B., Novakovic S., Wong K., Sze P., Tzoumaka E.,
RA Stewart G.R., Herman R.C., Chan H., Eglen R.M., Hunter J.C.;
RT "A novel tetrodotoxin-sensitive, voltage-gated sodium channel expressed in
RT rat and human dorsal root ganglia.";
RL J. Biol. Chem. 272:14805-14809(1997).
RN [3]
RP PROTEIN SEQUENCE OF 527-547, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
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. It is a tetrodotoxin-
CC sensitive Na(+) channel isoform. Plays a role in pain mechanisms,
CC especially in the development of inflammatory pain.
CC {ECO:0000250|UniProtKB:Q15858}.
CC -!- SUBUNIT: The sodium channel complex consists of a large, channel-
CC forming alpha subunit (SCN9A) regulated by one or more beta subunits
CC (SCN1B, SCN2B, SCN3B and SCN4B) (By similarity). SCN1B and SCN3B are
CC non-covalently associated with SCN2A. SCN2B and SCN4B are disulfide-
CC linked to SCN2A (By similarity). Interacts with NEDD4 and NEDD4L (By
CC similarity). Interacts with the conotoxin GVIIJ (PubMed:24497506).
CC {ECO:0000250|UniProtKB:Q15858, ECO:0000250|UniProtKB:Q62205,
CC ECO:0000269|PubMed:24497506}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15858};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Cell
CC projection, neuron projection {ECO:0000269|PubMed:9037087}. Note=In
CC neurite terminals. {ECO:0000269|PubMed:9037087}.
CC -!- TISSUE SPECIFICITY: Expressed at high level in the dorsal root ganglion
CC and at much lower levels in the brain, sciatic nerve, nodose ganglia,
CC heart, thyroid and adrenal glands and Schwann cells, but not in the
CC cardiac and skeletal muscles, brain and liver.
CC {ECO:0000269|PubMed:9037087, ECO:0000269|PubMed:9169448}.
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 -!- PTM: Phosphorylation at Ser-1488 by PKC in a highly conserved
CC cytoplasmic loop increases peak sodium currents.
CC {ECO:0000250|UniProtKB:Q15858}.
CC -!- PTM: Ubiquitinated by NEDD4L; which may promote its endocytosis. Does
CC not seem to be ubiquitinated by NEDD4. {ECO:0000250|UniProtKB:Q62205}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.7/SCN9A subfamily. {ECO:0000305}.
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DR EMBL; U79568; AAB50403.1; -; mRNA.
DR EMBL; AF000368; AAB80701.1; -; mRNA.
DR RefSeq; NP_579823.1; NM_133289.1.
DR AlphaFoldDB; O08562; -.
DR BMRB; O08562; -.
DR SMR; O08562; -.
DR BioGRID; 249364; 2.
DR STRING; 10116.ENSRNOP00000059170; -.
DR BindingDB; O08562; -.
DR ChEMBL; CHEMBL3312; -.
DR GuidetoPHARMACOLOGY; 584; -.
DR GlyGen; O08562; 5 sites.
DR iPTMnet; O08562; -.
DR PhosphoSitePlus; O08562; -.
DR SwissPalm; O08562; -.
DR PaxDb; O08562; -.
DR PRIDE; O08562; -.
DR ABCD; O08562; 1 sequenced antibody.
DR GeneID; 78956; -.
DR KEGG; rno:78956; -.
DR UCSC; RGD:69368; rat.
DR CTD; 6335; -.
DR RGD; 69368; Scn9a.
DR VEuPathDB; HostDB:ENSRNOG00000006639; -.
DR VEuPathDB; HostDB:ENSRNOG00000053122; -.
DR eggNOG; KOG2301; Eukaryota.
DR HOGENOM; CLU_000540_5_0_1; -.
DR InParanoid; O08562; -.
DR OMA; SKYMTDV; -.
DR OrthoDB; 56920at2759; -.
