AK1BF_HUMAN
ID AK1BF_HUMAN Reviewed; 316 AA.
AC C9JRZ8; C9J3V2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Aldo-keto reductase family 1 member B15 {ECO:0000305};
DE EC=1.1.1.- {ECO:0000269|PubMed:25577493};
DE EC=1.1.1.300 {ECO:0000269|PubMed:26222439};
DE EC=1.1.1.54 {ECO:0000269|PubMed:26222439};
DE AltName: Full=Estradiol 17-beta-dehydrogenase AKR1B15 {ECO:0000305};
DE AltName: Full=Farnesol dehydrogenase {ECO:0000305|PubMed:26222439};
DE EC=1.1.1.216 {ECO:0000269|PubMed:26222439};
DE AltName: Full=Testosterone 17beta-dehydrogenase {ECO:0000305|PubMed:25577493};
DE EC=1.1.1.64 {ECO:0000269|PubMed:25577493};
GN Name=AKR1B15 {ECO:0000312|HGNC:HGNC:37281};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Eye, and Testis;
RX PubMed=21276782; DOI=10.1016/j.cbi.2011.01.020;
RA Salabei J.K., Li X.P., Petrash J.M., Bhatnagar A., Barski O.A.;
RT "Functional expression of novel human and murine AKR1B genes.";
RL Chem. Biol. Interact. 191:177-184(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY (ISOFORM 1),
RP BIOPHYSICOCHEMICAL PROPERTIES (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORMS 1
RP AND 2), ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=25577493; DOI=10.1074/jbc.m114.610121;
RA Weber S., Salabei J.K., Moller G., Kremmer E., Bhatnagar A., Adamski J.,
RA Barski O.A.;
RT "Aldo-keto reductase 1B15 (AKR1B15): a mitochondrial human aldo-keto
RT reductase with activity towards steroids and 3-keto-acyl-coa conjugates.";
RL J. Biol. Chem. 290:6531-6545(2015).
RN [5]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=26222439; DOI=10.1371/journal.pone.0134506;
RA Gimenez-Dejoz J., Kolar M.H., Ruiz F.X., Crespo I., Cousido-Siah A.,
RA Podjarny A., Barski O.A., Fanfrlik J., Pares X., Farres J., Porte S.;
RT "Substrate Specificity, Inhibitor Selectivity and Structure-Function
RT Relationships of Aldo-Keto Reductase 1B15: A Novel Human Retinaldehyde
RT Reductase.";
RL PLoS ONE 10:E0134506-E0134506(2015).
CC -!- FUNCTION: [Isoform 1]: Catalyzes the NADPH-dependent reduction of a
CC variety of carbonyl substrates, like aromatic aldehydes, alkenals,
CC ketones and alpha-dicarbonyl compounds (PubMed:26222439,
CC PubMed:21276782). In addition, catalyzes the reduction of androgens and
CC estrogens with high positional selectivity (shows 17-beta-
CC hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs
CC (PubMed:25577493). Displays strong enzymatic activity toward all-trans-
CC retinal and 9-cis-retinal (PubMed:26222439). May play a physiological
CC role in retinoid metabolism (PubMed:26222439).
CC {ECO:0000269|PubMed:21276782, ECO:0000269|PubMed:25577493,
CC ECO:0000269|PubMed:26222439}.
