ALDR_MOUSE
ID ALDR_MOUSE Reviewed; 316 AA.
AC P45376; O70130; Q99KC9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Aldo-keto reductase family 1 member B1;
DE EC=1.1.1.300 {ECO:0000250|UniProtKB:P15121};
DE EC=1.1.1.372 {ECO:0000250|UniProtKB:P15121};
DE EC=1.1.1.54 {ECO:0000250|UniProtKB:P15121};
DE AltName: Full=Aldehyde reductase;
DE AltName: Full=Aldo-keto reductase family 1 member B3 {ECO:0000312|MGI:MGI:1353494};
DE AltName: Full=Aldose reductase;
DE Short=AR;
DE EC=1.1.1.21 {ECO:0000269|PubMed:7851421};
GN Name=Akr1b1;
GN Synonyms=Akr1b3 {ECO:0000312|MGI:MGI:1353494}, Aldor1, Aldr1,
GN Alr2 {ECO:0000303|PubMed:10913167};
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], TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=7851421; DOI=10.1111/j.1432-1033.1995.tb20408.x;
RA Gui T., Tanimoto T., Kokai Y., Nishimura C.;
RT "Presence of a closely related subgroup in the aldo-ketoreductase family of
RT the mouse.";
RL Eur. J. Biochem. 227:448-453(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR X Swiss Webster; TISSUE=Liver;
RA Iwata T., Carper D.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Kidney;
RA Daoudal S., Berger M., Pailhoux E., Tournaire C., Veyssiere G., Jean C.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Ola;
RX PubMed=9485485;
RA McGowan M.H., Iwata T., Carper D.A.;
RT "Characterization of the mouse aldose reductase gene and promoter in a lens
RT epithelial cell line.";
RL Mol. Vis. 4:2-2(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=10092857; DOI=10.1046/j.1432-1327.1999.00110.x;
RA Ho H.T.B., Jenkins N.A., Copeland N.G., Gilbert D.J., Winkles J.A.,
RA Louie H.W.Y., Lee F.K., Chung S.S.M., Chung S.K.;
RT "Comparisons of genomic structures and chromosomal locations of the mouse
RT aldose reductase and aldose reductase-like genes.";
RL Eur. J. Biochem. 259:726-730(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=10049784; DOI=10.1006/bbrc.1999.0164;
RA Li H., Nobukuni Y., Gui T., Yabe-Nishimura C.;
RT "Characterization of genomic regions directing the cell-specific expression
RT of the mouse aldose reductase gene.";
RL Biochem. Biophys. Res. Commun. 255:759-764(1999).
RN [7]
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 [8]
RP PROTEIN SEQUENCE OF 156-169.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=10913167; DOI=10.1128/mcb.20.16.5840-5846.2000;
RA Ho H.T., Chung S.K., Law J.W., Ko B.C., Tam S.C., Brooks H.L.,
RA Knepper M.A., Chung S.S.;
RT "Aldose reductase-deficient mice develop nephrogenic diabetes insipidus.";
RL Mol. Cell. Biol. 20:5840-5846(2000).
RN [11]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP AND FUNCTION.
RX PubMed=17381426; DOI=10.1042/bj20061743;
RA Spite M., Baba S.P., Ahmed Y., Barski O.A., Nijhawan K., Petrash J.M.,
RA Bhatnagar A., Srivastava S.;
RT "Substrate specificity and catalytic efficiency of aldo-keto reductases
RT with phospholipid aldehydes.";
RL Biochem. J. 405:95-105(2007).
RN [12]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=19010934; DOI=10.1093/jb/mvn152;
RA Kabututu Z., Manin M., Pointud J.C., Maruyama T., Nagata N., Lambert S.,
RA Lefrancois-Martinez A.M., Martinez A., Urade Y.;
RT "Prostaglandin F2alpha synthase activities of aldo-keto reductase 1B1, 1B3
RT and 1B7.";
RL J. Biochem. 145:161-168(2009).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of
CC carbonyl-containing compounds to their corresponding alcohols
CC (PubMed:17381426, PubMed:19010934, PubMed:7851421). Displays enzymatic
CC activity towards endogenous metabolites such as aromatic and aliphatic
CC aldehydes, ketones, monosacharides, bile acids and xenobiotics
CC substrates. Key enzyme in the polyol pathway, catalyzes reduction of
CC glucose to sorbitol during hyperglycemia. Reduces steroids and their
CC derivatives and prostaglandins (PubMed:19010934). Displays low
CC enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis-
CC retinal. Catalyzes the reduction of diverse phospholipid aldehydes such
CC as 1-palmitoyl-2-(5-oxovaleroyl)-sn -glycero-3-phosphoethanolamin
CC (POVPC) and related phospholipid aldehydes that are generated from the
CC oxydation of phosphotidylcholine and phosphatdyleethanolamides
CC (PubMed:17381426). Plays a role in detoxifying dietary and lipid-
CC derived unsaturated carbonyls, such as crotonaldehyde, 4-
CC hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their
CC glutathione-conjugates carbonyls (GS-carbonyls) (By similarity).
