ID GSK3A_MOUSE Reviewed; 490 AA.
AC Q2NL51;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=Glycogen synthase kinase-3 alpha;
DE Short=GSK-3 alpha;
DE EC=2.7.11.26;
DE AltName: Full=Serine/threonine-protein kinase GSK3A;
DE EC=2.7.11.1 {ECO:0000269|PubMed:22539723};
GN Name=Gsk3a;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 227-490.
RC TISSUE=Eye;
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 INTERACTION WITH ARRB2.
RX PubMed=16051150; DOI=10.1016/j.cell.2005.05.012;
RA Beaulieu J.-M., Sotnikova T.D., Marion S., Lefkowitz R.J.,
RA Gainetdinov R.R., Caron M.G.;
RT "An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic
RT neurotransmission and behavior.";
RL Cell 122:261-273(2005).
RN [4]
RP FUNCTION, MUTAGENESIS OF SER-21, AND PHOSPHORYLATION AT SER-21.
RX PubMed=15791206; DOI=10.1038/sj.emboj.7600633;
RA McManus E.J., Sakamoto K., Armit L.J., Ronaldson L., Shpiro N., Marquez R.,
RA Alessi D.R.;
RT "Role that phosphorylation of GSK3 plays in insulin and Wnt signalling
RT defined by knockin analysis.";
RL EMBO J. 24:1571-1583(2005).
RN [5]
RP FUNCTION IN MCL1 PHOSPHORYLATION.
RX PubMed=16543145; DOI=10.1016/j.molcel.2006.02.009;
RA Maurer U., Charvet C., Wagman A.S., Dejardin E., Green D.R.;
RT "Glycogen synthase kinase-3 regulates mitochondrial outer membrane
RT permeabilization and apoptosis by destabilization of MCL-1.";
RL Mol. Cell 21:749-760(2006).
RN [6]
RP FUNCTION IN AXON FORMATION, AND TISSUE SPECIFICITY.
RX PubMed=17391670; DOI=10.1016/j.febslet.2007.03.018;
RA Garrido J.J., Simon D., Varea O., Wandosell F.;
RT "GSK3 alpha and GSK3 beta are necessary for axon formation.";
RL FEBS Lett. 581:1579-1586(2007).
RN [7]
RP FUNCTION IN HEPATIC GLYCOGEN METABOLISM, AND DISRUPTION PHENOTYPE.
RX PubMed=17908561; DOI=10.1016/j.cmet.2007.08.013;
RA MacAulay K., Doble B.W., Patel S., Hansotia T., Sinclair E.M.,
RA Drucker D.J., Nagy A., Woodgett J.R.;
RT "Glycogen synthase kinase 3alpha-specific regulation of murine hepatic
RT glycogen metabolism.";
RL Cell Metab. 6:329-337(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Lung, Spleen, 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 [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22539723; DOI=10.1126/science.1217032;
RA Lin S.Y., Li T.Y., Liu Q., Zhang C., Li X., Chen Y., Zhang S.M., Lian G.,
RA Liu Q., Ruan K., Wang Z., Zhang C.S., Chien K.Y., Wu J., Li Q., Han J.,
RA Lin S.C.;
RT "GSK3-TIP60-ULK1 signaling pathway links growth factor deprivation to
RT autophagy.";
RL Science 336:477-481(2012).
CC -!- FUNCTION: Constitutively active protein kinase that acts as a negative
CC regulator in the hormonal control of glucose homeostasis, Wnt signaling
CC and regulation of transcription factors and microtubules, by
CC phosphorylating and inactivating glycogen synthase (GYS1 or GYS2),
CC CTNNB1/beta-catenin, APC and AXIN1 (PubMed:15791206, PubMed:17908561).
CC Requires primed phosphorylation of the majority of its substrates
CC (PubMed:22539723). Contributes to insulin regulation of glycogen
CC synthesis by phosphorylating and inhibiting GYS1 activity and hence
CC glycogen synthesis (PubMed:15791206, PubMed:17908561). Regulates
CC glycogen metabolism in liver, but not in muscle (PubMed:17908561). May
CC also mediate the development of insulin resistance by regulating
CC activation of transcription factors (By similarity). In Wnt signaling,
CC regulates the level and transcriptional activity of nuclear
CC CTNNB1/beta-catenin (PubMed:15791206). Facilitates amyloid precursor
CC protein (APP) processing and the generation of APP-derived amyloid
CC plaques found in Alzheimer disease (By similarity). May be involved in
CC the regulation of replication in pancreatic beta-cells (By similarity).
