ID   ALDR_DROME              Reviewed;         350 AA.
AC   M9PF61; M9PI17; Q8IQF8; Q9VTK9;
DT   27-NOV-2024, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 1.
DT   04-NOV-2026, entry version 88.
DE   RecName: Full=Aldo-keto reductase 1B {ECO:0000312|FlyBase:FBgn0086254};
DE            EC=1.1.1.21 {ECO:0000250|UniProtKB:P15121};
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=Aldose reductase {ECO:0000303|PubMed:31350199};
DE            Short=dAR1 {ECO:0000303|PubMed:31350199};
GN   Name=Ar1 {ECO:0000303|PubMed:31350199,
GN   ECO:0000312|FlyBase:FBgn0086254};
GN   Synonyms=Akr1B {ECO:0000312|FlyBase:FBgn0086254};
GN   ORFNames=CG6084 {ECO:0000312|FlyBase:FBgn0086254};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN   [1] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3] {ECO:0000312|EMBL:AAO25037.1, ECO:0000312|EMBL:AAR96205.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAO25037.1,
RC   ECO:0000312|EMBL:AAR96205.1};
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000305}
RP   FUNCTION, INDUCTION BY GRAM-NEGATIVE BACTERIA INFECTION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=31350199; DOI=10.1016/j.chom.2019.07.001;
RA   Yang S., Zhao Y., Yu J., Fan Z., Gong S.T., Tang H., Pan L.;
RT   "Sugar Alcohols of Polyol Pathway Serve as Alarmins to Mediate Local-
RT   Systemic Innate Immune Communication in Drosophila.";
RL   Cell Host Microbe 26:240-251.e8(2019).
RN   [5] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=38283991; DOI=10.3389/fcell.2023.1257751;
RA   Mellentine S.Q., Brown H.N., Ramsey A.S., Li J., Tootle T.L.;
RT   "Specific prostaglandins are produced in the migratory cells and the
RT   surrounding substrate to promote Drosophila border cell migration.";
RL   Front. Cell Dev. Biol. 11:1257751-1257751(2023).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of
CC       carbonyl-containing compounds to their corresponding alcohols. Displays
CC       enzymatic activity towards endogenous metabolites such as aromatic and
CC       aliphatic aldehydes, ketones, monosaccharides, bile acids and
CC       xenobiotics substrates. Key enzyme in the polyol pathway, catalyzes
CC       reduction of glucose to sorbitol during hyperglycemia. Reduces steroids
CC       and their derivatives and prostaglandins (By similarity). Through
CC       production of prostaglandin F2alpha may regulate the activity of non-
CC       muscle myosin II in an autocrine or paracrine fashion; influences
CC       border cell and nurse cell stiffness to facilitate border cell cluster
CC       migration (PubMed:38283991). Also regulates the cell surface
CC       localization of integrins in an autocrine or paracrine fashion;
CC       influences border cell adhesion to maintain border cell cluster
CC       morphology (PubMed:38283991). In hemocytes, probably contributes to
CC       production of sugar alcohols in the hemolymph, which act as alarmins
CC       involved in gut-fat body innate immunological communication (GFIC);
CC       leads to activation of the imd/Relish signaling pathway in the fat body
CC       (PubMed:31350199). {ECO:0000250|UniProtKB:P15121,
CC       ECO:0000269|PubMed:31350199, ECO:0000269|PubMed:38283991}.
