ID GYS2_MOUSE Reviewed; 704 AA. AC Q8VCB3; Q3UTY0; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 27-MAR-2024, entry version 135. DE RecName: Full=Glycogen [starch] synthase, liver {ECO:0000305|PubMed:24982189}; DE EC=2.4.1.11 {ECO:0000269|PubMed:24982189}; DE AltName: Full=Glycogen synthase 2 {ECO:0000312|MGI:MGI:2385254}; GN Name=Gys2 {ECO:0000312|MGI:MGI:2385254}; 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 [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684, AND IDENTIFICATION BY RP 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 [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity RT chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Kidney, and Liver; 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 [6] RP INDUCTION. RX PubMed=20430893; DOI=10.1074/jbc.m110.110361; RA Doi R., Oishi K., Ishida N.; RT "CLOCK regulates circadian rhythms of hepatic glycogen synthesis through RT transcriptional activation of Gys2."; RL J. Biol. Chem. 285:22114-22121(2010). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, RP INTERACTION WITH GYG1, AND MUTAGENESIS OF SER-8; TRP-135; GLY-141; TYR-239; RP CYS-243 AND GLU-510. RX PubMed=24982189; DOI=10.1073/pnas.1402926111; RA Zeqiraj E., Tang X., Hunter R.W., Garcia-Rocha M., Judd A., Deak M., RA von Wilamowitz-Moellendorff A., Kurinov I., Guinovart J.J., Tyers M., RA Sakamoto K., Sicheri F.; RT "Structural basis for the recruitment of glycogen synthase by glycogenin."; RL Proc. Natl. Acad. Sci. U.S.A. 111:E2831-2840(2014). CC -!- FUNCTION: Glycogen synthase participates in the glycogen biosynthetic CC process along with glycogenin and glycogen branching enzyme. Extends CC the primer composed of a few glucose units formed by glycogenin by CC adding new glucose units to it. In this context, glycogen synthase CC transfers the glycosyl residue from UDP-Glc to the non-reducing end of CC alpha-1,4-glucan. {ECO:0000269|PubMed:24982189}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)- CC alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:18549, Rhea:RHEA- CC COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.11; CC Evidence={ECO:0000269|PubMed:24982189}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18550; CC Evidence={ECO:0000269|PubMed:24982189}; CC -!- ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate. CC Phosphorylation reduces the activity towards UDP-glucose. When in the CC non-phosphorylated state, glycogen synthase does not require glucose-6- CC phosphate as an allosteric activator; when phosphorylated it does (By CC similarity). {ECO:0000250|UniProtKB:P13834, CC ECO:0000250|UniProtKB:P54840}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.48 mM for UDP-glucose (at 30 degrees Celsius) CC {ECO:0000269|PubMed:24982189}; CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC {ECO:0000269|PubMed:24982189}. CC -!- SUBUNIT: Part of the glycogen synthase (GS)-glycogenin complex, a CC heterooctamer composed of a tetramer of GS and 2 dimers of glycogenin, CC where each GS protomer binds to one glycogenin subunit (via glycogenin CC C-terminus); the GS tetramer may dissociate from glycogenin dimers to CC continue glycogen polymerization on its own (By similarity). May also CC form a heterooctamer complex with GYG1 (via GYG1 C-terminus) CC (Probable). {ECO:0000250|UniProtKB:P13807, CC ECO:0000305|PubMed:24982189}. CC -!- TISSUE SPECIFICITY: Specifically expressed in liver. {ECO:0000305}. CC -!- INDUCTION: Expression in the liver oscillates in a circadian manner CC with peak levels during the night. {ECO:0000269|PubMed:20430893}. CC -!- PTM: Phosphorylation reduces the activity towards UDP-alpha-D-glucose CC (By similarity). Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 CC and CSNK2A2 is required for inhibitory phosphorylation at Ser-641 (site CC 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A CC an GSK3B (By similarity). Dephosphorylation at Ser-641 and Ser-645 by CC PP1 activates the enzyme (By similarity). Phosphorylation at Ser-8 is CC not required for interaction with GYG1 (PubMed:24982189). Interaction CC with GYG1 does not regulate the phosphorylation at Ser-8 and Ser-641 CC (PubMed:24982189). {ECO:0000250|UniProtKB:P13807, CC ECO:0000250|UniProtKB:P13834, ECO:0000250|UniProtKB:P17625, CC ECO:0000250|UniProtKB:P54840, ECO:0000269|PubMed:24982189}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 3 family. {ECO:0000305}. 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; AK138992; BAE23850.1; -; mRNA. DR EMBL; BC021322; AAH21322.1; -; mRNA. DR EMBL; BC158081; AAI58082.1; -; mRNA. DR CCDS; CCDS20683.1; -. DR RefSeq; NP_663547.2; NM_145572.2. DR AlphaFoldDB; Q8VCB3; -. DR SMR; Q8VCB3; -. DR IntAct; Q8VCB3; 1. DR STRING; 10090.ENSMUSP00000032371; -. DR CAZy; GT3; Glycosyltransferase Family 3. DR GlyGen; Q8VCB3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8VCB3; -. DR PhosphoSitePlus; Q8VCB3; -. DR SwissPalm; Q8VCB3; -. DR jPOST; Q8VCB3; -. DR MaxQB; Q8VCB3; -. DR PaxDb; 10090-ENSMUSP00000032371; -. DR PeptideAtlas; Q8VCB3; -. DR ProteomicsDB; 271353; -. DR Antibodypedia; 24071; 130 antibodies from 25 providers. DR DNASU; 232493; -. DR Ensembl; ENSMUST00000032371.8; ENSMUSP00000032371.8; ENSMUSG00000030244.8. DR GeneID; 232493; -. DR KEGG; mmu:232493; -. DR UCSC; uc009epi.2; mouse. DR AGR; MGI:2385254; -. DR CTD; 2998; -. DR MGI; MGI:2385254; Gys2. DR VEuPathDB; HostDB:ENSMUSG00000030244; -. DR eggNOG; KOG3742; Eukaryota. DR GeneTree; ENSGT00390000018612; -. DR HOGENOM; CLU_015910_1_0_1; -. DR InParanoid; Q8VCB3; -. DR OMA; RMHKSNV; -. DR OrthoDB; 9432at2759; -. DR PhylomeDB; Q8VCB3; -. DR TreeFam; TF300306; -. DR UniPathway; UPA00164; -. DR BioGRID-ORCS; 232493; 5 hits in 79 CRISPR screens. DR PRO; PR:Q8VCB3; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; Q8VCB3; Protein. DR Bgee; ENSMUSG00000030244; Expressed in hepatobiliary system and 46 other cell types or tissues. DR ExpressionAtlas; Q8VCB3; baseline and differential. DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB. DR GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005536; F:glucose binding; ISO:MGI. DR GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:MGI. DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:MGI. DR GO; GO:0005977; P:glycogen metabolic process; ISO:MGI. DR GO; GO:0009749; P:response to glucose; ISS:UniProtKB. DR CDD; cd03793; GT3_GSY2-like; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR008631; Glycogen_synth. DR PANTHER; PTHR10176:SF1; GLYCOGEN [STARCH] SYNTHASE, LIVER; 1. DR PANTHER; PTHR10176; GLYCOGEN SYNTHASE; 1. DR Pfam; PF05693; Glycogen_syn; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2. DR Genevisible; Q8VCB3; MM. PE 1: Evidence at protein level; KW Allosteric enzyme; Glycogen biosynthesis; Glycosyltransferase; KW Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1..704 FT /note="Glycogen [starch] synthase, liver" FT /id="PRO_0000274489" FT REGION 620..704 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 657..673 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 690..704 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 40 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 205 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 211 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 291 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 292 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 294 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 297 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 301 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 331 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 331 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 501 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 