SCNAA_MOUSE
ID SCNAA_MOUSE Reviewed; 1958 AA.
AC Q6QIY3; Q62243; Q6EWG7; Q6KCH7; Q703F9;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 943-1090 (ISOFORMS 1 AND 2).
RC STRAIN=129P2; 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 by a
RT conserved mechanism in mouse and rat.";
RL J. Biol. Chem. 279:24826-24833(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 3).
RC STRAIN=C3H/HeJ;
RA Jover E., Shah V.;
RT "Mouse sodium channel clone BC in pSB+.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RC STRAIN=CD-1; TISSUE=Spinal ganglion;
RA Puhl H.L. III, King M.M., Ikeda S.R.;
RT "cDNA cloning of the mouse sensory neuron specific sodium channel Nav1.8
RT (Scn10a).";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH NEDD4 AND NEDD4L, PROBABLE UBIQUITINATION, AND MUTAGENESIS
RP OF TYR-1922.
RX PubMed=15123669; DOI=10.1074/jbc.m402820200;
RA Fotia A.B., Ekberg J., Adams D.J., Cook D.I., Poronnik P., Kumar S.;
RT "Regulation of neuronal voltage-gated sodium channels by the ubiquitin-
RT protein ligases Nedd4 and Nedd4-2.";
RL J. Biol. Chem. 279:28930-28935(2004).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF GLN-861.
RX PubMed=24159039; DOI=10.1126/science.1236451;
RA Rowe A.H., Xiao Y., Rowe M.P., Cummins T.R., Zakon H.H.;
RT "Voltage-gated sodium channel in grasshopper mice defends against bark
RT scorpion toxin.";
RL Science 342:441-446(2013).
CC -!- FUNCTION: Tetrodotoxin-resistant channel that mediates the voltage-
CC dependent sodium ion permeability of excitable membranes. Assuming
CC opened or closed conformations in response to the voltage difference
CC across the membrane, the protein forms a sodium-selective channel
CC through which sodium ions may pass in accordance with their
CC electrochemical gradient. Plays a role in neuropathic pain mechanisms.
CC {ECO:0000269|PubMed:24159039}.
CC -!- SUBUNIT: The channel consists of an ion conducting pore forming alpha-
CC subunit regulated by one or more associated auxiliary subunits SCN1B,
CC SCN2B and SCN3B; electrophysiological properties may vary depending on
CC the type of the associated beta subunits. Found in a number of
CC complexes with PRX, DYNLT1 and PDZD2. Interacts with proteins such as
CC FSTL1, PRX, DYNLT1, PDZD2, S100A10 and many others (By similarity).
CC Interacts with NEDD4 and NEDD4L. {ECO:0000250,
CC ECO:0000269|PubMed:15123669}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D0E0C2};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Note=It can
CC be translocated to the cell membrane through association with S100A10.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6QIY3-1; Sequence=Displayed;
CC Name=2; Synonyms=Nav1.8c;
CC IsoId=Q6QIY3-2; Sequence=VSP_012257;
CC Name=3;
CC IsoId=Q6QIY3-3; Sequence=VSP_012256;
CC -!- TISSUE SPECIFICITY: Expressed in dorsal root ganglion and trigeminal
CC ganglion.
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: Ubiquitinated by NEDD4L; which promotes its endocytosis.
CC {ECO:0000305}.
CC -!- PTM: Phosphorylation at Ser-1452 by PKC in a highly conserved
CC cytoplasmic loop slows inactivation of the sodium channel and reduces
CC peak sodium currents. {ECO:0000250}.
CC -!- PTM: Lacks the cysteine which covalently binds the conotoxin GVIIJ.
CC This cysteine (position 815) is speculated in other sodium channel
CC subunits alpha to be implied in covalent binding with the sodium
CC channel subunit beta-2 or beta-4. {ECO:0000250|UniProtKB:P15389}.
CC -!- MISCELLANEOUS: Mus musculus is sensitive to the pain-inducing
CC components of the bark scorpion (Centruroides sculpturatus) venom while
CC Onychomys torridus is not. Gln-861 may account for the difference
CC between both rodents and its replacement by a glutamate, the
CC corresponding amino acid found in the Onychomys torridus ortholog,
CC allows inhibition of Snc10a by the venom, which in turn, inhibits
CC sodium currents, blocks action potential propagation and may induce
CC analgesia (PubMed:24159039). {ECO:0000305|PubMed:24159039}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.8/SCN10A subfamily. {ECO:0000305}.
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DR EMBL; AJ622906; CAF22039.1; -; Genomic_DNA.
DR EMBL; AJ623269; CAF25039.1; -; mRNA.
DR EMBL; AJ623270; CAF25040.1; -; mRNA.
DR EMBL; L42342; AAA68000.1; -; mRNA.
DR EMBL; AY538273; AAS45602.1; -; mRNA.
