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   02-SEP-2026, entry version 201.
DE   RecName: Full=Aldo-keto reductase family 1 member B1;
DE            EC=1.1.1.21 {ECO:0000269|PubMed:7851421};
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;
GN   Name=Akr1b1;
GN   Synonyms=Akr1b3 {ECO:0000312|MGI:MGI:1353494}, Aldor1, Aldr1, Alr2
GN   {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,
RC   Pancreas, 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, monosaccharides, bile acids and xenobiotics
CC       substrates (PubMed:17381426, PubMed:19010934, PubMed:7851421). It
CC       catalyzes the reduction of glucose to sorbitol, the first step of the
CC       polyol pathway, an alternative route of glucose metabolism that
CC       converts glucose to fructose. This pathway becomes highly active under
CC       elevated glucose levels, such as during hyperglycemia (By similarity).
CC       Reduces steroids and their derivatives and prostaglandins
CC       (PubMed:19010934). Displays low enzymatic activity toward all-trans-
CC       retinal, 9-cis-retinal, and 13-cis-retinal. Catalyzes the reduction of
CC       diverse phospholipid aldehydes such as 1-palmitoyl-2-(5-oxovaleroyl)-sn
CC       -glycero-3-phosphoethanolamin (POVPC) and related phospholipid
CC       aldehydes that are generated from the oxydation of phosphotidylcholine
CC       and phosphatdyleethanolamides (PubMed:17381426). Plays a role in
CC       detoxifying dietary and lipid-derived unsaturated carbonyls, such as
CC       crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal
CC       and their glutathione-conjugates carbonyls (GS-carbonyls) (By
CC       similarity). {ECO:0000250|UniProtKB:P15121,
CC       ECO:0000269|PubMed:17381426, ECO:0000269|PubMed:19010934,
CC       ECO:0000269|PubMed:7851421}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alditol + NADP(+) = an aldose + NADPH + H(+);
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       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12791;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-sorbitol + NADP(+) = D-glucose + NADPH + H(+);
CC         Xref=Rhea:RHEA:59924, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17924, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:59926;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=erythritol + NADP(+) = D-erythrose + NADPH + H(+);
CC         Xref=Rhea:RHEA:59928, ChEBI:CHEBI:15378, ChEBI:CHEBI:17113,
CC         ChEBI:CHEBI:27904, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=xylitol + NADP(+) = D-xylose + NADPH + H(+);
CC         Xref=Rhea:RHEA:27445, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC         ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arabinitol + NADP(+) = L-arabinose + NADPH + H(+);
CC         Xref=Rhea:RHEA:25229, ChEBI:CHEBI:15378, ChEBI:CHEBI:17535,
CC         ChEBI:CHEBI:18403, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.21;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=galactitol + NADP(+) = D-galactose + NADPH + H(+);
CC         Xref=Rhea:RHEA:37967, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16813, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.21;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ribitol + NADP(+) = D-ribose + NADPH + H(+);
CC         Xref=Rhea:RHEA:59932, ChEBI:CHEBI:15378, ChEBI:CHEBI:15963,
CC         ChEBI:CHEBI:47013, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-gulonate + NADP(+) = aldehydo-D-glucuronate + NADPH + H(+);
CC         Xref=Rhea:RHEA:14909, ChEBI:CHEBI:13115, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142686;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + NADPH +
CC         H(+); 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 + NADPH + H(+);
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 + NADPH + H(+);
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 + NADPH + H(+);
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(+) = L-glyceraldehyde + NADPH + H(+);
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=benzyl alcohol + NADP(+) = benzaldehyde + NADPH + H(+);
CC         Xref=Rhea:RHEA:59944, ChEBI:CHEBI:15378, ChEBI:CHEBI:17169,
CC         ChEBI:CHEBI:17987, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:P15121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prenol + NADP(+) = 3-methyl-2-butenal + NADPH + H(+);
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 + NADPH + H(+);
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         NADPH + H(+); 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 + NADPH +
CC         H(+); 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=prostaglandin F2alpha + NADP(+) = prostaglandin H2 + NADPH +
CC         H(+); 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 + NADPH + H(+);
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         + NADPH + H(+) = 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         + NADPH + H(+) = 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         NADPH + H(+) = 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 + NADPH + H(+) = 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   -!- ACTIVITY REGULATION: Cys-299 acts as a redox-sensitive regulatory site.
CC       Its thiol group undergoes reversible oxidative and nitrosative
CC       modifications (S-nitrosylation, S-glutathiolation) that modulate enzyme
CC       activity, linking AKR1B1 function to the cellular redox environment.
CC       Tolrestat inhibits retinal reduction. {ECO:0000250|UniProtKB:P15121}.
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
CC         1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine
CC         {ECO:0000269|PubMed:17381426};
CC         KM=13 uM for
CC         1-hexadecanoyl-2-(7-oxoheptanoyl)-sn-glycero-3-phosphocholine
CC         {ECO:0000269|PubMed:17381426};
CC         KM=18 uM for
CC         1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine
CC         {ECO:0000269|PubMed:17381426};
CC         KM=15 uM for
CC         1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphoethanolamine
CC         {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
CC         D-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; 9.
