SOS1_MOUSE
ID SOS1_MOUSE Reviewed; 1319 AA.
AC Q62245; Q62244;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Son of sevenless homolog 1;
DE Short=SOS-1;
DE Short=mSOS-1;
GN Name=Sos1;
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 [MRNA].
RC STRAIN=SWR/J; TISSUE=Eye;
RX PubMed=1631150; DOI=10.1073/pnas.89.14.6511;
RA Bowtell D.D., Fu P., Simon M.A., Senior P.V.;
RT "Identification of murine homologues of the Drosophila son of sevenless
RT gene: potential activators of ras.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6511-6515(1992).
RN [2]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH ABI1 AND EPS8E.
RX PubMed=10499589; DOI=10.1038/45822;
RA Scita G., Nordstrom J., Carbone R., Tenca P., Giardina G., Gutkind S.,
RA Bjarnegard M., Betsholtz C., Di Fiore P.P.;
RT "EPS8 and E3B1 transduce signals from Ras to Rac.";
RL Nature 401:290-293(1999).
RN [3]
RP FUNCTION, AND INTERACTION WITH EPS8.
RX PubMed=11524436; DOI=10.1083/jcb.200103146;
RA Scita G., Tenca P., Areces L.B., Tocchetti A., Frittoli E., Giardina G.,
RA Ponzanelli I., Sini P., Innocenti M., Di Fiore P.P.;
RT "An effector region in Eps8 is responsible for the activation of the Rac-
RT specific GEF activity of Sos-1 and for the proper localization of the Rac-
RT based actin-polymerizing machine.";
RL J. Cell Biol. 154:1031-1044(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1078 AND SER-1082, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1082 AND SER-1261, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP STRUCTURE BY NMR OF 415-548.
RX PubMed=9217262; DOI=10.1006/jmbi.1997.1041;
RA Koshiba S., Kigawa T., Kim J.-H., Shirouzu M., Bowtell D., Yokoyama S.;
RT "The solution structure of the pleckstrin homology domain of mouse Son-of-
RT sevenless 1 (mSos1).";
RL J. Mol. Biol. 269:579-591(1997).
CC -!- FUNCTION: Promotes the exchange of Ras-bound GDP by GTP. Probably by
CC promoting Ras activation, regulates phosphorylation of MAP kinase MAPK3
CC in response to EGF (By similarity). Catalytic component of a trimeric
CC complex that participates in transduction of signals from Ras to Rac by
CC promoting the Rac-specific guanine nucleotide exchange factor (GEF)
CC activity (PubMed:10499589, PubMed:11524436).
CC {ECO:0000250|UniProtKB:Q07889, ECO:0000269|PubMed:10499589,
CC ECO:0000269|PubMed:11524436}.
CC -!- SUBUNIT: Interacts (via C-terminus) with GRB2 (via SH3 domain). Forms a
CC complex with phosphorylated MUC1 and GRB2 (via its SH3 domains).
CC Interacts with phosphorylated LAT2. Interacts with NCK1 and NCK2 (By
CC similarity). Part of a complex consisting of ABI1, EPS8 and SOS1
CC (PubMed:10499589, PubMed:11524436). Interacts (Ser-1120 and Ser-1147
CC phosphorylated form) with YWHAB and YWHAE (By similarity).
CC {ECO:0000250|UniProtKB:Q07889, ECO:0000269|PubMed:10499589,
CC ECO:0000269|PubMed:11524436}.
CC -!- INTERACTION:
CC Q62245; Q60631: Grb2; NbExp=7; IntAct=EBI-1693, EBI-1688;
CC Q62245; P62993: GRB2; Xeno; NbExp=4; IntAct=EBI-1693, EBI-401755;
CC Q62245; P62993-1: GRB2; Xeno; NbExp=2; IntAct=EBI-1693, EBI-15787932;
CC Q62245; P29355: sem-5; Xeno; NbExp=2; IntAct=EBI-1693, EBI-315286;
CC Q62245; P26663; Xeno; NbExp=2; IntAct=EBI-1693, EBI-6857429;
CC -!- TISSUE SPECIFICITY: Expressed in most embryonic and adult tissues.
CC -!- PTM: Phosphorylation at Ser-1120 and Ser-1147 by RPS6KA3 create YWHAB
CC and YWHAE binding sites and which contribute to the negative regulation
CC of EGF-induced MAPK1/3 phosphorylation. {ECO:0000250|UniProtKB:Q07889}.
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DR EMBL; Z11574; CAA77662.1; -; mRNA.
DR EMBL; Z11578; CAA77665.1; -; mRNA.
DR CCDS; CCDS37704.1; -.
DR PIR; S25715; S25715.
DR PIR; S25716; S25716.
DR RefSeq; NP_033257.2; NM_009231.2.
DR PDB; 1B07; X-ray; 2.50 A; C=1135-1144.
