F16P1_MOUSE
ID F16P1_MOUSE Reviewed; 338 AA.
AC Q9QXD6; P97323; Q3UEH1;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Fructose-1,6-bisphosphatase 1;
DE Short=FBPase 1;
DE EC=3.1.3.11 {ECO:0000250|UniProtKB:P19112};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 1;
DE AltName: Full=Fructose-1,6-bisphosphatase isozyme 3;
DE Short=FBPase 3;
DE AltName: Full=Liver FBPase;
GN Name=Fbp1; Synonyms=Fbp, Fbp3;
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.
RC TISSUE=Liver;
RX PubMed=11250076; DOI=10.1016/s0378-1119(01)00325-0;
RA Stein S., Liehr T., Eschrich K.;
RT "Characterization of the mouse liver fructose-1,6-bisphosphatase gene.";
RL Gene 264:215-224(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Liver;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 154-247.
RC STRAIN=C57BL/6J;
RX PubMed=9106734; DOI=10.1097/00001756-199702100-00008;
RA Cloix J.F., Beaulieu E., Hevor T.K.;
RT "Various fructose-1,6-bisphosphatase mRNAs in mouse brain, liver, kidney
RT and heart.";
RL NeuroReport 8:617-622(1997).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16497803; DOI=10.1210/en.2005-1498;
RA Lamont B.J., Visinoni S., Fam B.C., Kebede M., Weinrich B.,
RA Papapostolou S., Massinet H., Proietto J., Favaloro J., Andrikopoulos S.;
RT "Expression of human fructose-1,6-bisphosphatase in the liver of transgenic
RT mice results in increased glycerol gluconeogenesis.";
RL Endocrinology 147:2764-2772(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, 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 [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18375435; DOI=10.2337/db07-1326;
RA Kebede M., Favaloro J., Gunton J.E., Laybutt D.R., Shaw M., Wong N.,
RA Fam B.C., Aston-Mourney K., Rantzau C., Zulli A., Proietto J.,
RA Andrikopoulos S.;
RT "Fructose-1,6-bisphosphatase overexpression in pancreatic beta-cells
RT results in reduced insulin secretion: a new mechanism for fat-induced
RT impairment of beta-cell function.";
RL Diabetes 57:1887-1895(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216; TYR-245 AND TYR-265, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, 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 TISSUE SPECIFICITY.
RX PubMed=20719858; DOI=10.1210/en.2009-1185;
RA Zhang Y., Xie Z., Zhou G., Zhang H., Lu J., Zhang W.J.;
RT "Fructose-1,6-bisphosphatase regulates glucose-stimulated insulin secretion
RT of mouse pancreatic beta-cells.";
RL Endocrinology 151:4688-4695(2010).
RN [10]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-151, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
CC fructose 6-phosphate in the presence of divalent cations, acting as a
CC rate-limiting enzyme in gluconeogenesis. Plays a role in regulating
CC glucose sensing and insulin secretion of pancreatic beta-cells. Appears
CC to modulate glycerol gluconeogenesis in liver. Important regulator of
CC appetite and adiposity; increased expression of the protein in liver
CC after nutrient excess increases circulating satiety hormones and
CC reduces appetite-stimulating neuropeptides and thus seems to provide a
CC feedback mechanism to limit weight gain. {ECO:0000269|PubMed:16497803,
CC ECO:0000269|PubMed:18375435, ECO:0000269|PubMed:20719858}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC Evidence={ECO:0000250|UniProtKB:P19112};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00636};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P00636};
CC -!- ACTIVITY REGULATION: Subject to complex allosteric regulation. The
CC enzyme can assume an active R-state, or an inactive T-state.
CC Intermediate conformations may exist. AMP acts as allosteric inhibitor.
CC AMP binding affects the turnover of bound substrate and not the
CC affinity for substrate. Fructose 2,6-bisphosphate acts as competitive
CC inhibitor. Fructose 2,6-bisphosphate and AMP have synergistic effects
CC (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00636}.
CC -!- TISSUE SPECIFICITY: Detected in pancreatic beta-cell lines MIN6 and
CC beta-TC and in liver (at protein level). Preferentially expressed in
CC liver, with lower levels detected in pancreatic islets and intestine,
CC and very low levels in blood, muscle, brain and spleen.
CC {ECO:0000269|PubMed:11250076, ECO:0000269|PubMed:16497803,
CC ECO:0000269|PubMed:18375435, ECO:0000269|PubMed:20719858}.
CC -!- INDUCTION: Up-regulated in pancreas by obesity and dietary fat intake
CC and in diabetic animals. {ECO:0000269|PubMed:18375435}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR EMBL; AJ132693; CAB65244.1; -; mRNA.
DR EMBL; AK002216; BAB21941.1; -; mRNA.
DR EMBL; AK149527; BAE28940.1; -; mRNA.
DR EMBL; BC011480; AAH11480.1; -; mRNA.
DR EMBL; BC051392; AAH51392.1; -; mRNA.
DR EMBL; Y11067; CAA71946.1; -; mRNA.
DR CCDS; CCDS26590.1; -.
DR RefSeq; NP_062268.1; NM_019395.3.
