Reviewed, UniProtKB/Swiss-Prot Q9DCT1 (AKCL2_MOUSE)

Names and origin

Protein names

Recommended name:
    1,5-anhydro-D-fructose reductase
      Short name=AF reductase
    EC=1.1.1.263
Alternative name(s):
    Aldo-keto reductase family 1 member C-like protein 2
    Aldo-keto reductase family 1 member E1

Gene names

Name:	Akr1e1
Synonyms:	Akr1cl2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. Can also catalyze the reduction of various aldehydes and quinones.
Catalytic activity	1,5-anhydro-D-glucitol + NADP+ = 1,5-anhydro-D-fructose + NADPH.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the aldo/keto reductase family.
Biophysicochemical properties	Kinetic parameters: KM=1.02 mM for 1,5-anhydro-D-fructose Vmax=0.57 µmol/min/mg enzyme

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 301	301	1,5-anhydro-D-fructose reductase		PRO_0000124673
Sites
	Active site	40	1	Proton donor By similarity
	Binding site	102	1	Substrate By similarity
	Site	69	1	Lowers pKa of active site Tyr By similarity
Experimental info
	Sequence conflict	105	1	M → I in AAB37274. Ref.1
	Sequence conflict	283	1	L → F in AAB37274. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9DCT1-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 5633663685EF32CA	FASTA	301	34,461
	10 20 30 40 50 60 MENIPTVGLG TWKASPGEVT DAVKLAINLG YRHFDCAYLY HNESEVGMGI SEKIKEGVVK 70 80 90 100 110 120 REDLFVVSKL WCTCHKKSLV KTACTNTLEA LNLDYLDLYL IHWPMGFKPG EKDIPLDRNG 130 140 150 160 170 180 KVIPSHTSFL DTWEAMEDLV FEGLVKNLGV SNFNHEQLER LLDKPGLRVR PITNQIECHP 190 200 210 220 230 240 YLNQKKLIDF CHKRNVSVTA YRPLGGSGGG FHLMDDTVIR KIAKKHGKSP AQILIRFQIQ 250 260 270 280 290 300 RNLIVIPKSV TPSRIRENIQ VFDFELTEKD MEELLSLDKN LRLATFPTTE NHQDYPFHIE Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a novel murine aldo-keto reductase." Bohren K.M., Barski O.A., Gabbay K.H. (In) Weiner H. (eds.); Enzymology and molecular biology of carbonyl metabolism 6, pp.1-1, Plenum Press, New York (1996) Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Strain: 129/Sv. Tissue: Liver.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary tumor.
[4]	"Mouse AKR1E1 is an ortholog of pig liver NADPH dependent 1,5-anhydro-D-fructose reductase." Sakuma M., Kubota S. Biosci. Biotechnol. Biochem. 72:872-876(2008) [PubMed: 18323634] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. Strain: C57BL/6J.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U68535 mRNA. Translation: AAB37274.1. AK002507 mRNA. Translation: BAB22152.1. BC012692 mRNA. Translation: AAH12692.1.
IPI	IPI00121305.
RefSeq	NP_061347.2.
UniGene	Mm.251908
3D structure databases
HSSP	HSSP built from PDB template 1AZ1 based on UniProtKB P15121.
ModBase	Search...
Proteomic databases
PRIDE	Q9DCT1.
Genome annotation databases
Ensembl	ENSMUSG00000045410. Mus musculus. [Contig view]
GeneID	56043.
KEGG	mmu:56043.
Organism-specific databases
MGI	MGI:1914758. Akr1e1.
Phylogenomic databases
HOGENOM	Q9DCT1.
HOVERGEN	Q9DCT1.
Gene expression databases
ArrayExpress	Q9DCT1.
Bgee	Q9DCT1.
CleanEx	MM_AKR1E1.
GermOnline	ENSMUSG00000045410. Mus musculus.
Family and domain databases
InterPro	IPR001395. Aldo/ket_red. IPR018170. Aldo/ket_reductase_CS. [Graphical view]
Gene3D	G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHER	PTHR11732. Aldo/ket_red. 1 hit.
Pfam	PF00248. Aldo_ket_red. 1 hit. [Graphical view]
ProDom	PD000288. Aldo/ket_red. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00798. ALDOKETO_REDUCTASE_1. 1 hit. PS00062. ALDOKETO_REDUCTASE_2. 1 hit. PS00063. ALDOKETO_REDUCTASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	311808.
SOURCE	Search...

Entry information

Entry name

AKCL2_MOUSE

Accession

Primary (citable) accession number: Q9DCT1
Secondary accession number(s): O09125

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2002
Last sequence update:	June 1, 2001
Last modified:	July 7, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)