DR CCDS; CCDS57716.1; -. [Q6QIY3-1]
DR CCDS; CCDS90682.1; -. [Q6QIY3-2]
DR RefSeq; NP_033160.2; NM_009134.3. [Q6QIY3-2]
DR RefSeq; XP_017168712.1; XM_017313223.1. [Q6QIY3-1]
DR AlphaFoldDB; Q6QIY3; -.
DR SMR; Q6QIY3; -.
DR BioGRID; 203097; 8.
DR STRING; 10090.ENSMUSP00000081845; -.
DR BindingDB; Q6QIY3; -.
DR ChEMBL; CHEMBL5158; -.
DR GlyGen; Q6QIY3; 9 sites.
DR iPTMnet; Q6QIY3; -.
DR PhosphoSitePlus; Q6QIY3; -.
DR PaxDb; Q6QIY3; -.
DR PRIDE; Q6QIY3; -.
DR ProteomicsDB; 256752; -. [Q6QIY3-1]
DR ProteomicsDB; 256753; -. [Q6QIY3-2]
DR ProteomicsDB; 256754; -. [Q6QIY3-3]
DR ABCD; Q6QIY3; 1 sequenced antibody.
DR Antibodypedia; 28790; 242 antibodies from 29 providers.
DR DNASU; 20264; -.
DR Ensembl; ENSMUST00000213392; ENSMUSP00000148987; ENSMUSG00000034533. [Q6QIY3-2]
DR GeneID; 20264; -.
DR KEGG; mmu:20264; -.
DR UCSC; uc009sbf.2; mouse. [Q6QIY3-3]
DR UCSC; uc009sbg.3; mouse. [Q6QIY3-2]
DR CTD; 6336; -.
DR MGI; MGI:108029; Scn10a.
DR VEuPathDB; HostDB:ENSMUSG00000034533; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000154992; -.
DR InParanoid; Q6QIY3; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; Q6QIY3; -.
DR Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR BioGRID-ORCS; 20264; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q6QIY3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6QIY3; protein.
DR Bgee; ENSMUSG00000034533; Expressed in dorsal root ganglion and 15 other tissues.
DR ExpressionAtlas; Q6QIY3; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0044299; C:C-fiber; IDA:MGI.
DR GO; GO:0071439; C:clathrin complex; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:MGI.
DR GO; GO:0086016; P:AV node cell action potential; ISO:MGI.
DR GO; GO:0086043; P:bundle of His cell action potential; ISO:MGI.
DR GO; GO:0061337; P:cardiac conduction; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IDA:MGI.
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:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; IMP:MGI.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; ISO:MGI.
DR GO; GO:0002027; P:regulation of heart rate; ISO:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; ISO:MGI.
DR GO; GO:0019233; P:sensory perception of pain; ISO:MGI.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006814; P:sodium ion transport; IDA:MGI.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR028809; Na_channel_a10su.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR PANTHER; PTHR10037:SF208; PTHR10037:SF208; 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; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Sodium; Sodium channel; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..1958
FT /note="Sodium channel protein type 10 subunit alpha"
FT /id="PRO_0000048508"
FT TOPO_DOM 1..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 126..149
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..154
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..174
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..206
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..212
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..232
FT /note="Helical; Voltage-sensor; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 249..272
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..340
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 341..365
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 366..372
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 373..398
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..658
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 659..683
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 684..694
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 695..718
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..726
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 727..746
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 747..752
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 753..772
FT /note="Helical; Voltage-sensor; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 773..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 789..809
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 810..833
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 834..854
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 855..863
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 864..889
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 890..1148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1149..1172
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1173..1185
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1186..1211
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1212..1217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1218..1239
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1240..1243
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1244..1265
FT /note="Helical; Voltage-sensor; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1266..1284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1285..1312
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1313..1354
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1355..1376
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1377..1392
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1393..1419
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1420..1472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1473..1496
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1497..1507
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1508..1531
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1532..1537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1538..1561
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1562..1573
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1574..1595
FT /note="Helical; Voltage-sensor; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1596..1610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1611..1633
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1634..1647
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1648..1670
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1671..1698
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1699..1723
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1724..1958
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 116..404
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 646..910
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1141..1450
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1459..1758
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1852..1881
FT /note="IQ"
FT REGION 27..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1901..1958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1076
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1907..1945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT MOD_RES 1452
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q14524"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 276..318
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 856..865
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT VAR_SEQ 1..1435
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_012256"
FT VAR_SEQ 1030
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15047701"
FT /id="VSP_012257"
FT MUTAGEN 861
FT /note="Q->E: Sensitive to inhibition by some components of
FT the venom of Centruroides sculpturatus."
FT /evidence="ECO:0000269|PubMed:24159039"
FT MUTAGEN 1922
FT /note="Y->A: No regulation by NEDD4L."