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: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=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:0000250|UniProtKB:P15121};
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=pyridine 3-methanol + NADP(+) = pyridine-3-carbaldehyde +
CC         NADPH + H(+); Xref=Rhea:RHEA:58776, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28345, ChEBI:CHEBI:45213, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; 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:0000250|UniProtKB:P15121};
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:0000250|UniProtKB:P15121};
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:0000250|UniProtKB:P15121};
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:0000250|UniProtKB:P15121};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:38283991}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=C {ECO:0000312|FlyBase:FBgn0086254};
CC         IsoId=M9PF61-1; Sequence=Displayed;
CC       Name=D {ECO:0000312|FlyBase:FBgn0086254};
CC         IsoId=M9PF61-2; Sequence=VSP_062421, VSP_062422, VSP_062423;
CC       Name=B {ECO:0000312|FlyBase:FBgn0086254};
CC         IsoId=M9PF61-3; Sequence=VSP_062423;
CC       Name=A {ECO:0000312|FlyBase:FBgn0086254};
CC         IsoId=M9PF61-4; Sequence=VSP_062421, VSP_062422;
CC   -!- DEVELOPMENTAL STAGE: Expressed in both germline and somatic cells in
CC       the follicle during oogenesis. {ECO:0000269|PubMed:38283991}.
CC   -!- INDUCTION: By oral infection with Gram-negative bacteria; induced in
CC       hemocytes but not in the fat body. {ECO:0000269|PubMed:31350199}.
CC   -!- DISRUPTION PHENOTYPE: More compact border cell clusters that are
CC       delayed in their migration during oogenesis (PubMed:38283991).
CC       Integrins fail to localize to the cell surface in border cells
CC       (PubMed:38283991). Impaired IMD signaling pathway response in the fat
CC       body, but not in the gut, upon Gram-negative bacteria infection
CC       (PubMed:31350199). Conditional RNAi-mediated knockdown in oocyte
CC       somatic cells slightly delays border cell migration and produces a more
CC       compact border cell cluster (PubMed:38283991). Conditional RNAi-
CC       mediated knockdown in oocyte germline cells has no effect on border
CC       cell migration but results in an elongated border cell cluster
CC       (PubMed:38283991). Conditional RNAi-mediated knockdown in hemocytes
CC       reduces the gut-fat body innate immunological communication (GFIC)
CC       response to oral infection by Gram-negative bacteria; RNAi-mediated
CC       knockdown in the fat body or in the gut has no effect upon GFIC
CC       (PubMed:31350199). {ECO:0000269|PubMed:31350199,
CC       ECO:0000269|PubMed:38283991}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014296; AAF50039.2; -; Genomic_DNA.
DR   EMBL; AE014296; AAN11878.1; -; Genomic_DNA.
DR   EMBL; AE014296; AGB94410.1; -; Genomic_DNA.
DR   EMBL; AE014296; AGB94411.1; -; Genomic_DNA.
DR   EMBL; BT003280; AAO25037.1; -; mRNA.
DR   EMBL; BT011413; AAR96205.1; -; mRNA.
DR   RefSeq; NP_001261716.1; NM_001274787.1. [M9PF61-1]
DR   RefSeq; NP_001261717.1; NM_001274788.1. [M9PF61-2]
DR   RefSeq; NP_648484.1; NM_140227.2. [M9PF61-4]
DR   RefSeq; NP_729726.1; NM_168467.2. [M9PF61-3]
DR   AlphaFoldDB; M9PF61; -.
DR   SMR; M9PF61; -.
DR   FunCoup; M9PF61; 1091.
DR   IntAct; M9PF61; 206.
DR   GlyGen; M9PF61; 1 site, 1 O-linked glycan (1 site).
DR   PaxDb; 7227-FBpp0075869; -.
DR   PeptideAtlas; M9PF61; -.
DR   DNASU; 39304; -.
DR   EnsemblMetazoa; FBtr0331546; FBpp0303936; FBgn0086254.
DR   GeneID; 39304; -.
DR   KEGG; dme:Dmel_CG6084; -.
DR   AGR; FB:FBgn0086254; -.
DR   CTD; 39304; -.
DR   FlyBase; FBgn0086254; Ar1.
DR   VEuPathDB; VectorBase:FBgn0086254; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   HOGENOM; CLU_023205_0_0_1; -.
DR   InParanoid; M9PF61; -.
DR   OrthoDB; 416253at2759; -.
DR   Reactome; R-DME-193144; Estrogen biosynthesis.
