ID SOX2_MOUSE Reviewed; 319 AA. AC P48432; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 27-MAR-2024, entry version 173. DE RecName: Full=Transcription factor SOX-2; GN Name=Sox2; Synonyms=Sox-2; 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], AND TISSUE SPECIFICITY. RX PubMed=7590241; DOI=10.1101/gad.9.21.2635; RA Yuan H., Corbi N., Basilico C., Dailey L.; RT "Developmental-specific activity of the FGF-4 enhancer requires the RT synergistic action of Sox2 and Oct-3."; RL Genes Dev. 9:2635-2645(1995). RN [2] RP SEQUENCE REVISION. RA Yuan H., Corbi N., Basilico C., Dailey L.; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129; RX PubMed=8625802; DOI=10.1242/dev.122.2.509; RA Collignon J., Sockanathan S., Hacker A., Cohen-Tannoudji M., Norris D., RA Rastan S., Stevanovic M., Goodfellow P.N., Lovell-Badge R.; RT "A comparison of the properties of Sox-3 with Sry and two related genes, RT Sox-1 and Sox-2."; RL Development 122:509-520(1996). RN [4] RP FUNCTION, INTERACTION WITH POU5F1, TISSUE SPECIFICITY, AND DISRUPTION RP PHENOTYPE. RX PubMed=15863505; DOI=10.1074/jbc.m501423200; RA Maruyama M., Ichisaka T., Nakagawa M., Yamanaka S.; RT "Differential roles for Sox15 and Sox2 in transcriptional control in mouse RT embryonic stem cells."; RL J. Biol. Chem. 280:24371-24379(2005). RN [5] RP SUMOYLATION AT LYS-247, MUTAGENESIS OF LYS-247, SUBCELLULAR LOCATION, AND RP FUNCTION. RX PubMed=17097055; DOI=10.1016/j.bbrc.2006.10.130; RA Tsuruzoe S., Ishihara K., Uchimura Y., Watanabe S., Sekita Y., Aoto T., RA Saitoh H., Yuasa Y., Niwa H., Kawasuji M., Baba H., Nakao M.; RT "Inhibition of DNA binding of Sox2 by the SUMO conjugation."; RL Biochem. Biophys. Res. Commun. 351:920-926(2006). RN [6] RP BIOTECHNOLOGY. RX PubMed=16904174; DOI=10.1016/j.cell.2006.07.024; RA Takahashi K., Yamanaka S.; RT "Induction of pluripotent stem cells from mouse embryonic and adult RT fibroblast cultures by defined factors."; RL Cell 126:663-676(2006). RN [7] RP INTERACTION WITH SOX3 AND FGFR1. RX PubMed=17728342; DOI=10.1242/dev.007906; RA Rizzoti K., Lovell-Badge R.; RT "SOX3 activity during pharyngeal segmentation is required for craniofacial RT morphogenesis."; RL Development 134:3437-3448(2007). RN [8] RP FUNCTION, AND INTERACTION WITH ZSCAN10. RX PubMed=19740739; DOI=10.1074/jbc.m109.016162; RA Yu H.B., Kunarso G., Hong F.H., Stanton L.W.; RT "Zfp206, Oct4, and Sox2 are integrated components of a transcriptional RT regulatory network in embryonic stem cells."; RL J. Biol. Chem. 284:31327-31335(2009). RN [9] RP SUBCELLULAR LOCATION. RX PubMed=19349578; DOI=10.1083/jcb.200810106; RA Gontan C., Guettler T., Engelen E., Demmers J., Fornerod M., Grosveld F.G., RA Tibboel D., Goerlich D., Poot R.A., Rottier R.J.; RT "Exportin 4 mediates a novel nuclear import pathway for Sox family RT transcription factors."; RL J. Cell Biol. 185:27-34(2009). RN [10] RP FUNCTION, AND INDUCTION. RX PubMed=22198669; DOI=10.1038/nature10712; RA Andreu-Agullo C., Maurin T., Thompson C.B., Lai E.C.; RT "Ars2 maintains neural stem-cell identity through direct transcriptional RT activation of Sox2."; RL Nature 481:195-198(2012). RN [11] RP INTERACTION WITH PHF20L1. RX PubMed=29358331; DOI=10.1074/jbc.ra117.000342; RA Zhang C., Hoang N., Leng F., Saxena L., Lee L., Alejo S., Qi D., Khal A., RA Sun H., Lu F., Zhang H.; RT "LSD1 demethylase and the methyl-binding protein PHF20L1 prevent SET7 RT methyltransferase-dependent proteolysis of the stem-cell protein SOX2."; RL J. Biol. Chem. 293:3663-3674(2018). RN [12] RP INTERACTION WITH L3MBTL3; DCAF5 AND RCOR1. RX PubMed=30442713; DOI=10.1074/jbc.ra118.005336; RA Zhang C., Leng F., Saxena L., Hoang N., Yu J., Alejo S., Lee L., Qi D., RA Lu F., Sun H., Zhang H.; RT "Proteolysis of methylated SOX2 protein is regulated by L3MBTL3 and CRL4- RT DCAF5 ubiquitin ligase."; RL J. Biol. Chem. 294:476-489(2019). RN [13] RP DEVELOPMENTAL STAGE. RX PubMed=32758484; DOI=10.1016/j.ydbio.2020.07.016; RA Simonson L., Vold S., Mowers C., Massey