CC {ECO:0000250|UniProtKB:P15121, ECO:0000269|PubMed:17381426,
CC ECO:0000269|PubMed:19010934, ECO:0000269|PubMed:7851421}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alditol + NADP(+) = an aldose + H(+) + NADPH;
CC Xref=Rhea:RHEA:12789, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.21;
CC Evidence={ECO:0000269|PubMed:7851421};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) +
CC NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.300; Evidence={ECO:0000250|UniProtKB:P15121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-retinol + NADP(+) = 9-cis-retinal + H(+) + NADPH;
CC Xref=Rhea:RHEA:54916, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273;
CC Evidence={ECO:0000250|UniProtKB:P15121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-retinol + NADP(+) = 13-cis-retinal + H(+) + NADPH;
CC Xref=Rhea:RHEA:54920, ChEBI:CHEBI:15378, ChEBI:CHEBI:45479,
CC ChEBI:CHEBI:45487, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:P15121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol + NADP(+) = D-glyceraldehyde + H(+) + NADPH;
CC Xref=Rhea:RHEA:23592, ChEBI:CHEBI:15378, ChEBI:CHEBI:17378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.372; Evidence={ECO:0000250|UniProtKB:P15121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol + NADP(+) = H(+) + L-glyceraldehyde + NADPH;
CC Xref=Rhea:RHEA:38111, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:27975, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.372; Evidence={ECO:0000250|UniProtKB:P15121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + prenol = 3-methyl-2-butenal + H(+) + NADPH;
CC Xref=Rhea:RHEA:58420, ChEBI:CHEBI:15378, ChEBI:CHEBI:15825,
CC ChEBI:CHEBI:16019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:P15121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-hex-2-en-1-ol + NADP(+) = (E)-hex-2-enal + H(+) + NADPH;
CC Xref=Rhea:RHEA:58424, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:141205;
CC Evidence={ECO:0000250|UniProtKB:P15121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E,E)-2,4-hexadien-1-ol + NADP(+) = (E,E)-2,4-hexadienal +
CC H(+) + NADPH; Xref=Rhea:RHEA:58428, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:82334,
CC ChEBI:CHEBI:142625; Evidence={ECO:0000250|UniProtKB:P15121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-hydroxynonen-1-ol + NADP(+) = a 4-hydroxynonenal + H(+) +
CC NADPH; Xref=Rhea:RHEA:58336, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:142593, ChEBI:CHEBI:142606;
CC Evidence={ECO:0000250|UniProtKB:P15121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin
CC H2; Xref=Rhea:RHEA:45312, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:19010934};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allyl alcohol + NADP(+) = acrolein + H(+) + NADPH;
CC Xref=Rhea:RHEA:12168, ChEBI:CHEBI:15368, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16605, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.54;
CC Evidence={ECO:0000250|UniProtKB:P15121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine
CC + H(+) + NADPH = 1-hexadecanoyl-2-(5-hydroxypentanoyl)-sn-glycero-3-
CC phosphocholine + NADP(+); Xref=Rhea:RHEA:58512, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77890,
CC ChEBI:CHEBI:142747; Evidence={ECO:0000269|PubMed:17381426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(7-oxoheptanoyl)-sn-glycero-3-phosphocholine
CC + H(+) + NADPH = 1-hexadecanoyl-2-(7-hydroxyheptanoyl)-sn-glycero-3-
CC phosphocholine + NADP(+); Xref=Rhea:RHEA:58752, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:134601,
CC ChEBI:CHEBI:142748; Evidence={ECO:0000269|PubMed:17381426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine +
CC H(+) + NADPH = 1-hexadecanoyl-2-(9-hydroxynonanoyl)-sn-glycero-3-
