PFKAP_MOUSE
ID PFKAP_MOUSE Reviewed; 784 AA.
AC Q9WUA3; Q3TNA9; Q3U4P1; Q3U7G4; Q4KUG1; Q543K8; Q8C5I6; Q9JI86;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=ATP-dependent 6-phosphofructokinase, platelet type {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=PFK-P;
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=6-phosphofructokinase type C;
DE AltName: Full=Phosphofructo-1-kinase isozyme C;
DE Short=PFK-C;
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=Pfkp; Synonyms=Pfkc;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Ascitic tumor;
RX PubMed=10814514; DOI=10.1006/bbrc.2000.2681;
RA Sanchez-Martinez C., Estevez A.M., Aragon J.J.;
RT "Phosphofructokinase C isozyme from ascites tumor cells: cloning,
RT expression, and properties.";
RL Biochem. Biophys. Res. Commun. 271:635-640(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT PRO-180.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=11137296; DOI=10.1016/s0378-1119(00)00463-7;
RA Gunasekera D., Kemp R.G.;
RT "Genomic organization, 5'flanking region and tissue-specific expression of
RT mouse phosphofructokinase C gene.";
RL Gene 260:103-112(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLN-261; MET-292;
RP ASP-694; PRO-777 AND GLY-782.
RC STRAIN=LG/J, and SM/J;
RX PubMed=15919810; DOI=10.2337/diabetes.54.6.1863;
RA Ehrich T.H., Hrbek T., Kenney-Hunt J.P., Pletscher L.S., Wang B.,
RA Semenkovich C.F., Cheverud J.M.;
RT "Fine-mapping gene-by-diet interactions on chromosome 13 in a LG/J x SM/J
RT murine model of obesity.";
RL Diabetes 54:1863-1872(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP VAL-104; GLY-145; GLN-261; MET-292; GLU-402; SER-679; ASP-694; PHE-696;
RP PRO-777 AND GLY-782.
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Hippocampus, Kidney, and Olfactory bulb;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-650, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-687, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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 phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03184};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SUBUNIT: Homo- and heterotetramers (By similarity). Phosphofructokinase
CC (PFK) enzyme functions as a tetramer composed of different combinations
CC of 3 types of subunits, called PFKM (M), PFKL (L) and PFKP (P). The
CC composition of the PFK tetramer differs according to the tissue type it
CC is present in. The kinetic and regulatory properties of the tetrameric
CC enzyme are dependent on the subunit composition, hence can vary across
CC tissues (Probable). Interacts with ATG4B; promoting phosphorylation of
CC ATG4B. {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WUA3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WUA3-2; Sequence=VSP_016664, VSP_016665;
CC -!- TISSUE SPECIFICITY: Expression is constant during tumor growth and
CC markedly decreases when cell proliferation stops.
CC {ECO:0000269|PubMed:10814514}.
CC -!- PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E'
CC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
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DR EMBL; Y19008; CAB64347.1; -; mRNA.
DR EMBL; AF123533; AAD23571.1; -; mRNA.
DR EMBL; AF249893; AAF75700.1; -; Genomic_DNA.
DR EMBL; AF250369; AAF75700.1; JOINED; Genomic_DNA.
DR EMBL; AF250370; AAF75700.1; JOINED; Genomic_DNA.
DR EMBL; AF250371; AAF75700.1; JOINED; Genomic_DNA.
DR EMBL; AF250372; AAF75700.1; JOINED; Genomic_DNA.
DR EMBL; AF251021; AAF75700.1; JOINED; Genomic_DNA.
DR EMBL; AY779275; AAX11357.1; -; mRNA.
DR EMBL; AY779276; AAX11358.1; -; mRNA.
DR EMBL; AK049841; BAC33949.1; -; mRNA.
DR EMBL; AK078254; BAC37195.1; -; mRNA.
DR EMBL; AK152670; BAE31405.1; -; mRNA.
DR EMBL; AK154125; BAE32390.1; -; mRNA.
DR EMBL; AK165422; BAE38177.1; -; mRNA.
DR EMBL; AK165425; BAE38180.1; -; mRNA.
DR EMBL; AK170624; BAE41918.1; -; mRNA.
DR EMBL; AK171062; BAE42221.1; -; mRNA.
DR EMBL; CT010268; CAJ18476.1; -; mRNA.