CC -!- FUNCTION: [Isoform 2]: No oxidoreductase activity observed with the
CC tested substrates. {ECO:0000269|PubMed:25577493}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH;
CC Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:25577493};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + testosterone = androst-4-ene-3,17-dione + H(+) +
CC NADPH; Xref=Rhea:RHEA:14981, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422,
CC ChEBI:CHEBI:17347, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.64;
CC Evidence={ECO:0000269|PubMed:25577493};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-hydroxy-5alpha-androstan-3-one + NADP(+) = 5alpha-
CC androstan-3,17-dione + H(+) + NADPH; Xref=Rhea:RHEA:42120,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16330,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:25577493};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta-hydroxyandrost-5-en-17-one + H(+) + NADPH = androst-5-
CC en-3beta,17beta-diol + NADP(+); Xref=Rhea:RHEA:46628,
CC ChEBI:CHEBI:2710, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:25577493};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3alpha-hydroxy-5alpha-androstan-17-one + H(+) + NADPH =
CC 5alpha-androstane-3alpha,17beta-diol + NADP(+); Xref=Rhea:RHEA:42156,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16032, ChEBI:CHEBI:36713,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:25577493};
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:0000269|PubMed:26222439};
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:0000269|PubMed:26222439};
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:0000269|PubMed:26222439};
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:0000269|PubMed:26222439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + nonan-2-one = (3E)-nonen-2-one + H(+) + NADPH;
CC Xref=Rhea:RHEA:50616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77927, ChEBI:CHEBI:133457;
CC Evidence={ECO:0000269|PubMed:26222439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesol + NADP(+) = (2E,6E)-farnesal + H(+) + NADPH;
CC Xref=Rhea:RHEA:14697, ChEBI:CHEBI:15378, ChEBI:CHEBI:15894,
CC ChEBI:CHEBI:16619, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.216; Evidence={ECO:0000269|PubMed:26222439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetoin + NADP(+) = diacetyl + H(+) + NADPH;
CC Xref=Rhea:RHEA:35607, ChEBI:CHEBI:15378, ChEBI:CHEBI:15688,
CC ChEBI:CHEBI:16583, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:26222439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-hydroxynon-2-en-1-ol + NADP(+) = (E)-4-hydroxynon-2-enal
CC + H(+) + NADPH; Xref=Rhea:RHEA:58416, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58968,
CC ChEBI:CHEBI:142617; Evidence={ECO:0000269|PubMed:26222439};
CC -!- ACTIVITY REGULATION: Inhibited by the inhibitor JF0064.
CC {ECO:0000269|PubMed:26222439}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.8 uM for androsterone (tested with isoform 1 in the reductive
CC reaction) {ECO:0000269|PubMed:25577493};
CC KM=1.9 uM for delta-4-androstenedione (tested with isoform 1 in the
CC reductive reaction) {ECO:0000269|PubMed:25577493};
CC KM=2.5 uM for estrone (tested with isoform 1 in the reductive
CC reaction) {ECO:0000269|PubMed:25577493};
CC KM=63.4 uM for acetoacetyl-CoA (tested with isoform 1 in the
CC reductive reaction) {ECO:0000269|PubMed:25577493};
CC KM=19.2 uM for 3-alpha,17-beta-androstandiol (tested with isoform 1
CC in the oxidative reaction) {ECO:0000269|PubMed:25577493};
CC KM=7.1 uM for testosterone (tested with isoform 1 in the oxidative
CC reaction) {ECO:0000269|PubMed:25577493};
CC KM=9.1 uM for 17-beta-estradiol (tested with isoform 1 in the
CC oxidative reaction) {ECO:0000269|PubMed:25577493};
CC KM=1 uM for all-trans-retinal {ECO:0000269|PubMed:26222439};
CC KM=0.16 uM for 9-cis-retinal {ECO:0000269|PubMed:26222439};
CC KM=880 uM for D,L-glyceraldehyde {ECO:0000269|PubMed:26222439};
CC KM=2.9 uM for pyridine-3-aldehyde {ECO:0000269|PubMed:26222439};
CC KM=3.1 uM for hexanal {ECO:0000269|PubMed:26222439};
CC KM=36 uM for acrolein {ECO:0000269|PubMed:26222439};
CC KM=5 uM for trans-2-hexenal {ECO:0000269|PubMed:26222439};
CC KM=2.2 uM for 4-hydroxy-2-nonenal {ECO:0000269|PubMed:26222439};
CC KM=1.7 uM for 3-nonen-2-one {ECO:0000269|PubMed:26222439};
CC KM=1 uM for 2,3-butanedione {ECO:0000269|PubMed:26222439};
CC KM=1 uM for farnesal {ECO:0000269|PubMed:26222439};
CC KM=5.7 uM for NADPH {ECO:0000269|PubMed:26222439};
CC Note=kcat is 1.7 min(-1) using isoform 1 for the reduction of
CC androsterone. kcat is 1.1 min(-1) using isoform 1 for the reduction
CC of delta-4-androstenedione. kcat is 1.0 min(-1) using isoform 1 for
CC the reduction of estrone. kcat is 0.5 min(-1) using isoform 1 for the
CC reduction of acetoacetyl-CoA. kcat is 3.0 min(-1) using isoform 1 for
CC the oxidation of 3-alpha,17-beta-androstandiol. kcat is 0.6 min(-1)
CC using isoform 1 for the oxidation of testosterone. kcat is 0.5 min(-
CC 1) using isoform 1 for the oxidation of 17-beta-estradiol
CC (PubMed:25577493). kcat is 10.7 min(-1) with D,L-glyceraldehyde as
CC substrate. kcat is 9 min(-1) with pyridine-3-aldehyde as substrate.
