ID   SCNAA_ONYTO             Reviewed;        1959 AA.
AC   P0DMA5; U6BRW2;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Sodium channel protein type 10 subunit alpha;
GN   Name=Scn10a; Synonyms=Sns;
OS   Onychomys torridus (Southern grasshopper mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Onychomys.
OX   NCBI_TaxID=38674;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, AND MUTAGENESIS
RP   OF 746-ILE--ALA-747 AND 859-GLN--GLN-862.
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).
RN   [2]
RP   MUTAGENESIS OF ARG-215; ARG-218; 756-ARG--ARG-759 AND 859-GLN--GLN-862, AND
RP   3D-STRUCTURE MODELING IN COMPLEX WITH SCORPION NATX36 TOXIN.
RX   PubMed=35662692; DOI=10.3389/fphar.2022.846992;
RA   George K., Lopez-Mateos D., Abd El-Aziz T.M., Xiao Y., Kline J., Bao H.,
RA   Raza S., Stockand J.D., Cummins T.R., Fornelli L., Rowe M.P.,
RA   Yarov-Yarovoy V., Rowe A.H.;
RT   "Structural and functional characterization of a novel scorpion toxin that
RT   inhibits NaV1.8 via interactions with the DI voltage sensor and DII pore
RT   module.";
RL   Front. Pharmacol. 13:846992-846992(2022).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC         ChEBI:CHEBI:29101; Evidence={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. Interacts with
CC       NEDD4 and NEDD4L (By similarity). {ECO:0000250}.
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   -!- 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-1453 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 816) 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: O.torridus is resistant to the pain-inducing components
CC       of the venom of its prey, the bark scorpion (Centruroides
CC       sculpturatus). It is most probably due to the unique inhibition by some
CC       venom components of the Scn10a sodium-channel in those rodents.
CC       Inhibition of Snc10a would, in turn, inhibit sodium currents, block
CC       action potential propagation and induce analgesia. Glu-862 plays a
CC       central role in that inhibition and its replacement by a Gln, the
CC       corresponding amino acid found in the M.musculus ortholog, prevents the
CC       inhibition of Snc10a. This would explain why the venom induces pain in
CC       M.musculus but not in O.torridus (PubMed:24159039).
CC       {ECO:0000305|PubMed:24159039}.
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.8/SCN10A subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=A pain soothed - Issue 157
CC       of January 2014;
CC       URL="https://web.expasy.org/spotlight/back_issues/157/";
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DR   EMBL; KF717604; AHA38158.1; -; mRNA.
DR   AlphaFoldDB; P0DMA5; -.
DR   SMR; P0DMA5; -.
DR   GlyCosmos; P0DMA5; 3 sites, No reported glycans.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; ISS:UniProtKB.
DR   GO; GO:0086010; P:membrane depolarization during action potential; ISS:UniProtKB.
DR   CDD; cd13433; Na_channel_gate; 1.
DR   Gene3D; 1.10.287.70; -; 4.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 1.20.5.1190; iswi atpase; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR044564; Na_chnl_inactivation_gate.
DR   InterPro; IPR010526; Na_trans_assoc_dom.
DR   InterPro; IPR043203; VGCC_Ca_Na.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF208; SODIUM CHANNEL PROTEIN TYPE 10 SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   PRINTS; PR00170; NACHANNEL.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Membrane; Phosphoprotein; Repeat; Sodium; Sodium channel; Sodium transport;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
KW   Voltage-gated channel.