DR   FunCoup; P45376; 1578.
DR   IntAct; P45376; 3.
DR   STRING; 10090.ENSMUSP00000100045; -.
DR   ChEMBL; CHEMBL3108653; -.
DR   SwissLipids; SLP:000001113; -.
DR   GlyGen; P45376; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P45376; -.
DR   PhosphoSitePlus; P45376; -.
DR   SwissPalm; P45376; -.
DR   REPRODUCTION-2DPAGE; IPI00223757; -.
DR   REPRODUCTION-2DPAGE; P45376; -.
DR   jPOST; P45376; -.
DR   PaxDb; 10090-ENSMUSP00000100045; -.
DR   PeptideAtlas; P45376; -.
DR   ProteomicsDB; 296092; -.
DR   Pumba; P45376; -.
DR   Antibodypedia; 4365; 624 antibodies from 45 providers.
DR   DNASU; 11677; -.
DR   Ensembl; ENSMUST00000102980.11; ENSMUSP00000100045.5; ENSMUSG00000001642.19.
DR   GeneID; 11677; -.
DR   KEGG; mmu:11677; -.
DR   UCSC; uc009bgy.2; mouse.
DR   AGR; MGI:1353494; -.
DR   CTD; 231; -.
DR   MGI; MGI:1353494; Akr1b1.
DR   VEuPathDB; HostDB:ENSMUSG00000001642; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   GeneTree; ENSGT00940000153272; -.
DR   HOGENOM; CLU_023205_0_0_1; -.
DR   InParanoid; P45376; -.
DR   OMA; VHWPSEG; -.
DR   OrthoDB; 416253at2759; -.
DR   PhylomeDB; P45376; -.
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 83 CRISPR screens.
DR   PRO; PR:P45376; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P45376; protein.
DR   Bgee; ENSMUSG00000001642; Expressed in urinary bladder and 114 other cell types or tissues.
DR   ExpressionAtlas; P45376; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; ISO:GO_Central.
DR   GO; GO:0042629; C:mast cell granule; ISO:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0033010; C:paranodal junction; ISO:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:GO_Central.
DR   GO; GO:0032838; C:plasma membrane bounded cell projection cytoplasm; ISO:GO_Central.
DR   GO; GO:0043220; C:Schmidt-Lanterman incisure; ISO:GO_Central.
DR   GO; GO:0097454; C:Schwann cell microvillus; ISO:GO_Central.
DR   GO; GO:0004032; F:aldose reductase (NADPH) activity; IDA:MGI.
DR   GO; GO:0052650; F:all-trans-retinol dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR   GO; GO:0047655; F:allyl-alcohol dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0018505; F:cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase activity; ISO:GO_Central.
DR   GO; GO:0032866; F:D-xylose reductase (NADPH) activity; IEA:RHEA.
DR   GO; GO:0043795; F:glyceraldehyde oxidoreductase activity; ISO:GO_Central.
DR   GO; GO:0047956; F:glycerol dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR   GO; GO:0032867; F:L-arabinose reductase (NADPH) activity; IEA:RHEA.
DR   GO; GO:0047939; F:L-glucuronate reductase activity; IMP:MGI.
DR   GO; GO:0036130; F:prostaglandin H2 endoperoxidase reductase activity; EXP:UniProtKB.
DR   GO; GO:0001758; F:retinal dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0071475; P:cellular hyperosmotic salinity response; ISO:GO_Central.
DR   GO; GO:0006060; P:D-sorbitol metabolic process; ISS:UniProtKB.
DR   GO; GO:0044597; P:daunorubicin metabolic process; ISO:GO_Central.
DR   GO; GO:0044598; P:doxorubicin metabolic process; ISO:GO_Central.
DR   GO; GO:0002070; P:epithelial cell maturation; IMP:MGI.
DR   GO; GO:0046370; P:fructose biosynthetic process; IMP:MGI.
DR   GO; GO:0072205; P:metanephric collecting duct development; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP: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:0001523; P:retinoid metabolic process; ISS:UniProtKB.
DR   CDD; cd19107; AKR_AKR1B1-19; 1.
DR   FunFam; 3.20.20.100:FF:000009; Aldo-keto reductase family 1 member B1; 1.
DR   Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR036812; NAD(P)_OxRdtase_dom_sf.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   PANTHER; PTHR11732; ALDO/KETO REDUCTASE; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 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         20
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         21
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         22
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         44
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         49
FT                   /ligand="alpha-D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58225"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         112
FT                   /ligand="alpha-D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58225"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         160
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         161
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         211
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         213
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         215
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         263
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         264
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         265
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         266
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         269
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         272
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         273
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   BINDING         299
FT                   /ligand="alpha-D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58225"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   SITE            78
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
FT   SITE            299
FT                   /note="Redox-sensitive site"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
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
//