CC phosphocholine + NADP(+); Xref=Rhea:RHEA:58592, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61042,
CC ChEBI:CHEBI:142749; Evidence={ECO:0000269|PubMed:17381426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-
CC phosphoethanolamine + H(+) + NADPH = 1-hexadecanoyl-2-(5-
CC hydroxypentanoyl)-sn-glycero-3-phosphoethanolamine + NADP(+);
CC Xref=Rhea:RHEA:58756, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:142750, ChEBI:CHEBI:142751;
CC Evidence={ECO:0000269|PubMed:17381426};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=44 uM for D,L-glyceraldehyde {ECO:0000269|PubMed:7851421};
CC KM=5000 uM for D-xylose {ECO:0000269|PubMed:7851421};
CC KM=8200 uM for D-glucose {ECO:0000269|PubMed:7851421};
CC KM=4700 uM for D-galactose {ECO:0000269|PubMed:7851421};
CC KM=1040 uM for D-glucuronate {ECO:0000269|PubMed:7851421};
CC KM=18.7 uM for 1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-
CC phosphocholine {ECO:0000269|PubMed:17381426};
CC KM=13 uM for 1-hexadecanoyl-2-(7-oxoheptanoyl)-sn-glycero-3-
CC phosphocholine {ECO:0000269|PubMed:17381426};
CC KM=18 uM for 1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-
CC phosphocholine {ECO:0000269|PubMed:17381426};
CC KM=15 uM for 1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-
CC phosphoethanolamine {ECO:0000269|PubMed:17381426};
CC Note=kcat is 1.3 sec(-1) for D,L-glyceraldehyde as substrate. kcat is
CC 0.95 sec(-1) for D-xylose as substrate. kcat is 0.9 sec(-1) for D-
CC glucose as substrate. kcat is 1.1 sec(-1) for D-galactose as
CC substrate. kcat is 0.9 sec(-1) for D-glucuronate.
CC {ECO:0000269|PubMed:7851421};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P15121}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Abundant in the testis, skeletal muscle and kidney.
CC {ECO:0000269|PubMed:7851421}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice have no apparent developmental or
CC reproductive abnormality except a defect in their urine-concentrating
CC ability, which resulted in polyuria and polydipsia.
CC {ECO:0000269|PubMed:10913167}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; D32250; BAA06980.1; -; mRNA.
DR EMBL; L39795; AAA62176.1; -; mRNA.
DR EMBL; U29152; AAA69958.1; -; mRNA.
DR EMBL; U89150; AAC13358.1; -; Genomic_DNA.
DR EMBL; U89140; AAC13358.1; JOINED; Genomic_DNA.
DR EMBL; U89142; AAC13358.1; JOINED; Genomic_DNA.
DR EMBL; U89143; AAC13358.1; JOINED; Genomic_DNA.
DR EMBL; U89144; AAC13358.1; JOINED; Genomic_DNA.
DR EMBL; U89145; AAC13358.1; JOINED; Genomic_DNA.
DR EMBL; U89146; AAC13358.1; JOINED; Genomic_DNA.
DR EMBL; U89147; AAC13358.1; JOINED; Genomic_DNA.
DR EMBL; U89148; AAC13358.1; JOINED; Genomic_DNA.
DR EMBL; U89149; AAC13358.1; JOINED; Genomic_DNA.
DR EMBL; U93231; AAD32300.1; -; Genomic_DNA.
DR EMBL; U93230; AAD32300.1; JOINED; Genomic_DNA.
DR EMBL; AB016665; BAA76413.1; -; Genomic_DNA.
DR EMBL; BC004725; AAH04725.1; -; mRNA.
DR EMBL; BC021655; AAH21655.1; -; mRNA.
DR CCDS; CCDS19990.1; -.
DR PIR; I49484; I49484.
DR RefSeq; NP_033788.3; NM_009658.3.
DR AlphaFoldDB; P45376; -.
DR SMR; P45376; -.
DR BioGRID; 198069; 7.
DR IntAct; P45376; 3.
DR STRING; 10090.ENSMUSP00000100045; -.
DR ChEMBL; CHEMBL3108653; -.
DR SwissLipids; SLP:000001113; -.
DR iPTMnet; P45376; -.
DR PhosphoSitePlus; P45376; -.
DR SwissPalm; P45376; -.
DR COMPLUYEAST-2DPAGE; P45376; -.
DR REPRODUCTION-2DPAGE; IPI00223757; -.
DR REPRODUCTION-2DPAGE; P45376; -.
DR SWISS-2DPAGE; P45376; -.
DR EPD; P45376; -.
DR jPOST; P45376; -.
DR PaxDb; P45376; -.
DR PeptideAtlas; P45376; -.
DR PRIDE; P45376; -.
DR ProteomicsDB; 296092; -.
DR Antibodypedia; 4365; 592 antibodies from 42 providers.
DR DNASU; 11677; -.
DR Ensembl; ENSMUST00000102980; ENSMUSP00000100045; ENSMUSG00000001642.
DR GeneID; 11677; -.
DR KEGG; mmu:11677; -.
DR UCSC; uc009bgy.2; mouse.