DR AlphaFoldDB; Q9QXD6; -.
DR SMR; Q9QXD6; -.
DR BioGRID; 199610; 2.
DR IntAct; Q9QXD6; 13.
DR MINT; Q9QXD6; -.
DR STRING; 10090.ENSMUSP00000090564; -.
DR BindingDB; Q9QXD6; -.
DR ChEMBL; CHEMBL5360; -.
DR iPTMnet; Q9QXD6; -.
DR PhosphoSitePlus; Q9QXD6; -.
DR SwissPalm; Q9QXD6; -.
DR REPRODUCTION-2DPAGE; IPI00228630; -.
DR REPRODUCTION-2DPAGE; Q9QXD6; -.
DR jPOST; Q9QXD6; -.
DR MaxQB; Q9QXD6; -.
DR PaxDb; Q9QXD6; -.
DR PeptideAtlas; Q9QXD6; -.
DR PRIDE; Q9QXD6; -.
DR ProteomicsDB; 275824; -.
DR Antibodypedia; 1620; 291 antibodies from 33 providers.
DR DNASU; 14121; -.
DR Ensembl; ENSMUST00000092888; ENSMUSP00000090564; ENSMUSG00000069805.
DR GeneID; 14121; -.
DR KEGG; mmu:14121; -.
DR UCSC; uc007qxg.2; mouse.
DR CTD; 2203; -.
DR MGI; MGI:95492; Fbp1.
DR VEuPathDB; HostDB:ENSMUSG00000069805; -.
DR eggNOG; KOG1458; Eukaryota.
DR GeneTree; ENSGT00390000015513; -.
DR HOGENOM; CLU_039977_1_0_1; -.
DR InParanoid; Q9QXD6; -.
DR OMA; YIPENCP; -.
DR OrthoDB; 1381522at2759; -.
DR PhylomeDB; Q9QXD6; -.
DR TreeFam; TF314824; -.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR UniPathway; UPA00138; -.
DR BioGRID-ORCS; 14121; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Fbp1; mouse.
DR PRO; PR:Q9QXD6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9QXD6; protein.
DR Bgee; ENSMUSG00000069805; Expressed in left lobe of liver and 120 other tissues.
DR ExpressionAtlas; Q9QXD6; baseline and differential.
DR Genevisible; Q9QXD6; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016208; F:AMP binding; ISS:UniProtKB.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IMP:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0048029; F:monosaccharide binding; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0071286; P:cellular response to magnesium ion; ISS:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IMP:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0045820; P:negative regulation of glycolytic process; ISS:UniProtKB.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central.
DR CDD; cd00354; FBPase; 1.
DR HAMAP; MF_01855; FBPase_class1; 1.
DR InterPro; IPR044015; FBPase_C_dom.
DR InterPro; IPR000146; FBPase_class-1.
DR InterPro; IPR033391; FBPase_N.
DR InterPro; IPR028343; FBPtase.
DR InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR PANTHER; PTHR11556; PTHR11556; 1.
DR Pfam; PF00316; FBPase; 1.
DR Pfam; PF18913; FBPase_C; 1.
DR PIRSF; PIRSF500210; FBPtase; 1.
DR PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR PRINTS; PR00115; F16BPHPHTASE.
DR PROSITE; PS00124; FBPASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Allosteric enzyme; Carbohydrate metabolism; Gluconeogenesis;
KW Hydrolase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00637"
FT CHAIN 2..338
FT /note="Fructose-1,6-bisphosphatase 1"
FT /id="PRO_0000200499"
FT BINDING 18..22
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 28..32
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 113..114
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 122..125
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 141
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 213..216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 244..249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 275..277
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P00637"
FT MOD_RES 151
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 216
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 245
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 265
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 198
FT /note="D -> E (in Ref. 4; CAA71946)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="V -> G (in Ref. 4; CAA71946)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="D -> N (in Ref. 4; CAA71946)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="N -> L (in Ref. 4; CAA71946)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="L -> H (in Ref. 4; CAA71946)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="K -> Q (in Ref. 4; CAA71946)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..235
FT /note="PP -> HE (in Ref. 4; CAA71946)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="S -> T (in Ref. 4; CAA71946)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="A -> T (in Ref. 4; CAA71946)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 36912 MW; 50AE999F0D517E4F CRC64;
MANHAPFETD ISTLTRFVME QGRKAQGTGE LTQLLNSLCT AIKAISSAVR QAGIAQLYGI
AGSTNVTGDQ VKKLDILSND LVINMLKSSY ATCVLVSEEN TNAIIIEPEK RGKYVVCFDP
LDGSSNIDCL VSIGTIFGIY RKKSTDEPSE KDALQPGRDL VAAGYALYGS ATMLVLAMDC
GVNCFMLDPS IGEFIMVDRD VKMKKKGNIY SLNEGYAKDF DPAINEYLQR KKFPPDGSAP
YGARYVGSMV ADIHRTLVYG GIFLYPANKK SPSGKLRLLY ECNPIAYVME KAGGLATTGD
KDILDIVPTE IHQKAPVVMG SSEDVQEFLE IYRKHKAK