DR   Reactome; R-DME-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR   Reactome; R-DME-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
DR   Reactome; R-DME-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR   Reactome; R-DME-196108; Pregnenolone biosynthesis.
DR   Reactome; R-DME-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR   Reactome; R-DME-5365859; RA biosynthesis pathway.
DR   Reactome; R-DME-5652227; Fructose biosynthesis.
DR   Reactome; R-DME-70221; Glycogen breakdown (glycogenolysis).
DR   Reactome; R-DME-975634; Retinoid metabolism and transport.
DR   Reactome; R-DME-9757110; Prednisone ADME.
DR   BioGRID-ORCS; 39304; 0 hits in 3 CRISPR screens.
DR   PRO; PR:M9PF61; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0086254; Expressed in secondary oocyte and 173 other cell types or tissues.
DR   ExpressionAtlas; M9PF61; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; EXP:UniProtKB.
DR   GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR   GO; GO:0005576; C:extracellular region; IDA:FlyBase.
DR   GO; GO:0005739; C:mitochondrion; ISS:FlyBase.
DR   GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR   GO; GO:0004032; F:aldose reductase (NADPH) activity; IDA:FlyBase.
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:0047681; F:aryl-alcohol dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0047956; F:glycerol dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR   GO; GO:0047939; F:L-glucuronate reductase activity; ISS:FlyBase.
DR   GO; GO:0036130; F:prostaglandin H2 endoperoxidase reductase activity; ISS:UniProtKB.
DR   GO; GO:0042840; P:D-glucuronate catabolic process; ISS:FlyBase.
DR   GO; GO:0006061; P:D-sorbitol biosynthetic process; IGI:FlyBase.
DR   GO; GO:0046370; P:fructose biosynthetic process; IGI:FlyBase.
DR   GO; GO:0046173; P:polyol biosynthetic process; IMP:FlyBase.
DR   FunFam; 3.20.20.100:FF:000006; Aldo-keto reductase family 1 member A1; 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   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..350
FT                   /note="Aldo-keto reductase 1B"
FT                   /id="PRO_0000461209"
FT   ACT_SITE        84
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PIRSR:PIRSR000097-1"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PIRSR:PIRSR000097-2"
FT   BINDING         244..306
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P15121"
FT   SITE            113
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000255|PIRSR:PIRSR000097-3"
FT   VAR_SEQ         1..50
FT                   /note="MNTLMKIQLVRPVFRITLRNYGKPERFMWCQKEYARAPKVVCLDGNEIPV
FT                   -> MAVPNVKFNNGKEVPI (in isoform D and isoform A)"
FT                   /id="VSP_062421"
FT   VAR_SEQ         56..57
FT                   /note="FN -> WG (in isoform D and isoform A)"
FT                   /id="VSP_062422"
FT   VAR_SEQ         336..347
FT                   /note="NQYGHPHHPFEK -> KDAGTHKYYPFH (in isoform D and
FT                   isoform B)"
FT                   /id="VSP_062423"
SQ   SEQUENCE   350 AA;  40137 MW;  2AF573E3293E594A CRC64;
     MNTLMKIQLV RPVFRITLRN YGKPERFMWC QKEYARAPKV VCLDGNEIPV IGLGTFNSPK
     GQVTEAVKVA IDAGYRHIDC AYVYQNEDEV GDGVEAKIKE GVVKREDLFI TSKLWNTFHR
     PDLVKSALEN TLSSLKLKYL DLYLIHWPMG YKEGCDLFPT DKDGKTLYSP VDYVDTWKAM
     EKLVEEGLVK SIGVSNFNRR QIERVLEVAT IPPVTNQIEC HPYLTQKKLI DFCKSKDITI
     TAYSPLGSPN RPWAKAGDPV ILEEAKIKEI AAKKKKTPGQ ILIRYQVQRA NIVIPKSVTK
     DRIESNFQVF DFELTPEEIE IIESFECNGR LVPLLNQYGH PHHPFEKDEY
//