GenomeNet

Database: UniProt/SWISS-PROT
Entry: PFKAP_MOUSE
LinkDB: PFKAP_MOUSE
Original site: 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   13-FEB-2019, entry version 157.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RP   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
RT   expression of 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
RT   SM/J murine model of obesity.";
RL   Diabetes 54:1863-1872(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP   VARIANTS VAL-104; GLY-145; GLN-261; MET-292; GLU-402; SER-679;
RP   ASP-694; PHE-696; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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.,
RA   Mollenhauer J., 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-650, AND IDENTIFICATION
RP   BY 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-687, AND IDENTIFICATION BY
RP   MASS 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.,
RA   Zhang Y., 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
CC       to 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
CC         1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000255|HAMAP-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
CC       fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
CC       citrate. {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).
CC       Phosphofructokinase (PFK) enzyme functions as a tetramer composed
CC       of different combinations of 3 types of subunits, called PFKM (M),
CC       PFKL (L) and PFKP (P). The composition of the PFK tetramer differs
CC       according to the tissue type it is present in. The kinetic and
CC       regulatory properties of the tetrameric enzyme are dependent on
CC       the subunit composition, hence can vary across tissues (Probable).
CC       {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         Note=May be due to intron retention. No experimental
CC         confirmation available.;
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   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
CC       clade "E" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
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   UniGene; Mm.273874; -.
DR   ProteinModelPortal; Q9WUA3; -.
DR   SMR; Q9WUA3; -.
DR   BioGrid; 207967; 4.
DR   ComplexPortal; CPX-2053; 6-phosphofructokinase, P4 homotetramer.
DR   IntAct; Q9WUA3; 6.
DR   MINT; Q9WUA3; -.
DR   STRING; 10090.ENSMUSP00000117030; -.
DR   iPTMnet; Q9WUA3; -.
DR   PhosphoSitePlus; Q9WUA3; -.
DR   SwissPalm; Q9WUA3; -.
DR   EPD; Q9WUA3; -.
DR   jPOST; Q9WUA3; -.
DR   PaxDb; Q9WUA3; -.
DR   PeptideAtlas; Q9WUA3; -.
DR   PRIDE; Q9WUA3; -.
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   eggNOG; KOG2440; Eukaryota.
DR   eggNOG; COG0205; LUCA.
DR   GeneTree; ENSGT00940000155002; -.
DR   HOVERGEN; HBG000976; -.
DR   InParanoid; Q9WUA3; -.
DR   KO; K00850; -.
DR   OMA; PLVECVQ; -.
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   ChiTaRS; Pfkp; mouse.
DR   PRO; PR:Q9WUA3; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   Bgee; ENSMUSG00000021196; Expressed in 319 organ(s), highest expression level in heart.
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: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:0006007; P:glucose catabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; ISO:MGI.
DR   GO; GO:0061615; P:glycolytic process through fructose-6-phosphate; ISS:MGI.
DR   GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
DR   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
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   Complete proteome; Cytoplasm; Glycolysis; Glycoprotein; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN         1    784       ATP-dependent 6-phosphofructokinase,
FT                                platelet type.
FT                                /FTId=PRO_0000112025.
FT   NP_BIND      96     97       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   NP_BIND     126    129       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   REGION        1    398       N-terminal catalytic PFK domain 1.
FT   REGION      172    174       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      216    218       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      306    309       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      399    410       Interdomain linker.
FT   REGION      411    784       C-terminal regulatory PFK domain 2.
FT   REGION      537    541       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      582    584       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      670    673       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   ACT_SITE    174    174       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   METAL       127    127       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING      33     33       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     209    209       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     272    272       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     300    300       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     480    480       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     575    575       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     638    638       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     664    664       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     743    743       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES       2      2       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P47860}.
FT   MOD_RES       6      6       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES      20     20       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES     141    141       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P47860}.
FT   MOD_RES     394    394       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES     485    485       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q01813}.
FT   MOD_RES     650    650       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:17947660}.
FT   MOD_RES     687    687       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   CARBOHYD    539    539       O-linked (GlcNAc) serine. {ECO:0000250}.
FT   VAR_SEQ     457    496       IKEIGWADVGGWTGQGGSILGTKRTLPGKYLEKIAEQMHS
FT                                -> VSLPGVLGMLKCYCIWGGHPPLTAPTKSRFLVVGLYQI
FT                                LI (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_016664.
FT   VAR_SEQ     497    784       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_016665.
FT   VARIANT     104    104       E -> V (in strain: NOD).
FT                                {ECO:0000269|PubMed:16141072}.
FT   VARIANT     145    145       E -> G (in strain: C57BL/6J).
FT                                {ECO:0000269|PubMed:16141072}.
FT   VARIANT     180    180       T -> P (in strain: C57BL/6).
FT                                {ECO:0000269|PubMed:11137296}.
FT   VARIANT     261    261       R -> Q (in strain: LG/J and NOD).
FT                                {ECO:0000269|PubMed:15919810,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     292    292       V -> M (in strain: LG/J and NOD).
FT                                {ECO:0000269|PubMed:15919810,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     402    402       D -> E (in strain: C57BL/6J).
FT                                {ECO:0000269|PubMed:16141072}.
FT   VARIANT     679    679       P -> S (in strain: C57BL/6J).
FT                                {ECO:0000269|PubMed:16141072}.
FT   VARIANT     694    694       E -> D (in strain: LG/J and NOD).
FT                                {ECO:0000269|PubMed:15919810,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     696    696       I -> F (in strain: NOD).
FT                                {ECO:0000269|PubMed:16141072}.
FT   VARIANT     777    777       S -> P (in strain: LG/J and NOD).
FT                                {ECO:0000269|PubMed:15919810,
FT                                ECO:0000269|PubMed:16141072}.
FT   VARIANT     782    782       E -> G (in strain: LG/J and NOD).
FT                                {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
//
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