510 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 512 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 513 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 515 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 582 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /evidence="ECO:0000250|UniProtKB:P13807" FT BINDING 586 FT /ligand="alpha-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58225" FT /ligand_note="allosteric activator; ligand shared between FT two neighboring subunits" FT /evidence="ECO:0000250|UniProtKB:P13807" FT MOD_RES 8 FT /note="Phosphoserine; by AMPK and PKA" FT /evidence="ECO:0000250|UniProtKB:P17625" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 627 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54840" FT MOD_RES 641 FT /note="Phosphoserine; by GSK3-alpha and GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P13834" FT MOD_RES 645 FT /note="Phosphoserine; by GSK3-alpha and GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P13834" FT MOD_RES 649 FT /note="Phosphoserine; by GSK3-alpha and GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P13834" FT MOD_RES 653 FT /note="Phosphoserine; by GSK3-alpha and GSK3-beta" FT /evidence="ECO:0000250|UniProtKB:P13834" FT MOD_RES 657 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000250|UniProtKB:P13834" FT MOD_RES 684 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355" FT MUTAGEN 8 FT /note="S->A: Abolishes phosphorylation. No effect on the FT interaction with GYG1. Does not affect the result of other FT mutations; when associated with A-135; R-135; R-141; A-239; FT A-243; or R-243." FT /evidence="ECO:0000269|PubMed:24982189" FT MUTAGEN 135 FT /note="W->A: No effect on the interaction with GYG1. No FT effect on the interaction with GYG1; when associated with FT A-8." FT /evidence="ECO:0000269|PubMed:24982189" FT MUTAGEN 135 FT /note="W->R: Loss of interaction with GYG1. Loss of FT interaction with GYG1; when associated with A-8." FT /evidence="ECO:0000269|PubMed:24982189" FT MUTAGEN 141 FT /note="G->R: Loss of interaction with GYG1. Loss of FT function. Loss of interaction with GYG1; when associated FT with A-8." FT /evidence="ECO:0000269|PubMed:24982189" FT MUTAGEN 239 FT /note="Y->A: Loss of interaction with GYG1. Loss of FT function. Loss of interaction with GYG1; when associated FT with A-8." FT /evidence="ECO:0000269|PubMed:24982189" FT MUTAGEN 243 FT /note="C->A: No effect on the interaction with GYG1. Loss FT of interaction with GYG1; when associated with A-8." FT /evidence="ECO:0000269|PubMed:24982189" FT MUTAGEN 243 FT /note="C->R: Loss of interaction with GYG1. Loss of FT function. Loss of interaction with GYG1; when associated FT with A-8." FT /evidence="ECO:0000269|PubMed:24982189" FT MUTAGEN 510 FT /note="E->A: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:24982189" FT CONFLICT 630 FT /note="T -> M (in Ref. 2; AAH21322)" FT /evidence="ECO:0000305" FT CONFLICT 656 FT /note="C -> S (in Ref. 2; AAH21322)" FT /evidence="ECO:0000305" SQ SEQUENCE 704 AA; 80871 MW; C4B87195B5FC41FE CRC64; MLRGRSLSVT SLGGLPVWEA ERLPVEDLLL FEVSWEVTNK VGGICTVIQT KAKTTADEWG ENYFLIGPYF EHNMKTQVEQ CEPTNDAVRK AVDAMNKHGC QVHFGRWLIE GSPYVVLFDI SSSAWNLDRW KGDFWEACGV GIPHHDREAN DMLIFGSLTA WFLKEVTDHA DGKHVIAQFH EWQAGTGLIL SRARKLPIAT VFTTHATLLG RYLCAANIDF YNQLDKFDID KEAGERQIYH RYCMERASVH CAHVFTTVSE ITAIEAEHML KRKPDVVTPN GLNVKKFSAV HEFQNLHAMY KARIQDFVRG HFYGHLDFDL EKTLFLFIAG RYEFSNKGAD IFLESLSRLN FLLRMHKSNV TVVVFFIMPA KTNNFNVETL KGQAVRKQLW DTVHCLKEKF GKKLYDGLLR GEIPDMNSIL DRDDLTIMKR AIFSTQRQSL PPVTTHNMID DSTDPILSTI RRIGLFNNRA DRVKVILHPE FLSSTSPLLP MDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSVTTN LSGFGCFVQE HVADPTAYGI YIVDRRFRSP DDSCNQLTQF LYGFCKQSRR QRIIQRNRTE RLSDLLDWRY LGRYYQHARH LTLSRAFPDK FHLEPTSPPT TDGFKYPRPS SVPPSPSGSQ ASSPQCSDAE DEEDEDERYD EEEEAERDRL NIKSPFSLNH FPKGKKKLHG EYKN //