CC kcat is 7.3 min(-1) with hexanal as substrate. kcat is 9 min(-1) with
CC acrolein as substrate. kcat is 11.3 min(-1) with trans-2-hexenal as
CC substrate. kcat is 5.2 min(-1) with 4-hydroxy-2-nonenal as substrate.
CC kcat is 4.8 min(-1) with farnesal as substrate. kcat is 1.7 min(-1)
CC with 2,3-butanedione as substrate. kcat is 5.4 min(-1) with all-
CC trans-retinaldehyde as substrate. kcat is 3.8 min(-1) with 9-cis-
CC retinal as substrate (PubMed:26222439). {ECO:0000269|PubMed:25577493,
CC ECO:0000269|PubMed:26222439};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26222439}.
CC -!- INTERACTION:
CC C9JRZ8-2; Q12933: TRAF2; NbExp=3; IntAct=EBI-17190479, EBI-355744;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000269|PubMed:25577493}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:25577493}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=AKR1B15.1 {ECO:0000303|PubMed:25577493};
CC IsoId=C9JRZ8-1; Sequence=Displayed;
CC Name=2; Synonyms=AKR1B15.2 {ECO:0000303|PubMed:25577493};
CC IsoId=C9JRZ8-2; Sequence=VSP_041606;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at highest levels in
CC steroid-sensitive tissues, such as placenta, testis and adipose tissue.
CC {ECO:0000269|PubMed:25577493}.
CC -!- MISCELLANEOUS: Has no counterpart in murine species. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AC078847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471070; EAW83819.1; -; Genomic_DNA.
DR CCDS; CCDS47715.2; -. [C9JRZ8-2]
DR RefSeq; NP_001074007.2; NM_001080538.2. [C9JRZ8-2]
DR RefSeq; XP_011514543.2; XM_011516241.2.
DR RefSeq; XP_016867713.1; XM_017012224.1. [C9JRZ8-2]
DR AlphaFoldDB; C9JRZ8; -.
DR SMR; C9JRZ8; -.
DR BioGRID; 137330; 13.
DR IntAct; C9JRZ8; 3.
DR STRING; 9606.ENSP00000389289; -.
DR DrugBank; DB06077; Lumateperone.
DR SwissLipids; SLP:000001307; -. [C9JRZ8-1]
DR iPTMnet; C9JRZ8; -.
DR PhosphoSitePlus; C9JRZ8; -.
DR BioMuta; AKR1B15; -.
DR EPD; C9JRZ8; -.
DR jPOST; C9JRZ8; -.
DR MassIVE; C9JRZ8; -.
DR MaxQB; C9JRZ8; -.
DR PaxDb; C9JRZ8; -.
DR PeptideAtlas; C9JRZ8; -.
DR PRIDE; C9JRZ8; -.
DR ProteomicsDB; 11424; -. [C9JRZ8-1]
DR ProteomicsDB; 11425; -. [C9JRZ8-2]
DR Antibodypedia; 67875; 6 antibodies from 5 providers.