CC Is necessary for the establishment of neuronal polarity and axon
CC outgrowth (PubMed:17391670). Through phosphorylation of the anti-
CC apoptotic protein MCL1, may control cell apoptosis in response to
CC growth factors deprivation (PubMed:16543145). Acts as a regulator of
CC autophagy by mediating phosphorylation of KAT5/TIP60 under starvation
CC conditions, activating KAT5/TIP60 acetyltransferase activity and
CC promoting acetylation of key autophagy regulators, such as ULK1 and
CC RUBCNL/Pacer (PubMed:22539723). Negatively regulates extrinsic
CC apoptotic signaling pathway via death domain receptors. Promotes the
CC formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B,
CC at death receptors, including TNFRSF10B. The anti-apoptotic function is
CC most effective with weak apoptotic signals and can be overcome by
CC stronger stimulation (By similarity). {ECO:0000250|UniProtKB:P49840,
CC ECO:0000250|UniProtKB:P49841, ECO:0000269|PubMed:15791206,
CC ECO:0000269|PubMed:16543145, ECO:0000269|PubMed:17391670,
CC ECO:0000269|PubMed:17908561, ECO:0000269|PubMed:22539723}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.26;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:22539723};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Activated by phosphorylation at Tyr-279. In
CC response to insulin, inhibited by phosphorylation at Ser-21 by
CC PKB/AKT1; phosphorylation at this site causes a conformational change,
CC preventing access of substrates to the active site. Inhibited by
CC lithium.
CC -!- SUBUNIT: Monomer. Interacts with AXIN1 and CTNNB1/beta-catenin (By
CC similarity). Interacts with ARRB2 (PubMed:16051150). Interacts with
CC CTNND2 (By similarity). Interacts with LMBR1L (By similarity).
CC Interacts with DDX3X (By similarity). Interacts with TNFRSF10B (By
CC similarity). {ECO:0000250|UniProtKB:P49840,
CC ECO:0000269|PubMed:16051150}.
CC -!- PTM: Phosphorylated by AKT1 at Ser-21: upon insulin-mediated signaling,
CC the activated PKB/AKT1 protein kinase phosphorylates and deactivates
CC GSK3A, resulting in the dephosphorylation and activation of GYS1.
CC Activated by phosphorylation at Tyr-279. {ECO:0000269|PubMed:15791206}.
CC -!- DISRUPTION PHENOTYPE: Enhanced glucose tolerance and insulin
CC sensitivity, increased activity of hepatic glycogen synthase, elevated
CC hepatic glycogen storage and reduced fat mass.
CC {ECO:0000269|PubMed:17908561}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. GSK-3 subfamily. {ECO:0000305}.
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DR EMBL; AC156992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC111032; AAI11033.1; -; mRNA.
DR CCDS; CCDS20976.1; -.
DR RefSeq; NP_001026837.1; NM_001031667.1.
DR AlphaFoldDB; Q2NL51; -.
DR SMR; Q2NL51; -.
DR BioGRID; 546781; 19.
DR ComplexPortal; CPX-453; Beta-catenin destruction core complex, Apc-Axin1-Gsk3a variant.
DR ComplexPortal; CPX-456; Beta-catenin destruction core complex, Apc2-Axin1-Gsk3a variant.
DR ComplexPortal; CPX-457; Beta-catenin destruction core complex, Apc-Axin2-Gsk3a variant.
DR ComplexPortal; CPX-458; Beta-catenin destruction core complex, Apc2-Axin2-Gsk3a variant.
DR IntAct; Q2NL51; 2.
DR STRING; 10090.ENSMUSP00000071654; -.
DR ChEMBL; CHEMBL2176843; -.
DR iPTMnet; Q2NL51; -.
DR PhosphoSitePlus; Q2NL51; -.
DR SwissPalm; Q2NL51; -.
DR EPD; Q2NL51; -.
DR jPOST; Q2NL51; -.
DR MaxQB; Q2NL51; -.
DR PaxDb; 10090-ENSMUSP00000071654; -.
DR ProteomicsDB; 269640; -.
DR Pumba; Q2NL51; -.
DR Antibodypedia; 3833; 1344 antibodies from 49 providers.
DR Ensembl; ENSMUST00000071739.12; ENSMUSP00000071654.6; ENSMUSG00000057177.13.
DR GeneID; 606496; -.
DR KEGG; mmu:606496; -.
DR UCSC; uc009frx.1; mouse.
DR AGR; MGI:2152453; -.
DR CTD; 2931; -.
DR MGI; MGI:2152453; Gsk3a.
DR VEuPathDB; HostDB:ENSMUSG00000057177; -.