FT /evidence="ECO:0000269|PubMed:15123669"
SQ SEQUENCE 1958 AA; 220552 MW; 24830634E86490FF CRC64;
MEFPFGSVGT TNFRRFTPES LAEIEKQIAA HRAAKKGRPK QRGQKDKSEK PRPQLDLKAC
NQLPRFYGEL PAELVGEPLE DLDPFYSTHR TFIVLDKSRT ISRFSATWAL WLFSPFNLIR
RTAIKVSVHS WFSIFITVTI LVNCVCMTRT DLPEKLEYAF TVVYTFEALI KILARGFCLN
EFTYLRDPWN WLDFSVITLA YVGAAIDLRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI
HSVRKLADVT ILTVFCLSVF ALVGLQLFKG NLKNKCIKNG TDPHKADNLS SEMAGDIFIK
PGTTDPLLCG NGSDAGHCPN DYVCRKTSDN PDFNYTSFDS FAWAFLSLFR LMTQDSWERL
YQQTLRASGK MYMVFFVLVI FLGSFYLVNL ILAVVTMAYE EQSQATIAEI EAKEKKFKEA
LEVLQKEQEV LAALGIDTTS LYSHNGSPLA PKNANERRPR VKSRMSEGST DDNRSLQSDP
YNQRRMSFLG LSSGRRRASH SSVFHFRAPS QDVSFPDGIL DDGVFHGDQE SRRSSILLGR
GAGQAGPLPR SPLPQSPNPG PRRGEEGQRG VPTGELATGA PEGPALDAAG QKNFLSADYL
NEPFRAQRAM SVVSIMTSVI EELEESKLKC PPCLISLAQK YLIWECCPKW KKFKMVLFEL
VTDPFAELTI TLCIVVNTVF MAMEHYPMTD AFDAMLQAGN IVFTVFFTME MAFKIIAFDP
YYYFQKKWNI FDCVIVTVSL LELSTSKKGS LSVLRTFRLL RVFKLAKSWP TLNMLIKIIG
NSVGALGNLT FILAIIVFIF ALVGKQLLSE NYGCRRDGIS VWNGERLRWH MCDFFHSFLV
VFRILCGEWI ENMWVCMEVS QDYICLTLFL TVMVLGNLVV LNLFIALLLN SFSADNLTAP
EDDGEVNNLQ VALARIQVFG HRASRAITSY IRSHCRLRWP KVETQLGMKP PLTSCKAENH
IATDAVNAAV GNLAKPALGG PKENHGDFIT DPNVWVSVPI AEGESDLDEL EEDVEHASQS
SWQEESPKGQ QELLQQVQKC EDHQAARSPP SGMSSEDLAP YLGERWQREE SPRVPAEGVD
DTSSSEGSTV DCPDPEEILR KIPELAEELD EPDDCFPEGC TRRCPCCKVN TSKFPWATGW
QVRKTCYRIV EHSWFESFII FMILLSSGAL AFEDNYLEEK PRVKSVLEYT DRVFTFIFVF
EMLLKWVAYG FKKYFTNAWC WLDFLIVNIS LTSLIAKILE YSDVASIKAL RTLRALRPLR
ALSRFEGMRV VVDALVGAIP SIMNVLLVCL IFWLIFSIMG VNLFAGKFSR CVDTRSNPFS
VVNSTFVTNK SDCYNQNNTG HFFWVNVKVN FDNVAMGYLA LLQVATFKGW MDIMYAAVDS
RDINSQPNWE ESLYMYLYFV VFIIFGGFFT LNLFVGVIID NFNQQKKKLG GQDIFMTEEQ
KKYYNAMKKL GSKKPQKPIP RPLNKYQGFV FDIVTRQAFD IIIMALICLN MITMMVETDN
QSEEKTKVLG RINQFFVAVF TGECVMKMFA LRQYYFTNGW NVFDFIVVIL SISSLLFSAI
LSSLESYFSP TLLRVIRLAR IGRILRLIRA AKGIRTLLFA LMMSLPALFN IGLLLFLVMF
IYSIFGMASF ANVIDEAGID DMFNFKTFGN SMLCLFQITT SAGWDGLLSP ILNTGPPYCD
PNRPNSNGSK GNCGSPAVGI LFFTTYIIIS FLIVVNMYIA VILENFNVAT EESTEPLSED
DFDMFYETWE KFDPEATQFI AFSALSDFAD TLSGPLRIPK PNQNILIQMD LPLVPGDKIH
CLDILFAFTK NVLGESGELD SLKTNMEEKF MATNLSKASY EPIATTLRCK QEDISATIIQ
KAYRNYMLQR SLMLSNPLHV PRAEEDGVSL PREGYVTFMA NDNGGLPDKS ETASATSFPP
SYDSVTRGLS DRANISTSSS MQNEDEVTAK EGKSPGPQ