DR PhylomeDB; O08562; -.
DR TreeFam; TF323985; -.
DR Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
DR PRO; PR:O08562; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000006639; Expressed in cerebral cortex and 6 other tissues.
DR Genevisible; O08562; RN.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; 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:0061368; P:behavioral response to formalin induced pain; IMP:RGD.
DR GO; GO:0048266; P:behavioral response to pain; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0045759; P:negative regulation of action potential; IMP:RGD.
DR GO; GO:0019228; P:neuronal action potential; IDA:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0009409; P:response to cold; IMP:RGD.
DR GO; GO:0009408; P:response to heat; IMP:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR GO; GO:0043179; P:rhythmic excitation; NAS:RGD.
DR GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane 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; IPR000048; IQ_motif_EF-hand-BS.
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; IPR028803; SCN9A.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR PANTHER; PTHR10037:SF221; PTHR10037:SF221; 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 SMART; SM00015; IQ; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Direct protein sequencing; 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..1984
FT /note="Sodium channel protein type 9 subunit alpha"
FT /id="PRO_0000048505"
FT TOPO_DOM 1..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 127..145
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 146..152
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 174..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..205
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 206..211
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 212..228
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 229..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 248..267
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 268..346
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 347..371
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 372..378
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 379..399
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 400..743
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 744..762
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 763..773
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 774..793
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 794..807
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 808..827
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 828..829
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 830..847
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 848..863
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 864..882
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 883..911
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 912..932
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 933..945
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 946..966
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 967..1191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1192..1209
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1210..1222
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1223..1241
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1242..1255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1256..1274
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1275..1282
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1283..1301
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1302..1318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1319..1338
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1339..1390
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1391..1412
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1413..1429
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1430..1451
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1452..1514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1515..1532
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1533..1543
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1544..1562