R.J., Ong I.M., Longley B.J., RA Chang H.; RT "Keratin 13 deficiency causes white sponge nevus in mice."; RL Dev. Biol. 468:146-153(2020). RN [14] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=32127020; DOI=10.1186/s13041-020-00570-z; RA Miwa T., Ohta K., Ito N., Hattori S., Miyakawa T., Takeo T., Nakagata N., RA Song W.J., Minoda R.; RT "Tsukushi is essential for the development of the inner ear."; RL Mol. Brain 13:29-29(2020). RN [15] RP FUNCTION, AND INTERACTION WITH DDX56. RX PubMed=32703285; DOI=10.1186/s13287-020-01800-w; RA Wang J., Liu J., Ye M., Liu F., Wu S., Huang J., Shi G.; RT "Ddx56 maintains proliferation of mouse embryonic stem cells via ribosome RT assembly and interaction with the Oct4/Sox2 complex."; RL Stem Cell Res Ther 11:314-314(2020). CC -!- FUNCTION: Transcription factor that forms a trimeric complex with CC POU5F1 (OCT3/4) on DNA and controls the expression of a number of genes CC involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206 CC (PubMed:15863505, PubMed:17097055, PubMed:19740739, PubMed:32703285). CC Binds to the proximal enhancer region of NANOG (PubMed:15863505). CC Critical for early embryogenesis and for embryonic stem cell CC pluripotency (By similarity). Downstream SRRT target that mediates the CC promotion of neural stem cell self-renewal (PubMed:22198669). Keeps CC neural cells undifferentiated by counteracting the activity of CC proneural proteins and suppresses neuronal differentiation (By CC similarity). May function as a switch in neuronal development (By CC similarity). {ECO:0000250|UniProtKB:P48430, CC ECO:0000250|UniProtKB:P48431, ECO:0000269|PubMed:15863505, CC ECO:0000269|PubMed:17097055, ECO:0000269|PubMed:19740739, CC ECO:0000269|PubMed:22198669}. CC -!- SUBUNIT: Interacts with ZSCAN10 (PubMed:19740739). Interacts with SOX3 CC and FGFR1 (PubMed:17728342). Interacts with GLIS1 (By similarity). CC Interacts with POU5F1; binds synergistically with POU5F1 to DNA CC (PubMed:15863505). Interacts with DDX56 (PubMed:32703285). Interacts CC with L3MBTL3 and DCAF5 (PubMed:30442713). The interaction with L3MBTL3 CC and DCAF5 requires methylation at Lys-44 and is necessary to target CC SOX2 for ubiquitination by the CRL4-DCAF5 E3 ubiquitin ligase complex CC (By similarity). Interacts with RCOR1/CoREST (PubMed:30442713). CC Interacts with PHF20L1 (PubMed:29358331). The interaction with PHF20L1 CC requires methylation at Lys-44 and Lys-119 and protects SOX2 from CC degradation (By similarity). Interacts with TRIM26; this interaction CC prevents ubiquitination by WWP2 (By similarity). CC {ECO:0000250|UniProtKB:P48431, ECO:0000269|PubMed:15863505, CC ECO:0000269|PubMed:17728342, ECO:0000269|PubMed:19740739, CC ECO:0000269|PubMed:29358331, ECO:0000269|PubMed:30442713, CC ECO:0000269|PubMed:32703285}. CC -!- INTERACTION: CC P48432; Q80Z64: Nanog; NbExp=10; IntAct=EBI-2313612, EBI-2312517; CC P48432; P20263: Pou5f1; NbExp=4; IntAct=EBI-2313612, EBI-1606219; CC P48432; Q60520: Sin3a; NbExp=3; IntAct=EBI-2313612, EBI-349034; CC P48432; Q00899: Yy1; NbExp=2; IntAct=EBI-2313612, EBI-6921536; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, CC ECO:0000269|PubMed:17097055, ECO:0000269|PubMed:19349578, CC ECO:0000269|PubMed:32127020}. Cytoplasm {ECO:0000269|PubMed:19349578}. CC Note=Nuclear import is facilitated by XPO4, a protein that usually acts CC as a nuclear export signal receptor. {ECO:0000269|PubMed:19349578}. CC -!- TISSUE SPECIFICITY: Expressed in the cochlea (at protein level) CC (PubMed:32127020). Expressed in the brain and retina (PubMed:7590241, CC PubMed:15863505). A very low level of expression is seen in the stomach CC and lung (PubMed:7590241, PubMed:15863505). Expressed in the kidney CC (PubMed:15863505). {ECO:0000269|PubMed:15863505, CC ECO:0000269|PubMed:32127020, ECO:0000269|PubMed:7590241}. CC -!- DEVELOPMENTAL STAGE: Expressed in the basal cells of the tongue CC epithelium at birth until P20 (PubMed:32758484). Expressed in the CC suprabasal cells of the buccal mucosa and esophagus at P20 CC (PubMed:32758484). {ECO:0000269|PubMed:32758484}. CC -!