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   24-JAN-2024, entry version 182.
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; Evidence={ECO:0000255|HAMAP-
CC         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; 22.
DR   ComplexPortal; CPX-2053; 6-phosphofructokinase, P4 homotetramer.
DR   IntAct; Q9WUA3; 4.
DR   STRING; 10090.ENSMUSP00000117030; -.
DR   GlyCosmos; Q9WUA3; 1 site, No reported glycans.
DR   GlyGen; Q9WUA3; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9WUA3; -.
DR   PhosphoSitePlus; Q9WUA3; -.
DR   SwissPalm; Q9WUA3; -.
DR   EPD; Q9WUA3; -.
DR   jPOST; Q9WUA3; -.
DR   MaxQB; Q9WUA3; -.
DR   PaxDb; 10090-ENSMUSP00000117030; -.
DR   PeptideAtlas; Q9WUA3; -.
DR   ProteomicsDB; 287687; -. [Q9WUA3-1]
DR   ProteomicsDB; 287688; -. [Q9WUA3-2]
DR   Pumba; Q9WUA3; -.
DR   Antibodypedia; 23840; 599 antibodies from 35 providers.
DR   DNASU; 56421; -.
DR   Ensembl; ENSMUST00000138703.8; ENSMUSP00000117030.2; ENSMUSG00000021196.15. [Q9WUA3-1]
DR   GeneID; 56421; -.
DR   KEGG; mmu:56421; -.
DR   UCSC; uc007pjz.2; mouse. [Q9WUA3-1]
DR   UCSC; uc007pkc.2; mouse. [Q9WUA3-2]
DR   AGR; MGI:1891833; -.
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; EWQDQMC; -.
DR   OrthoDB; 374214at2759; -.
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 77 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 290 other cell types or tissues.
DR   ExpressionAtlas; Q9WUA3; baseline and differential.
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; 3.40.50.450; -; 2.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 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   NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR   PANTHER; PTHR13697:SF5; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE, PLATELET TYPE; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 2.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
DR   Genevisible; Q9WUA3; MM.
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
//