FT   CHAIN           1..1959
FT                   /note="Sodium channel protein type 10 subunit alpha"
FT                   /id="PRO_0000424959"
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..659
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        660..684
FT                   /note="Helical; Name=S1 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        685..695
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        696..719
FT                   /note="Helical; Name=S2 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        720..727
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        728..747
FT                   /note="Helical; Name=S3 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        748..753
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        754..773
FT                   /note="Helical; Voltage-sensor; Name=S4 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        774..789
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        790..810
FT                   /note="Helical; Name=S5 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        811..834
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        835..855
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        856..864
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        865..890
FT                   /note="Helical; Name=S6 of repeat II"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        891..1149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1150..1173
FT                   /note="Helical; Name=S1 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1174..1186
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1187..1212
FT                   /note="Helical; Name=S2 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1213..1218
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1219..1240
FT                   /note="Helical; Name=S3 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1241..1244
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1245..1266
FT                   /note="Helical; Voltage-sensor; Name=S4 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1267..1285
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1286..1313
FT                   /note="Helical; Name=S5 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1314..1355
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        1356..1377
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1378..1393
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1394..1420
FT                   /note="Helical; Name=S6 of repeat III"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1421..1473
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1474..1497
FT                   /note="Helical; Name=S1 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1498..1508
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1509..1532
FT                   /note="Helical; Name=S2 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1533..1538
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1539..1562
FT                   /note="Helical; Name=S3 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1563..1574
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1575..1596
FT                   /note="Helical; Voltage-sensor; Name=S4 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1597..1611
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1612..1634
FT                   /note="Helical; Name=S5 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1635..1648
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        1649..1671
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   TOPO_DOM        1672..1699
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1700..1724
FT                   /note="Helical; Name=S6 of repeat IV"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1725..1959
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REPEAT          116..404
FT                   /note="I"
FT                   /evidence="ECO:0000305"
FT   REPEAT          647..911
FT                   /note="II"
FT                   /evidence="ECO:0000305"
FT   REPEAT          1142..1451
FT                   /note="III"
FT                   /evidence="ECO:0000305"
FT   REPEAT          1460..1759
FT                   /note="IV"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          1853..1882
FT                   /note="IQ"
FT   REGION          30..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1004..1034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1071..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1901..1959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..484
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1907..1944
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         612
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         615
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
FT   MOD_RES         1453
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:Q14524"
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   DISULFID        276..318
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   DISULFID        857..866
FT                   /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT   MUTAGEN         215
FT                   /note="R->G: Complete loss of inhibition by the venom of
FT                   Centruroides sculpturatus. Decrease in inhibition by the
FT                   venom of Centruroides sculpturatus; when associated with
FT                   G-218."
FT                   /evidence="ECO:0000269|PubMed:35662692"
FT   MUTAGEN         218
FT                   /note="R->G: Decrease in inhibition by the venom of
FT                   Centruroides sculpturatus; when associated with G-215."
FT                   /evidence="ECO:0000269|PubMed:35662692"
FT   MUTAGEN         746..747
FT                   /note="IA->TS: No effect on inhibition by the venom of
FT                   Centruroides sculpturatus."
FT                   /evidence="ECO:0000269|PubMed:24159039"
FT   MUTAGEN         756..759
FT                   /note="RTFR->GTFG: No change in inhibition by the venom of
FT                   Centruroides sculpturatus."
FT                   /evidence="ECO:0000269|PubMed:35662692"
FT   MUTAGEN         859..862
FT                   /note="QVSE->EVSQ: Complete loss of inhibition by the venom
FT                   of Centruroides sculpturatus."