- INDUCTION: By SRRT. {ECO:0000269|PubMed:22198669}. CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large CC number of yeast and animal transcription factors. CC {ECO:0000250|UniProtKB:P41225}. CC -!- PTM: Sumoylation inhibits binding on DNA and negatively regulates the CC FGF4 transactivation. {ECO:0000269|PubMed:17097055}. CC -!- PTM: Methylation at Lys-44 and Lys-119 is necessary for the regulation CC of SOX2 proteasomal degradation. {ECO:0000250|UniProtKB:P48431}. CC -!- PTM: Ubiquitinated by WWP2, leading to proteasomal degradation. CC {ECO:0000250|UniProtKB:P48431}. CC -!- DISRUPTION PHENOTYPE: Embryonically lethal. CC {ECO:0000269|PubMed:15863505}. CC -!- BIOTECHNOLOGY: POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four CC Yamanaka factors. When combined, these factors are sufficient to CC reprogram differentiated cells to an embryonic-like state designated CC iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology CC and growth properties of ES cells and express ES cell marker genes. CC {ECO:0000269|PubMed:16904174}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U31967; AAC31791.1; -; mRNA. DR EMBL; X94127; CAA63847.1; -; Genomic_DNA. DR CCDS; CCDS38413.1; -. DR PIR; S10949; S10949. DR RefSeq; NP_035573.3; NM_011443.4. DR PDB; 1GT0; X-ray; 2.60 A; D=41-120. DR PDB; 6HT5; X-ray; 3.45 A; D=41-120. DR PDBsum; 1GT0; -. DR PDBsum; 6HT5; -. DR AlphaFoldDB; P48432; -. DR BMRB; P48432; -. DR SMR; P48432; -. DR BioGRID; 203406; 141. DR DIP; DIP-54522N; -. DR IntAct; P48432; 11. DR MINT; P48432; -. DR STRING; 10090.ENSMUSP00000096755; -. DR GlyGen; P48432; 6 sites, 1 O-linked glycan (6 sites). DR iPTMnet; P48432; -. DR PhosphoSitePlus; P48432; -. DR MaxQB; P48432; -. DR PaxDb; 10090-ENSMUSP00000096755; -. DR PeptideAtlas; P48432; -. DR ProteomicsDB; 261480; -. DR DNASU; 20674; -. DR GeneID; 20674; -. DR KEGG; mmu:20674; -. DR AGR; MGI:98364; -. DR CTD; 6657; -. DR MGI; MGI:98364; Sox2. DR eggNOG; KOG0527; Eukaryota. DR InParanoid; P48432; -. DR OrthoDB; 2902801at2759; -. DR PhylomeDB; P48432; -. DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex. DR BioGRID-ORCS; 20674; 2 hits in 78 CRISPR screens. DR EvolutionaryTrace; P48432; -. DR PRO; PR:P48432; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P48432; Protein. DR GO; GO:0000785; C:chromatin; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0035198; F:miRNA binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0021984; P:adenohypophysis development; IMP:MGI. DR GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IMP:MGI. DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0045165; P:cell fate commitment; IDA:MGI. DR GO; GO:0001708; P:cell fate specification; IMP:MGI. DR GO; GO:0071276; P:cellular response to cadmium ion; IDA:MGI. DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI. DR GO; GO:0050973; P:detection of mechanical stimulus involved in equilibrioception; IMP:MGI. DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:MGI. DR GO; GO:0048852; P:diencephalon morphogenesis; IMP:MGI. DR GO; GO:0048568; P:embryonic organ development; IMP:MGI. DR GO; GO:0001714; P:endodermal cell fate specification; ISO:MGI. DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IDA:MGI. DR GO; GO:0021879; P:forebrain neuron differentiation; IMP:MGI. DR GO; GO:0010467; P:gene expression; IMP:MGI. DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI. DR GO; GO:0060235; P:lens induction in camera-type eye; IGI:MGI. DR GO; GO:0048286; P:lung alveolus development; IDA:MGI. DR GO; GO:0030539; P:male genitalia development; IMP:MGI. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; ISO:MGI. DR GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI. DR GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:MGI. DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IGI:MGI. DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI. DR GO; GO:0030182; P:neuron differentiation; IDA:MGI. DR GO; GO:0048663; P:neuron fate commitment; IMP:MGI. DR GO; GO:0097150; P:neuronal stem cell population maintenance; IGI:UniProtKB. DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI. DR GO; GO:0030910; P:olfactory placode formation; IGI:MGI. DR GO; GO:0001649; P:osteoblast differentiation; IDA:MGI. DR GO; GO:0046148; P:pigment biosynthetic process; IMP:MGI. DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI. DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IDA:MGI. DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI. DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:MGI. DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI. DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:CACAO. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI. DR GO; GO:1904520; P:regulation of myofibroblast cell apoptotic process; ISO:MGI. DR GO; GO:0050767; P:regulation of neurogenesis; IGI:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0070848; P:response to growth factor; ISO:MGI. DR GO; GO:0010033; P:response to organic substance; IDA:MGI. DR GO; GO:0090649; P:response to oxygen-glucose deprivation; ISO:MGI. DR GO; GO:0032526; P:response to retinoic acid; IDA:MGI. DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:MGI. DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI. DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI. DR GO; GO:0048863; P:stem cell differentiation; IDA:MGI. DR GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB. DR GO; GO:0043586; P:tongue development; IMP:MGI. DR GO; GO:0001829; P:trophectodermal cell differentiation; IMP:MGI. DR GO; GO:0016055; P:Wnt signaling pathway; IGI:MGI. DR CDD; cd01388; HMG-box_SoxB; 1. DR Gene3D; 1.10.30.10; High mobility group box domain; 1. DR IDEAL; IID50261; -. DR InterPro; IPR009071; HMG_box_dom. DR InterPro; IPR036910; HMG_box_dom_sf. DR InterPro; IPR022097; SOX_fam. DR PANTHER; PTHR10270; SOX TRANSCRIPTION FACTOR; 1. DR PANTHER; PTHR10270:SF231; TRANSCRIPTION FACTOR SOX-2; 1. DR Pfam; PF00505; HMG_box; 1. DR Pfam; PF12336; SOXp; 1. DR SMART; SM00398; HMG; 1. DR SUPFAM; SSF47095; HMG-box; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; Cytoplasm; Developmental protein; DNA-binding; KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..319 FT /note="Transcription factor SOX-2" FT /id="PRO_0000048716" FT DNA_BIND 43..111 FT /note="HMG box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 247..267 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 299..319 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 274..282 FT /note="9aaTAD" FT /evidence="ECO:0000250|UniProtKB:P41225" FT COMPBIAS 247..266 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 44 FT /note="N6-methyllysine" FT /evidence="ECO:0000250|UniProtKB:P48431" FT MOD_RES 119 FT /note="N6-methyllysine" FT /evidence="ECO:0000250|UniProtKB:P48431" FT MOD_RES 253 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48431" FT CROSSLNK 247 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT MUTAGEN 247 FT /note="K->R: Absence of sumoylation. Increased FGF4 FT activation. No effect on nuclear localization." FT /evidence="ECO:0000269|PubMed:17097055" FT CONFLICT 153..155 FT /note="GGL -> AGV (in Ref. 3; CAA63847)" FT /evidence="ECO:0000305" FT CONFLICT 203 FT /note="V -> D (in Ref. 3; CAA63847)" FT /evidence="ECO:0000305" FT CONFLICT 310..311 FT /note="KY -> IN (in Ref. 3; CAA63847)" FT /evidence="ECO:0000305" FT HELIX 49..62 FT /evidence="ECO:0007829|PDB:1GT0" FT HELIX 70..81 FT /evidence="ECO:0007829|PDB:1GT0" FT HELIX 86..106 FT /evidence="ECO:0007829|PDB:1GT0" SQ SEQUENCE 319 AA; 34454 MW; C40DE49E524C49F1 CRC64; MYNMMETELK PPGPQQASGG GGGGGNATAA ATGGNQKNSP DRVKRPMNAF MVWSRGQRRK MAQENPKMHN SEISKRLGAE WKLLSETEKR PFIDEAKRLR ALHMKEHPDY KYRPRRKTKT LMKKDKYTLP GGLLAPGGNS MASGVGVGAG LGGGLNQRMD SYAHMNGWSN GSYSMMQEQL GYPQHPGLNA HGAAQMQPMH RYVVSALQYN SMTSSQTYMN GSPTYSMSYS QQGTPGMALG SMGSVVKSEA SSSPPVVTSS SHSRAPCQAG DLRDMISMYL PGAEVPEPAA PSRLHMAQHY QSGPVPGTAK YGTLPLSHM //