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1563..1574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1575..1592
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1593..1605
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1606..1622
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1623..1641
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1642..1659
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1660..1681
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1682..1704
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1705..1734
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1735..1757
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1758..1984
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 112..410
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 725..988
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1178..1486
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1495..1793
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1887..1916
FT /note="IQ"
FT REGION 26..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1916..1984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1916..1930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1931..1959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 821
FT /note="Is directly targeted by the spider protoxin-II"
FT /evidence="ECO:0000250|UniProtKB:Q15858"
FT SITE 826
FT /note="Is directly targeted by the spider protoxin-II"
FT /evidence="ECO:0000250|UniProtKB:Q15858"
FT MOD_RES 1488
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q15858"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 275..324
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 894
FT /note="Interchain; with SCN2B or SCN4B"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 894
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 896..902
FT /evidence="ECO:0000250|UniProtKB:Q15858"
FT DISULFID 934..943
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 1348..1368
FT /evidence="ECO:0000250|UniProtKB:Q15858"
FT DISULFID 1713..1728
FT /evidence="ECO:0000250|UniProtKB:Q15858"
SQ SEQUENCE 1984 AA; 226039 MW; 386C38B9B5097091 CRC64;
MAMLPPPGPQ SFVHFTKQSL ALIEQRISEE KAKEHKDEKK DDEEEGPKPS SDLEAGKQLP
FIYGDIPPGM VSEPLEDLDP YYADKKTFIV LNKGKAIFRF NATPALYMLS PFSPLRRISI
KILVHSLFSM LIMCTILTNC IFMTLSNPPE WTKNVEYTFT GIYTFESLIK ILARGFCVGE
FTFLRDPWNW LDFVVIVFAY LTEFVNLGNV SALRTFRVLR ALKTISVIPG LKTIVGALIQ
SVKKLSDVMI LTVFCLSVFA LIGLQLFMGN LKHKCFRKEL EENETLESIM NTAESEEELK
KYFYYLEGSK DALLCGFSTD SGQCPEGYIC VKAGRNPDYG YTSFDTFSWA FLALFRLMTQ
DYWENLYQQT LRAAGKTYMI FFVVVIFLGS FYLINLILAV VAMAYEEQNQ ANIEEAKQKE
LEFQQMLDRL KKEQEEAEAI AAAAAEFTSI GRSRIMGLSE SSSETSRLSS KSAKERRNRR
KKKKQKMSSG EEKGDDEKLS KSGSEESIRK KSFHLGVEGH HRTREKRLST PNQSPLSIRG
SLFSARRSSR TSLFSFKGRG RDLGSETEFA DDEHSIFGDN ESRRGSLFVP HRPRERRSSN
ISQASRSPPV LPVNGKMHSA VDCNGVVSLV DGPSALMLPN GQLLPEVIID KATSDDSGTT
NQMRKKRLSS SYFLSEDMLN DPHLRQRAMS RASILTNTVE ELEESRQKCP PWWYRFAHTF
LIWNCSPYWI KFKKLIYFIV MDPFVDLAIT ICIVLNTLFM AMEHHPMTEE FKNVLAVGNL
IFTGIFAAEM VLKLIAMDPY EYFQVGWNIF DSLIVTLSLI ELFLADVEGL SVLRSFRLLR
VFKLAKSWPT LNMLIKIIGN SVGALGNLTL VLAIIVFIFA VVGMQLFGKS YKECVCKINV
DCKLPRWHMN DFFHSFLIVF RVLCGEWIET MWDCMEVAGQ TMCLIVYMMV MVIGNLVVLN
LFLALLLSSF SSDNLTAIEE DTDANNLQIA VARIKRGINY VKQTLREFIL KSFSKKPKGS
KDTKRTADPN NKKENYISNR TLAEMSKDHN FLKEKDRISG YGSSLDKSFM DENDYQSFIH
NPSLTVTVPI APGESDLEIM NTEELSSDSD SDYSKEKRNR SSSSECSTVD NPLPGEEEAE
AEPVNADEPE ACFTDGCVRR FPCCQVNVDS GKGKVWWTIR KTCYRIVEHS WFESFIVLMI
LLSSGALAFE DIYIEKKKTI KIILEYADKI FTYIFILEML LKWVAYGYKT YFTNAWCWLD
FLIVDVSLVT LVANTLGYSD LGPIKSLRTL RALRPLRALS RFEGMRVVVN ALIGAIPSIM
NVLLVCLIFW LIFSIMGVNL FAGKFYECVN TTDGSRFPTS QVANRSECFA LMNVSGNVRW
KNLKVNFDNV GLGYLSLLQV ATFKGWMDIM YAAVDSVNVN EQPKYEYSLY MYIYFVIFII
FGSFFTLNLF IGVIIDNFNQ QKKKLGGQDI FMTEEQKKYY NAMKKLGSKK PQKPIPRPGN
KFQGCIFDLV TNQAFDITIM VLICLNMVTM MVEKEGQTEY MDYVLHWINM VFIILFTGEC
VLKLISLRHY YFTVGWNIFD FVVVILSIVG MFLAEMIEKY FVSPTLFRVI RLARIGRILR
LIKGAKGIRT LLFALMMSLP ALFNIGLLLF LVMFIYAIFG MSNFAYVKKE AGINDMFNFE
TFGNSMICLF QITTSAGWDG LLAPILNSAP PDCDPKKVHP GSSVEGDCGN PSVGIFYFVS
YIIISFLVVV NMYIAVILEN FSVATEESTE PLSEDDFEMF YEVWEKFDPD ATQFIEFCKL
SDFAAALDPP LLIAKPNKVQ LIAMDLPMVS GDRIHCLDIL FAFTKRVLGE GGEMDSLRSQ
MEERFMSANP SKVSYEPITT TLKRKQEEVS ATIIQRAYRR YRLRQHVKNI SSIYIKDGDR
DDDLPNKEDT VFDNVNENSS PEKTDVTAST ISPPSYDSVT KPDQEKYETD KTEKEDKEKD
ESRK