DR DNASU; 441282; -.
DR Ensembl; ENST00000423958.2; ENSP00000397009.2; ENSG00000227471.9. [C9JRZ8-2]
DR Ensembl; ENST00000457545.7; ENSP00000389289.1; ENSG00000227471.9. [C9JRZ8-2]
DR Ensembl; ENST00000652743.1; ENSP00000498877.1; ENSG00000227471.9. [C9JRZ8-1]
DR GeneID; 441282; -.
DR KEGG; hsa:441282; -.
DR MANE-Select; ENST00000457545.7; ENSP00000389289.1; NM_001080538.3; NP_001074007.2. [C9JRZ8-2]
DR UCSC; uc011kpr.3; human. [C9JRZ8-1]
DR CTD; 441282; -.
DR DisGeNET; 441282; -.
DR GeneCards; AKR1B15; -.
DR HGNC; HGNC:37281; AKR1B15.
DR HPA; ENSG00000227471; Tissue enriched (breast).
DR MIM; 616336; gene.
DR neXtProt; NX_C9JRZ8; -.
DR OpenTargets; ENSG00000227471; -.
DR PharmGKB; PA165617622; -.
DR VEuPathDB; HostDB:ENSG00000227471; -.
DR eggNOG; KOG1577; Eukaryota.
DR GeneTree; ENSGT00940000164182; -.
DR HOGENOM; CLU_023205_0_0_1; -.
DR InParanoid; C9JRZ8; -.
DR OMA; PWCMRQE; -.
DR OrthoDB; 1016440at2759; -.
DR TreeFam; TF106492; -.
DR BRENDA; 1.1.1.36; 2681.
DR BRENDA; 1.1.1.62; 2681.
DR PathwayCommons; C9JRZ8; -.
DR Reactome; R-HSA-193144; Estrogen biosynthesis.
DR SignaLink; C9JRZ8; -.
DR BioGRID-ORCS; 441282; 213 hits in 997 CRISPR screens.
DR GenomeRNAi; 441282; -.
DR Pharos; C9JRZ8; Tbio.
DR PRO; PR:C9JRZ8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; C9JRZ8; protein.
DR Bgee; ENSG00000227471; Expressed in duodenum and 72 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0047655; F:allyl-alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0047886; F:farnesol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0047045; F:testosterone 17-beta-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006703; P:estrogen biosynthetic process; TAS:Reactome.
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; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Lipid metabolism;
KW Mitochondrion; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..316
FT /note="Aldo-keto reductase family 1 member B15"
FT /id="PRO_0000395341"
FT ACT_SITE 49
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 20..22
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 160..161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 184
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 210..217
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT BINDING 261..273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT SITE 78
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:P14550"
FT MOD_RES 125
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60218"
FT VAR_SEQ 1..22
FT /note="MATFVELSTKAKMPIVGLGTWR -> MVLQMEPQVNSTNNFHQGPLDQPVGP
FT LTGLKSSLLKDTTSAGPLLRPYPA (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:21276782,
FT ECO:0000269|PubMed:25577493"
FT /id="VSP_041606"
SQ SEQUENCE 316 AA; 36537 MW; 5FB6CBFA7190C740 CRC64;
MATFVELSTK AKMPIVGLGT WRSLLGKVKE AVKVAIDAEY RHIDCAYFYE NQHEVGEAIQ
EKIQEKAVMR EDLFIVSKVW PTFFERPLVR KAFEKTLKDL KLSYLDVYLI HWPQGFKTGD
DFFPKDDKGN MISGKGTFLD AWEAMEELVD EGLVKALGVS NFNHFQIERL LNKPGLKYKP
VTNQVECHPY LTQEKLIQYC HSKGITVTAY SPLGSPDRPW AKPEDPSLLE DPKIKEIAAK
HKKTTAQVLI RFHIQRNVTV IPKSMTPAHI VENIQVFDFK LSDEEMATIL SFNRNWRAFD
FKEFSHLEDF PFDAEY
