FN3K_MOUSE
ID FN3K_MOUSE Reviewed; 309 AA.
AC Q9ER35; Q9D6N6;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Fructosamine-3-kinase {ECO:0000303|PubMed:11016445};
DE EC=2.7.1.171 {ECO:0000269|PubMed:11016445};
DE AltName: Full=Protein-psicosamine 3-kinase FN3K {ECO:0000305};
DE AltName: Full=Protein-ribulosamine 3-kinase FN3K {ECO:0000305};
DE EC=2.7.1.172 {ECO:0000250|UniProtKB:Q9H479};
GN Name=Fn3k {ECO:0000303|PubMed:11016445, ECO:0000312|MGI:MGI:1926834};
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], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Kidney;
RX PubMed=11016445; DOI=10.2337/diabetes.49.10.1627;
RA Delpierre G., Rider M.H., Collard F., Stroobant V., Vanstapel F.,
RA Santos H., Van Schaftingen E.;
RT "Identification, cloning, and heterologous expression of a mammalian
RT fructosamine-3-kinase.";
RL Diabetes 49:1627-1634(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 TISSUE SPECIFICITY.
RX PubMed=15331600; DOI=10.1074/jbc.m407678200;
RA Delplanque J., Delpierre G., Opperdoes F.R., Van Schaftingen E.;
RT "Tissue distribution and evolution of fructosamine 3-kinase and
RT fructosamine 3-kinase-related protein.";
RL J. Biol. Chem. 279:46606-46613(2004).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16819943; DOI=10.1042/bj20060684;
RA Veiga da-Cunha M., Jacquemin P., Delpierre G., Godfraind C., Theate I.,
RA Vertommen D., Clotman F., Lemaigre F., Devuyst O., Van Schaftingen E.;
RT "Increased protein glycation in fructosamine 3-kinase-deficient mice.";
RL Biochem. J. 399:257-264(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
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 [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=20009024; DOI=10.1152/ajpendo.00503.2009;
RA Pascal S.M., Veiga-da-Cunha M., Gilon P., Van Schaftingen E., Jonas J.C.;
RT "Effects of fructosamine-3-kinase deficiency on function and survival of
RT mouse pancreatic islets after prolonged culture in high glucose or ribose
RT concentrations.";
RL Am. J. Physiol. 298:E586-E596(2010).
RN [7]
RP FUNCTION.
RX PubMed=31398338; DOI=10.1016/j.cell.2019.07.031;
RA Sanghvi V.R., Leibold J., Mina M., Mohan P., Berishaj M., Li Z.,
RA Miele M.M., Lailler N., Zhao C., de Stanchina E., Viale A., Akkari L.,
RA Lowe S.W., Ciriello G., Hendrickson R.C., Wendel H.G.;
RT "The oncogenic action of NRF2 depends on de-glycation by fructosamine-3-
RT kinase.";
RL Cell 178:807-819(2019).
CC -!- FUNCTION: Fructosamine-3-kinase involved in protein deglycation by
CC mediating phosphorylation of fructoselysine residues on glycated
CC proteins, to generate fructoselysine-3 phosphate (PubMed:11016445,
CC PubMed:16819943). Fructoselysine-3 phosphate adducts are unstable and
CC decompose under physiological conditions (By similarity). Involved in
CC intracellular deglycation in erythrocytes and pancreatic islets
CC (PubMed:16819943, PubMed:20009024). Involved in the response to
CC oxidative stress by mediating deglycation of NFE2L2/NRF2, glycation
CC impairing NFE2L2/NRF2 function (PubMed:31398338). Also able to
CC phosphorylate psicosamines and ribulosamines (By similarity).
CC {ECO:0000250|UniProtKB:Q9H479, ECO:0000269|PubMed:11016445,
CC ECO:0000269|PubMed:16819943, ECO:0000269|PubMed:20009024,
CC ECO:0000269|PubMed:31398338}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-(D-fructosyl)-L-lysyl-[protein] = ADP + H(+) +
CC N(6)-(3-O-phospho-D-fructosyl)-L-lysyl-[protein];
CC Xref=Rhea:RHEA:59832, Rhea:RHEA-COMP:15451, Rhea:RHEA-COMP:15452,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:143253,
CC ChEBI:CHEBI:143254, ChEBI:CHEBI:456216; EC=2.7.1.171;
CC Evidence={ECO:0000269|PubMed:11016445};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59833;
CC Evidence={ECO:0000269|PubMed:11016445};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-D-ribulosyl-L-lysyl-[protein] = ADP + H(+) + N(6)-
CC (3-O-phospho-D-ribulosyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:48432,
CC Rhea:RHEA-COMP:12103, Rhea:RHEA-COMP:12104, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:90418, ChEBI:CHEBI:90420,
CC ChEBI:CHEBI:456216; EC=2.7.1.172;
CC Evidence={ECO:0000250|UniProtKB:Q9H479};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48433;
CC Evidence={ECO:0000250|UniProtKB:Q9H479};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-(D-psicosyl)-L-lysyl-[protein] = ADP + H(+) + N(6)-
CC (3-O-phospho-D-psicosyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:61392,
CC Rhea:RHEA-COMP:15796, Rhea:RHEA-COMP:15797, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:144621, ChEBI:CHEBI:144622,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9H479};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61393;
CC Evidence={ECO:0000250|UniProtKB:Q9H479};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9H479}.