DR EMBL; BC006926; AAH06926.1; -; mRNA.
DR CCDS; CCDS26230.1; -. [Q9WUA3-1]
DR RefSeq; NP_001278000.1; NM_001291071.1.
DR RefSeq; NP_062677.1; NM_019703.4. [Q9WUA3-1]
DR AlphaFoldDB; Q9WUA3; -.
DR SMR; Q9WUA3; -.
DR BioGRID; 207967; 21.
DR ComplexPortal; CPX-2053; 6-phosphofructokinase, P4 homotetramer.
DR IntAct; Q9WUA3; 4.
DR STRING; 10090.ENSMUSP00000117030; -.
DR GlyGen; Q9WUA3; 1 site.
DR iPTMnet; Q9WUA3; -.
DR PhosphoSitePlus; Q9WUA3; -.
DR SwissPalm; Q9WUA3; -.
DR EPD; Q9WUA3; -.
DR jPOST; Q9WUA3; -.
DR MaxQB; Q9WUA3; -.
DR PaxDb; Q9WUA3; -.
DR PeptideAtlas; Q9WUA3; -.
DR PRIDE; Q9WUA3; -.
DR ProteomicsDB; 287687; -. [Q9WUA3-1]
DR ProteomicsDB; 287688; -. [Q9WUA3-2]
DR Antibodypedia; 23840; 517 antibodies from 35 providers.
DR DNASU; 56421; -.
DR Ensembl; ENSMUST00000138703; ENSMUSP00000117030; ENSMUSG00000021196. [Q9WUA3-1]
DR GeneID; 56421; -.
DR KEGG; mmu:56421; -.
DR UCSC; uc007pjz.2; mouse. [Q9WUA3-1]
DR UCSC; uc007pkc.2; mouse. [Q9WUA3-2]
DR CTD; 5214; -.
DR MGI; MGI:1891833; Pfkp.
DR VEuPathDB; HostDB:ENSMUSG00000021196; -.
DR eggNOG; KOG2440; Eukaryota.
DR GeneTree; ENSGT00940000155002; -.
DR HOGENOM; CLU_011053_0_0_1; -.
DR InParanoid; Q9WUA3; -.
DR OMA; FEAYHST; -.
DR OrthoDB; 172878at2759; -.
DR TreeFam; TF300411; -.
DR BRENDA; 2.7.1.11; 3474.
DR Reactome; R-MMU-70171; Glycolysis.
DR SABIO-RK; Q9WUA3; -.
DR UniPathway; UPA00109; UER00182.
DR BioGRID-ORCS; 56421; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Pfkp; mouse.
DR PRO; PR:Q9WUA3; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9WUA3; protein.
DR Bgee; ENSMUSG00000021196; Expressed in retinal neural layer and 287 other tissues.
DR ExpressionAtlas; Q9WUA3; baseline and differential.
DR Genevisible; Q9WUA3; MM.
DR GO; GO:0005945; C:6-phosphofructokinase complex; ISS:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0003872; F:6-phosphofructokinase activity; ISS:UniProtKB.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0070095; F:fructose-6-phosphate binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISO:MGI.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISO:MGI.
DR GO; GO:0006096; P:glycolytic process; ISO:MGI.
DR GO; GO:0061615; P:glycolytic process through fructose-6-phosphate; ISS:MGI.
DR CDD; cd00764; Eukaryotic_PFK; 1.
DR Gene3D; 3.40.50.460; -; 2.
DR HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR041914; PFK_vert-type.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 2.
DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE 1: Evidence at protein level;
KW Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding;
KW Cytoplasm; Glycolysis; Glycoprotein; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..784
FT /note="ATP-dependent 6-phosphofructokinase, platelet type"
FT /id="PRO_0000112025"
FT REGION 1..398
FT /note="N-terminal catalytic PFK domain 1"
FT REGION 399..410
FT /note="Interdomain linker"
FT REGION 411..784
FT /note="C-terminal regulatory PFK domain 2"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 96..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 126..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 172..174
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 209
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 216..218
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 272
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 300
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 306..309
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 480
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 537..541
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 575
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 582..584
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 638
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 664
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 670..673
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 743
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q01813"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47860"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01813"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01813"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47860"
FT MOD_RES 394
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01813"
FT MOD_RES 485
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01813"
FT MOD_RES 650
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 687
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CARBOHYD 539
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 457..496
FT /note="IKEIGWADVGGWTGQGGSILGTKRTLPGKYLEKIAEQMHS -> VSLPGVLG
FT MLKCYCIWGGHPPLTAPTKSRFLVVGLYQILI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016664"
FT VAR_SEQ 497..784
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016665"
FT VARIANT 104
FT /note="E -> V (in strain: NOD)"
FT /evidence="ECO:0000269|PubMed:16141072"
FT VARIANT 145
FT /note="E -> G (in strain: C57BL/6J)"
FT /evidence="ECO:0000269|PubMed:16141072"
FT VARIANT 180
FT /note="T -> P (in strain: C57BL/6)"
FT /evidence="ECO:0000269|PubMed:11137296"
FT VARIANT 261
FT /note="R -> Q (in strain: LG/J and NOD)"
FT /evidence="ECO:0000269|PubMed:15919810,
FT ECO:0000269|PubMed:16141072"
FT VARIANT 292
FT /note="V -> M (in strain: LG/J and NOD)"
FT /evidence="ECO:0000269|PubMed:15919810,
FT ECO:0000269|PubMed:16141072"
FT VARIANT 402
FT /note="D -> E (in strain: C57BL/6J)"
FT /evidence="ECO:0000269|PubMed:16141072"
FT VARIANT 679
FT /note="P -> S (in strain: C57BL/6J)"
FT /evidence="ECO:0000269|PubMed:16141072"
FT VARIANT 694
FT /note="E -> D (in strain: LG/J and NOD)"
FT /evidence="ECO:0000269|PubMed:15919810,
FT ECO:0000269|PubMed:16141072"
FT VARIANT 696
FT /note="I -> F (in strain: NOD)"
FT /evidence="ECO:0000269|PubMed:16141072"
FT VARIANT 777
FT /note="S -> P (in strain: LG/J and NOD)"
FT /evidence="ECO:0000269|PubMed:15919810,
FT ECO:0000269|PubMed:16141072"
FT VARIANT 782
FT /note="E -> G (in strain: LG/J and NOD)"
FT /evidence="ECO:0000269|PubMed:15919810,
FT ECO:0000269|PubMed:16141072"
SQ SEQUENCE 784 AA; 85455 MW; E9C5AAABF26FCA65 CRC64;
MSDLDSSSSS AYPKYLEHLS GDGKAIGVLT SGGDAQGMNA AVRAVVRMGI YTGAKVYFIY
EGYQGLVDGG SNIVEAKWDC VSSILQVGGT IIGSARCKAF RSREGRLKAA CNLARLGITN
LCVIGGDGSL TGANLFRKEW SGLLEELARN GDIDNDTVQK YSYLNVVGMV GSIDNDFCGT
DMTIGTDSAL HRIIEVVDAI MTTAQSHQRT FVLEVMGRHC GYLALVSALT CGADWVFLPE
SPPEEDWEEN MCLKLSENRA RKKRLNIIIV SEGAIDMQNK PITSEKIKEL VVKNLGFDTR
VTILGHVQRG GTPSAFDRIL ASRMGVEAVI ALLEATPETP ACVVSLRGNQ AVRLPLMECV
QMTQDVQKAM DERRFKEAVK LRGRRFEGNL NTYKRLAIKL PDEKIVKSNC NVAVINVGAP
AAGMNAAVRS AVRVGIADGH KMFAIYDGFE GFANGQIKEI GWADVGGWTG QGGSILGTKR
TLPGKYLEKI AEQMHSHSIN ALLIIGGFEA YLGLLELAAA REKHEAFCVP MVMVPATVSN
NVPGSDFSIG ADTALNTITD TCDRIKQSAS GTKRRVFIIE TMGGYCGYLA NMGALAAGAD
AAYIFEEPFD IGDLQSNVVH LTEKMKTSIQ RGLVLRNESC SVNYTTDFIY QLYSEEGKGV
FDCRKNVLGH MQQGGAPSPF DRNFGTKISA KAMEWISAKL KGSQGTGKKF VSDDSICVLG
ICKRDLLFQP VAELKKVTDF EHRIPKEQWW LKLRPIMKIL AKYEASYDMS DSGKLESLQH
HEEL