DR PDB; 1GBQ; NMR; -; B=1135-1144.
DR PDB; 1PMS; NMR; -; A=414-548.
DR PDB; 2GBQ; NMR; -; B=1135-1144.
DR PDB; 3GBQ; NMR; -; B=1135-1144.
DR PDB; 4GBQ; NMR; -; B=1135-1144.
DR PDBsum; 1B07; -.
DR PDBsum; 1GBQ; -.
DR PDBsum; 1PMS; -.
DR PDBsum; 2GBQ; -.
DR PDBsum; 3GBQ; -.
DR PDBsum; 4GBQ; -.
DR AlphaFoldDB; Q62245; -.
DR SMR; Q62245; -.
DR BioGRID; 203394; 41.
DR ComplexPortal; CPX-413; GTPase Hras - Son of sevenless homolog 1 complex.
DR CORUM; Q62245; -.
DR DIP; DIP-29230N; -.
DR IntAct; Q62245; 19.
DR MINT; Q62245; -.
DR STRING; 10090.ENSMUSP00000067786; -.
DR ChEMBL; CHEMBL4523334; -.
DR iPTMnet; Q62245; -.
DR PhosphoSitePlus; Q62245; -.
DR EPD; Q62245; -.
DR jPOST; Q62245; -.
DR MaxQB; Q62245; -.
DR PaxDb; Q62245; -.
DR PRIDE; Q62245; -.
DR ProteomicsDB; 261551; -.
DR Antibodypedia; 2769; 244 antibodies from 36 providers.
DR DNASU; 20662; -.
DR Ensembl; ENSMUST00000068714; ENSMUSP00000067786; ENSMUSG00000024241.
DR GeneID; 20662; -.
DR KEGG; mmu:20662; -.
DR UCSC; uc008drg.1; mouse.
DR CTD; 6654; -.
DR MGI; MGI:98354; Sos1.
DR VEuPathDB; HostDB:ENSMUSG00000024241; -.
DR eggNOG; KOG3417; Eukaryota.
DR GeneTree; ENSGT00940000155423; -.
DR HOGENOM; CLU_002744_0_0_1; -.
DR InParanoid; Q62245; -.
DR OMA; YDVENIF; -.
DR OrthoDB; 576110at2759; -.
DR PhylomeDB; Q62245; -.
DR TreeFam; TF317296; -.
DR Reactome; R-MMU-112412; SOS-mediated signalling.
DR Reactome; R-MMU-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-1433559; Regulation of KIT signaling.
DR Reactome; R-MMU-167044; Signalling to RAS.
DR Reactome; R-MMU-179812; GRB2 events in EGFR signaling.
DR Reactome; R-MMU-180336; SHC1 events in EGFR signaling.
DR Reactome; R-MMU-186763; Downstream signal transduction.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-MMU-210993; Tie2 Signaling.
DR Reactome; R-MMU-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-MMU-2424491; DAP12 signaling.
DR Reactome; R-MMU-2428933; SHC-related events triggered by IGF1R.
DR Reactome; R-MMU-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-MMU-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-MMU-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-MMU-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-MMU-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-MMU-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-MMU-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-MMU-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-MMU-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-74749; Signal attenuation.
DR Reactome; R-MMU-74751; Insulin receptor signalling cascade.
DR Reactome; R-MMU-8851805; MET activates RAS signaling.
DR Reactome; R-MMU-8853659; RET signaling.
DR Reactome; R-MMU-8983432; Interleukin-15 signaling.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9028731; Activated NTRK2 signals through FRS2 and FRS3.
DR Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
DR Reactome; R-MMU-9607240; FLT3 Signaling.
DR Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR BioGRID-ORCS; 20662; 12 hits in 74 CRISPR screens.
DR ChiTaRS; Sos1; mouse.
DR EvolutionaryTrace; Q62245; -.
DR PRO; PR:Q62245; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q62245; protein.
DR Bgee; ENSMUSG00000024241; Expressed in medial preoptic region and 235 other tissues.
DR Genevisible; Q62245; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:1905360; C:GTPase complex; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0001782; P:B cell homeostasis; IGI:MGI.
DR GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0003209; P:cardiac atrium morphogenesis; IMP:MGI.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IGI:MGI.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:MGI.
DR GO; GO:0001942; P:hair follicle development; IGI:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0061384; P:heart trabecula morphogenesis; IMP:MGI.
DR GO; GO:0002260; P:lymphocyte homeostasis; IGI:MGI.
DR GO; GO:1904693; P:midbrain morphogenesis; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISO:MGI.
DR GO; GO:0003344; P:pericardium morphogenesis; IMP:MGI.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; TAS:ARUK-UCL.
DR GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; ISO:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0043405; P:regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:2000973; P:regulation of pro-B cell differentiation; IGI:MGI.
DR GO; GO:0033081; P:regulation of T cell differentiation in thymus; IGI:MGI.
