AKCL2_MOUSE
ID AKCL2_MOUSE Reviewed; 301 AA.
AC Q9DCT1; O09125;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=1,5-anhydro-D-fructose reductase;
DE Short=AF reductase;
DE EC=1.1.1.263 {ECO:0000269|PubMed:18323634};
DE AltName: Full=Aldo-keto reductase family 1 member C-like protein 2;
DE AltName: Full=Aldo-keto reductase family 1 member E1;
DE AltName: Full=Aldo-keto reductase family 1 member E2;
GN Name=Akr1e2; Synonyms=Akr1cl2, Akr1e1;
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 CHARACTERIZATION.
RC STRAIN=129/Sv; TISSUE=Liver;
RA Bohren K.M., Barski O.A., Gabbay K.H.;
RT "Characterization of a novel murine aldo-keto reductase.";
RL (In) Weiner H. (eds.);
RL Enzymology and molecular biology of carbonyl metabolism 6, pp.1-1, Plenum
RL Press, New York (1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 TISSUE=Mammary tumor;
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 FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=C57BL/6J;
RX PubMed=18323634; DOI=10.1271/bbb.70612;
RA Sakuma M., Kubota S.;
RT "Mouse AKR1E1 is an ortholog of pig liver NADPH dependent 1,5-anhydro-D-
RT fructose reductase.";
RL Biosci. Biotechnol. Biochem. 72:872-876(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-
CC fructose (AF) to 1,5-anhydro-D-glucitol. {ECO:0000269|PubMed:18323634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,5-anhydro-D-glucitol + NADP(+) = 1,5-anhydro-D-fructose +
CC H(+) + NADPH; Xref=Rhea:RHEA:20665, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16070, ChEBI:CHEBI:16715, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.263;
CC Evidence={ECO:0000269|PubMed:18323634};
CC -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoic acid and
CC alkyliodines. {ECO:0000250|UniProtKB:P82125}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.02 mM for 1,5-anhydro-D-fructose {ECO:0000269|PubMed:18323634};
CC Vmax=0.57 umol/min/mg enzyme {ECO:0000269|PubMed:18323634};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P82125}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; U68535; AAB37274.1; -; mRNA.
DR EMBL; AK002507; BAB22152.1; -; mRNA.
DR EMBL; BC012692; AAH12692.1; -; mRNA.
DR CCDS; CCDS26226.1; -.
DR RefSeq; NP_061347.2; NM_018859.2.
DR AlphaFoldDB; Q9DCT1; -.
DR SMR; Q9DCT1; -.
DR STRING; 10090.ENSMUSP00000089459; -.
DR iPTMnet; Q9DCT1; -.
DR PhosphoSitePlus; Q9DCT1; -.
DR EPD; Q9DCT1; -.
DR jPOST; Q9DCT1; -.
DR MaxQB; Q9DCT1; -.
DR PaxDb; Q9DCT1; -.
DR PeptideAtlas; Q9DCT1; -.
DR PRIDE; Q9DCT1; -.
DR ProteomicsDB; 285798; -.
DR Antibodypedia; 23956; 176 antibodies from 27 providers.
DR DNASU; 56043; -.
DR Ensembl; ENSMUST00000091848; ENSMUSP00000089459; ENSMUSG00000045410.
DR GeneID; 56043; -.
DR KEGG; mmu:56043; -.
DR UCSC; uc007pjs.1; mouse.
DR CTD; 56043; -.
DR MGI; MGI:1914758; Akr1e1.
DR VEuPathDB; HostDB:ENSMUSG00000045410; -.
DR eggNOG; KOG1577; Eukaryota.
DR GeneTree; ENSGT00940000153272; -.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; Q9DCT1; -.
DR OMA; AEMYANE; -.
DR OrthoDB; 1016440at2759; -.
DR PhylomeDB; Q9DCT1; -.
DR TreeFam; TF106492; -.
DR BRENDA; 1.1.1.292; 3474.
DR SABIO-RK; Q9DCT1; -.
DR BioGRID-ORCS; 56043; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q9DCT1; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9DCT1; protein.
DR Bgee; ENSMUSG00000045410; Expressed in right kidney and 232 other tissues.
DR ExpressionAtlas; Q9DCT1; baseline and differential.
DR Genevisible; Q9DCT1; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050571; F:1,5-anhydro-D-fructose reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:MGI.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..301
FT /note="1,5-anhydro-D-fructose reductase"
FT /id="PRO_0000124673"
FT ACT_SITE 40
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 175
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 246..258
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT SITE 69
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:P14550"
FT CONFLICT 105
FT /note="M -> I (in Ref. 1; AAB37274)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="L -> F (in Ref. 1; AAB37274)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 34461 MW; 5633663685EF32CA CRC64;
MENIPTVGLG TWKASPGEVT DAVKLAINLG YRHFDCAYLY HNESEVGMGI SEKIKEGVVK
REDLFVVSKL WCTCHKKSLV KTACTNTLEA LNLDYLDLYL IHWPMGFKPG EKDIPLDRNG
KVIPSHTSFL DTWEAMEDLV FEGLVKNLGV SNFNHEQLER LLDKPGLRVR PITNQIECHP
YLNQKKLIDF CHKRNVSVTA YRPLGGSGGG FHLMDDTVIR KIAKKHGKSP AQILIRFQIQ
RNLIVIPKSV TPSRIRENIQ VFDFELTEKD MEELLSLDKN LRLATFPTTE NHQDYPFHIE
Y