DR eggNOG; KOG0658; Eukaryota.
DR GeneTree; ENSGT00520000055635; -.
DR InParanoid; Q2NL51; -.
DR OMA; CLHAFFD; -.
DR OrthoDB; 2872909at2759; -.
DR PhylomeDB; Q2NL51; -.
DR TreeFam; TF101104; -.
DR BRENDA; 2.7.11.26; 3474.
DR BioGRID-ORCS; 606496; 4 hits in 79 CRISPR screens.
DR ChiTaRS; Gsk3a; mouse.
DR PRO; PR:Q2NL51; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q2NL51; Protein.
DR Bgee; ENSMUSG00000057177; Expressed in motor neuron and 250 other cell types or tissues.
DR ExpressionAtlas; Q2NL51; baseline and differential.
DR Genevisible; Q2NL51; MM.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0030877; C:beta-catenin destruction complex; NAS:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR GO; GO:0120283; F:protein serine/threonine kinase binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:ARUK-UCL.
DR GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0141068; P:autosome genomic imprinting; IMP:BHF-UCL.
DR GO; GO:0003214; P:cardiac left ventricle morphogenesis; IMP:BHF-UCL.
DR GO; GO:0016477; P:cell migration; IGI:MGI.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IGI:ARUK-UCL.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:0036016; P:cellular response to interleukin-3; IDA:UniProtKB.
DR GO; GO:0071285; P:cellular response to lithium ion; IDA:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IGI:ARUK-UCL.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:UniProtKB.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IMP:BHF-UCL.
DR GO; GO:2000171; P:negative regulation of dendrite development; ISO:MGI.
DR GO; GO:0046325; P:negative regulation of glucose import; ISO:MGI.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IMP:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IGI:ARUK-UCL.
DR GO; GO:0071879; P:positive regulation of adenylate cyclase-activating adrenergic receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0106071; P:positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
DR GO; GO:2000467; P:positive regulation of glycogen (starch) synthase activity; IMP:BHF-UCL.
DR GO; GO:0045823; P:positive regulation of heart contraction; IMP:BHF-UCL.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; ISO:MGI.
DR GO; GO:1901524; P:regulation of mitophagy; IEA:Ensembl.
DR GO; GO:0010975; P:regulation of neuron projection development; IBA:GO_Central.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IMP:BHF-UCL.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd14137; STKc_GSK3; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR039192; STKc_GSK3.
DR PANTHER; PTHR24057; GLYCOGEN SYNTHASE KINASE-3 ALPHA; 1.
DR PANTHER; PTHR24057:SF14; GLYCOGEN SYNTHASE KINASE-3 ALPHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Carbohydrate metabolism; Glycogen metabolism;
KW Kinase; Neurogenesis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase;
KW Signal transduction inhibitor; Transferase; Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49840"
FT CHAIN 2..490
FT /note="Glycogen synthase kinase-3 alpha"
FT /id="PRO_0000280395"
FT DOMAIN 119..404
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 244
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 125..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P49840"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49840"
FT MOD_RES 21
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:15791206"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49840"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49840"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49840"
FT MOD_RES 279
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18265"
FT MUTAGEN 21
FT /note="S->A: Loss of phosphorylation; No inhibition of
FT activity and constitutively active."
FT /evidence="ECO:0000269|PubMed:15791206"
SQ SEQUENCE 490 AA; 51661 MW; 739CDD86BBFB497B CRC64;
MSGGGPSGGG PGGSGRARTS SFAEPGGGGG GGGGGPGGSA SGPGGTGGGK ASVGAMGGGV
GASSSGGGPS GSGGGGSGGP GAGTSFPPPG VKLGRDSGKV TTVVATVGQG PERSQEVAYT
DIKVIGNGSF GVVYQARLAE TRELVAIKKV LQDKRFKNRE LQIMRKLDHC NIVRLRYFFY
SSGEKKDELY LNLVLEYVPE TVYRVARHFT KAKLITPIIY IKVYMYQLFR SLAYIHSQGV
CHRDIKPQNL LVDPDTAVLK LCDFGSAKQL VRGEPNVSYI CSRYYRAPEL IFGATDYTSS
IDVWSAGCVL AELLLGQPIF PGDSGVDQLV EIIKVLGTPT REQIREMNPN YTEFKFPQIK
AHPWTKVFKS SKTPPEAIAL CSSLLEYTPS SRLSPLEACA HSFFDELRRL GAQLPNDRPL
PPLFNFSPGE LSIQPSLNAI LIPPHLRSPA GPASPLTTSY NPSSQALTEA QTGQDWQPSD
ATTATLASSS
//