DR CTD; 11677; -.
DR MGI; MGI:1353494; Akr1b3.
DR VEuPathDB; HostDB:ENSMUSG00000001642; -.
DR eggNOG; KOG1577; Eukaryota.
DR GeneTree; ENSGT00940000153272; -.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; P45376; -.
DR OMA; HCRFVNM; -.
DR OrthoDB; 1016440at2759; -.
DR PhylomeDB; P45376; -.
DR TreeFam; TF106492; -.
DR BRENDA; 1.1.1.21; 3474.
DR Reactome; R-MMU-196108; Pregnenolone biosynthesis.
DR Reactome; R-MMU-5652227; Fructose biosynthesis.
DR SABIO-RK; P45376; -.
DR BioGRID-ORCS; 11677; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Akr1b3; mouse.
DR PRO; PR:P45376; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P45376; protein.
DR Bgee; ENSMUSG00000001642; Expressed in urinary bladder and 111 other tissues.
DR ExpressionAtlas; P45376; baseline and differential.
DR Genevisible; P45376; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0042629; C:mast cell granule; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0033010; C:paranodal junction; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032838; C:plasma membrane bounded cell projection cytoplasm; ISO:MGI.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; ISO:MGI.
DR GO; GO:0097454; C:Schwann cell microvillus; ISO:MGI.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:MGI.
DR GO; GO:0047655; F:allyl-alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0018505; F:cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase activity; ISO:MGI.
DR GO; GO:0043795; F:glyceraldehyde oxidoreductase activity; ISO:MGI.
DR GO; GO:0047956; F:glycerol dehydrogenase [NADP+] activity; IEA:RHEA.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0036130; F:prostaglandin H2 endoperoxidase reductase activity; IEA:RHEA.
DR GO; GO:0001758; F:retinal dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0071475; P:cellular hyperosmotic salinity response; ISO:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0097238; P:cellular response to methylglyoxal; ISO:MGI.
DR GO; GO:0044597; P:daunorubicin metabolic process; ISO:MGI.
DR GO; GO:0044598; P:doxorubicin metabolic process; ISO:MGI.
DR GO; GO:0002070; P:epithelial cell maturation; IMP:MGI.
DR GO; GO:0046370; P:fructose biosynthetic process; IMP:MGI.
DR GO; GO:0072061; P:inner medullary collecting duct development; ISO:MGI.
DR GO; GO:0072205; P:metanephric collecting duct development; IMP:MGI.
DR GO; GO:0005996; P:monosaccharide metabolic process; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0042415; P:norepinephrine metabolic process; ISO:MGI.
DR GO; GO:1901360; P:organic cyclic compound metabolic process; ISO:MGI.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0035809; P:regulation of urine volume; IDA:MGI.
DR GO; GO:0003091; P:renal water homeostasis; IMP:MGI.
DR GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR GO; GO:0009414; P:response to water deprivation; ISO:MGI.
DR GO; GO:0001523; P:retinoid metabolic process; ISS:UniProtKB.
DR GO; GO:0006061; P:sorbitol biosynthetic process; ISO:MGI.
DR GO; GO:0031098; P:stress-activated protein kinase signaling cascade; ISO:MGI.
DR GO; GO:0001894; P:tissue homeostasis; 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 Acetylation; Cytoplasm; Direct protein sequencing; Lipid metabolism; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P16116"
FT CHAIN 2..316
FT /note="Aldo-keto reductase family 1 member B1"
FT /id="PRO_0000124624"
FT ACT_SITE 49
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P15121"
FT BINDING 10..19
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 211..273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P15121"
FT SITE 78
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P16116"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07943"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P15121"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P15121"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P15121"
FT CONFLICT 46
FT /note="A -> S (in Ref. 1; BAA06980)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="A -> G (in Ref. 4; AAC13358)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="V -> L (in Ref. 7; AAH04725/AAH21655)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 35732 MW; E18759AD160B4A0E CRC64;
MASHLELNNG TKMPTLGLGT WKSPPGQVTE AVKVAIDLGY RHIDCAQVYQ NEKEVGVALQ
EKLKEQVVKR QDLFIVSKLW CTFHDKSMVK GAFQKTLSDL QLDYLDLYLI HWPTGFKPGP
DYFPLDASGN VIPSDTDFVD TWTAMEQLVD EGLVKTIGVS NFNPLQIERI LNKPGLKYKP
AVNQIECHPY LTQEKLIEYC HSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK
YNKTTAQVLI RFPIQRNLVV IPKSVTPVRI AENLKVFDFE VSSEDMATLL SYNRNWRVCA
LMSCAKHKDY PFHAEV