DR GO; GO:0042129; P:regulation of T cell proliferation; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IMP:MGI.
DR GO; GO:0007296; P:vitellogenesis; IMP:MGI.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Guanine-nucleotide releasing factor; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1319
FT /note="Son of sevenless homolog 1"
FT /id="PRO_0000068895"
FT DOMAIN 200..390
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 444..548
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 597..741
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 780..1019
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 1019..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1147
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1257
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1078
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 1082
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1120
FT /note="Phosphoserine; by RPS6KA3"
FT /evidence="ECO:0000250|UniProtKB:Q07889"
FT MOD_RES 1147
FT /note="Phosphoserine; by RPS6KA3"
FT /evidence="ECO:0000250|UniProtKB:Q07889"
FT MOD_RES 1164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07889"
FT MOD_RES 1196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07889"
FT MOD_RES 1215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07889"
FT MOD_RES 1261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:1PMS"
FT HELIX 419..427
FT /evidence="ECO:0007829|PDB:1PMS"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:1PMS"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:1PMS"
FT STRAND 446..454
FT /evidence="ECO:0007829|PDB:1PMS"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:1PMS"
FT STRAND 465..471
FT /evidence="ECO:0007829|PDB:1PMS"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:1PMS"
FT STRAND 490..495
FT /evidence="ECO:0007829|PDB:1PMS"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:1PMS"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:1PMS"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:1PMS"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:1PMS"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:1PMS"
FT HELIX 532..545
FT /evidence="ECO:0007829|PDB:1PMS"
SQ SEQUENCE 1319 AA; 150883 MW; 3286088A5BA0A4A6 CRC64;
MQAQQLPYEF FSEENAPKWR GLLVPALKKV QGQVHPTLES NDDALQYVEE LILQLLNMLC
QAQPRSASDV EERVQKSFPH PIDKWAIADA QSAIEKRKRR NPLSLPAERI HHLLREVLGY
KIDHQVSVYI VAVLEYISAD ILKLVGNYVR NIRHYEITKQ DIKVAMCADK VLMDMFHQDV
EDINILSLTD EEPSTSGEQT YYDLVKAFMA EIRQYIRELN LIIKVFREPF VSNSKLFSSN
DVENIFSRIV DIHELSVKLL GHIEDTVEMT DEGSPHPLVG SCFEDLAEEL AFDPYESYAR
DILRPGFHGH FLSQLSKPGA ALYLQSIGEG FKEAVQYVLP RLLLAPVYHC LHYFELLKQL
EEKSEDQEDK ECMKQAITAL LNVQSGMEKI CSKSLAKRRL SESACRFYSQ QMKGKQLAIK
KMNEIQKNID GWEGKDIGQC CNEFIMEGTL TRVGAKHERH IFLFDGLMIC CKSNHGQPRL
PGASSAEYRL KEKFFMRKVQ INDKDDTSEY KHAFEIILKD GNSVIFSAKS AEEKNNWMAA
LISLQYRSTL ERMLDVTVLQ EEKEEQMRLP SAEVYRFAEP DSEENILFEE NVQPKAGIPI
IKAGTVLKLI ERLTYHMYAD PNFVRTFLTT YRSFCRPQEL LSLLIERFEI PEPEPTEADR
IAIENGDQPL SAELKRFRKE YIQPVQLRVL NVCRHWVEHH FYDFERDADL LQRMEEFIGT
VRGKAMKKWV ESITKIIQRK KIARDNGPGH NITFQSSPPT VEWHISRPGH IETFDLLTLH
PIEIARQLTL LESDLYRAVQ PSELVGSVWT KEDKEINSPN LLKMIRHTTN LTLWFEKCIV
ETENLEERVA VVSRIIEILQ VFQELNNFNG VLEVVSAMNS SPVYRLDHTF EQIPSRQKKI
LEEAHELSED HYKKYLAKLR SINPPCVPFF GIYLTNILKT EEGNPEVLRR HGKELINFSK
RRRVAEITGE IQQYQNQPYC LRVEPDIKRF FENLNPMGNS MEKEFTDYLF NKSLEIEPRH
PKPLPRFPKK YSYPLKSPGV RPSNPRPGTM RHPTPLQQEP RKISYSRIPE SETESTASAP
NSPRTPLTPP PASGTSSNTD VCSVFDSDHS ASPFHSRSAS VSSISLSKGT DEVPVPPPVP
PRRRPESAPA ESSPSKIMSK HLDSPPAIPP RQPTSKAYSP RYSISDRTSI SDPPESPPLL
PPREPVRTPD VFSSSPLHLQ PPPLGKKSDH GNAFFPNSPS PFTPPPPQTP SPHGTRRHLP
SPPLTQEMDL HSIAGPPVPP RQSTSQLIPK LPPKTYKREH THPSMHRDGP PLLENAHSS