CC -!- TISSUE SPECIFICITY: Expressed in red blood cells, brain, heart, kidney
CC and muscle (PubMed:15331600). Lower expression is observed in liver
CC (PubMed:15331600). Not expressed in lung, spleen, testis and thymus
CC (PubMed:15331600). {ECO:0000269|PubMed:15331600}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and healthy and show normal blood
CC glucose and serum fructosamine levels (PubMed:16819943). They however
CC display increased protein glycation levels in cells such as
CC erythrocytes and pancreatic islets (PubMed:16819943, PubMed:20009024).
CC Increased levels of protein glycation levels do not affect the
CC maintenance and function of pancreatic islets (PubMed:20009024).
CC {ECO:0000269|PubMed:16819943, ECO:0000269|PubMed:20009024}.
CC -!- SIMILARITY: Belongs to the fructosamine kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK010151; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ404616; CAC16407.1; -; mRNA.
DR EMBL; AK010151; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS25776.1; -.
DR RefSeq; NP_071297.1; NM_022014.4.
DR AlphaFoldDB; Q9ER35; -.
DR SMR; Q9ER35; -.
DR BioGRID; 210990; 1.
DR IntAct; Q9ER35; 1.
DR STRING; 10090.ENSMUSP00000026175; -.
DR iPTMnet; Q9ER35; -.
DR PhosphoSitePlus; Q9ER35; -.
DR SwissPalm; Q9ER35; -.
DR MaxQB; Q9ER35; -.
DR PaxDb; Q9ER35; -.
DR PRIDE; Q9ER35; -.
DR ProteomicsDB; 271703; -.
DR Antibodypedia; 33043; 174 antibodies from 26 providers.
DR DNASU; 63828; -.
DR Ensembl; ENSMUST00000026175; ENSMUSP00000026175; ENSMUSG00000025175.
DR GeneID; 63828; -.
DR KEGG; mmu:63828; -.
DR UCSC; uc007mvx.2; mouse.
DR CTD; 64122; -.
DR MGI; MGI:1926834; Fn3k.
DR VEuPathDB; HostDB:ENSMUSG00000025175; -.
DR eggNOG; KOG3021; Eukaryota.
DR GeneTree; ENSGT00390000005730; -.
DR HOGENOM; CLU_036517_0_1_1; -.
DR InParanoid; Q9ER35; -.
DR OMA; QSDWPSF; -.
DR OrthoDB; 943202at2759; -.
DR PhylomeDB; Q9ER35; -.
DR TreeFam; TF313452; -.
DR BRENDA; 2.7.1.171; 3474.
DR Reactome; R-MMU-163841; Gamma carboxylation, hypusine formation and arylsulfatase activation.
DR BioGRID-ORCS; 63828; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9ER35; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9ER35; protein.
DR Bgee; ENSMUSG00000025175; Expressed in interventricular septum and 144 other tissues.
DR ExpressionAtlas; Q9ER35; baseline and differential.
DR Genevisible; Q9ER35; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0102194; F:protein-fructosamine 3-kinase activity; IDA:MGI.
DR GO; GO:0102193; F:protein-ribulosamine 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0030389; P:fructosamine metabolic process; IDA:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0036525; P:protein deglycation; IMP:UniProtKB.
DR InterPro; IPR016477; Fructo-/Ketosamine-3-kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR12149; PTHR12149; 1.
DR Pfam; PF03881; Fructosamin_kin; 1.
DR PIRSF; PIRSF006221; Ketosamine-3-kinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..309
FT /note="Fructosamine-3-kinase"
FT /id="PRO_0000216338"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WI99"
FT BINDING 89..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HA64"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H479"
SQ SEQUENCE 309 AA; 35032 MW; 7FD29F83C4FE7874 CRC64;
MEQLLRAQLH TTTLRAFGSS GGGCISEGYA YYTDSGPVFV KVNRRTQARQ MFEGEMASLE
ALRNTGLVRV PKPMKVIDLP GGGAVFVMEH LKMKSLSSQA SKLGEQMADL HLYNQKLREK
SKTRQNTVGC GAEGAEPQGV TKFGFHTVTC CGFIPQVNEW QEDWPTFFTR HRLQAQLDLI
EKDYADRETQ ELWSRLQVKI PDLFAGIEIV PALLHGDLWS GNVAEDDQGP VIYDPASFYG
HSEFELAIAS MFGGFPRSFF TAYHRKIPKA PGFDKRLLLY QLFNYLNHWN HFGREYRSPS
LGVMRKLLR
