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   04-NOV-2026, entry version 189.
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 an allosteric
CC       inhibitor. AMP binding affects the turnover of bound substrate and not
CC       the affinity for substrate. Fructose 2,6-bisphosphate acts as a
CC       competitive inhibitor. Fructose 2,6-bisphosphate and AMP have
CC       synergistic effects (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_019395.4.
DR   SMR; Q9QXD6; -.
DR   BioGRID; 199610; 3.
DR   IntAct; Q9QXD6; 14.
DR   STRING; 10090.ENSMUSP00000090564; -.
DR   BindingDB; Q9QXD6; -.
DR   ChEMBL; CHEMBL5360; -.
DR   GlyGen; Q9QXD6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9QXD6; -.
DR   PhosphoSitePlus; Q9QXD6; -.
DR   SwissPalm; Q9QXD6; -.
DR   REPRODUCTION-2DPAGE; IPI00228630; -.
DR   REPRODUCTION-2DPAGE; Q9QXD6; -.
DR   PaxDb; 10090-ENSMUSP00000090564; -.
DR   PeptideAtlas; Q9QXD6; -.
DR   ProteomicsDB; 275824; -.
DR   jPOST; Q9QXD6; -.
DR   DNASU; 14121; -.
DR   Ensembl; ENSMPUT00000006723; ENSMPUP00000006610; ENSMPUG00000006664.
DR   Ensembl; ENSMUST00000092888.11; ENSMUSP00000090564.5; ENSMUSG00000069805.11.
DR   GeneID; 14121; -.
DR   KEGG; mmu:14121; -.
DR   UCSC; uc007qxg.2; mouse.
DR   CTD; 2203; -.
DR   VEuPathDB; HostDB:ENSMUSG00000069805; -.
DR   AGR; MGI:95492; -.
DR   MGI; MGI:95492; Fbp1.
DR   eggNOG; KOG1458; Eukaryota.
DR   GeneTree; ENSGT00390000015513; -.
DR   HOGENOM; CLU_039977_1_0_1; -.
DR   InParanoid; Q9QXD6; -.
DR   OMA; AACYTMY; -.
DR   OrthoDB; 10256725at2759; -.
DR   PhylomeDB; Q9QXD6; -.
DR   BRENDA; 3.1.3.11; 3474.
DR   Reactome; R-MMU-70263; Gluconeogenesis.
DR   UniPathway; UPA00138; -.
DR   PRO; PR:Q9QXD6; -.
DR   Bgee; ENSMUSG00000069805; Expressed in left lobe of liver and 122 other cell types or tissues.
DR   ExpressionAtlas; Q9QXD6; baseline and differential.
DR   CDD; cd00354; FBPase; 1.
DR   FunFam; 3.30.540.10:FF:000037; Fructose-1,6-bisphosphatase 1; 1.
DR   FunFam; 3.40.190.80:FF:000001; Fructose-1,6-bisphosphatase class 1; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 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:SF11; FRUCTOSE-1,6-BISPHOSPHATASE 1; 1.
DR   PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 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   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   NCBIfam; NF006778; fbp; 1.
DR   PROSITE; PS00124; FBPASE; 1.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; ISO:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISO:GO_Central.
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:GO_Central.
DR   GO; GO:0071475; P:cellular hyperosmotic salinity response; IEA:Ensembl.
DR   GO; GO:0071477; P:cellular hypotonic salinity response; IEA:Ensembl.
DR   GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
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:1904628; P:cellular response to phorbol 13-acetate 12-myristate; IEA:Ensembl.
DR   GO; GO:0097403; P:cellular response to raffinose; IEA:Ensembl.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISS:UniProtKB.
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:GO_Central.
DR   GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
DR   GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR   Proteomes; UP000000589; Chromosome 13.
DR   Antibodypedia; 1620; 350 antibodies from 38 providers.
DR   RNAct; Q9QXD6; protein.
DR   BioGRID-ORCS; 14121; 1 hit in 78 CRISPR screens.
DR   AlphaFoldDB; Q9QXD6; -.
DR   FunCoup; Q9QXD6; 1329.
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
//