FT                   /evidence="ECO:0000269|PubMed:24159039,
FT                   ECO:0000269|PubMed:35662692"
SQ   SEQUENCE   1959 AA;  220523 MW;  FE84EC9345B5EB74 CRC64;
     MEFPIGSVGT TNFRRFTPES LAEIEKQIAA HGAAKKARAK HGERKGQDEK PRPQLDLKAC
     NQLPRFYGEL PAELVGEPLE DLDPFYSTHR TFMVLNKGRT ISRFSATWAL WLFSPFNLIR
     RTAIKVSVHA WFSIFITITI LFNCVCMTQN DLPEKIEYAF TVIYTFEALI KILARGFCLN
     EFTYLRDPWN WLDFSVITLA YVGAAIDLRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI
     HSVRKLADVT ILTVFCLSVF ALVGLQLFKG NLKNKCIKRS TDPHNAYNFS SQMADNFYIK
     NGTTEPLLCG NGSDAGHCPS GYICLKTSDN PDFNYTSFDS FAWAFLSLFR LMTQDSWERL
     YQQTLRASGK MYMVFFVLVI FLGSFYLVNL ILAVVTMAYE EQNQATIAEI EAKEKKFQEA
     LEVLQKEQEV LAALGIDTTS LHSHNGSPLA PKNANERKHR IKSRVSEGST DDNRSPQSDP
     YNQRRMSFLG LSSGRRRASH SSVFHFRAPS QDVSFPDGIT DDGVFHGDHE SHRSSLLLAR
     GAGQAGPLPR SPLASSPNPG PGHREEGQLT APTGELTTGA PEDLALEAAG QKKNFLSAEY
     LNEPFRAQRA MSVVSIMTSV IEELEESKLR CPPCLINLAQ KYLIWECCPK WMKFKMVLFE
     LVTDPFAELT ITLCIVVNTI FMAMEHYPMT DAFDAMLQAG NIVFTVFFTM EMAFKIIAFD
     PYYYFQKKWN VFDCVIVTVS LLELSIAKKG SLSVLRTFRL LRVFKLAKSW PTLNTLIKII
     GNSVGALGNL TFILAIIVFI FALVGKQLLG EDYGCRKDGT ALWNEGQLRW HMCDFFHSFL
     VIFRILCGEW IENMWVCMQV SEKSICLILF LTVMVLGNLV VLNLFIALLL NSFSADNLTA
     PEDDGEVNNL QVALARTQAF GQRASQAISS YFSSHCRLRW PKVGSQLGVK PSLTSSKAEH
     HITADAVNTA VGTSAKPALS GPKEDPRDFI TDANVWVSVP IAEGESDLDE LEEDIEQNSQ
     SSWREESPKG QQDQLWQIQR CEDHQVPNSP GSGMSSEDLA SYLGERWKSE ATPQVPAEGV
     DDTSSSEGST VDCPDPEEIL KKIPELADDL EEPDDCFTEG CTRHCPCCKV STSKFPWTTG
     WQVRKTCYRI VEHSWFESFI IFMILLSSGA LAFEDNYLEQ KPRVKSMLEY TDRVFTFIFV
     FEMLLKWVAY GFKKYFTNAW CWLDFLIVNI SLTSLIAKIL DYSDVASLKA LRTLRALRPL
     RALSRFEGMR VVVDALVGAI PSIMNVLLVC LIFWLIFSIM GVNLFAGKFS RCIDTSNNPF
     SVVNSTIVNN KSECRNQNHT GHFFWVNVKV NFDNVAMGYL ALLQVATFKG WMDIMYAAVD
     SREINSQPQW EDNLYMYLYF VVFIIFGGFF TLNLFVGVII DNFNQQKKKL GGQDIFMTEE
     QKKYYNAMKK LGSKKPQKPI PRPLNKYQGF VFDIVTRQAF DIIIMVLICL NMITMMVETD
     GQSEEKTKIL GRINQFFVAV FTGECVMKMF ALRQYYFTNG WNVFDFIVVI LSIGSLVFSA
     ILKSLESYFS PTLFRVIRLA RIGRILRLIR AAKGIRTLLF ALMMSLPALF NIGLLLFLVM
     FIYSIFGMAS FANVVEEAGI DDMFNFQTFG NSMLCLFQIT TSAGWDGLLS PILNTGPPYC
     DPNLSNNNTS KGNCGSPTVG IVFFTTYIII SFLIVVNMYI AVILENFNVA TEESTEPLSE
     DDFDMFYETW EKFDPEATQF IAFSALSDFA DTLSGPLRIP KPNQNILIQM DLPLVPGDKI
     HCLDILFAFT KNVLGESGEL DSLKTNMEEK FMATNLSKAS YEPIATTLRW KQEDISATVI
     QKAYRSYVLQ RSLTLSNPLR VPRAEDDDAP LPGEGYVTFM ANDSGRLPDK SETTSATSFP
     PSYDSVTRGL SDRVNISTSN SMHNEDEVTS KEGDSPGPQ
//