ID ALDR_HUMAN Reviewed; 316 AA. AC P15121; B2R8N3; Q5U031; Q6FGA4; Q6ICP2; Q9BS21; Q9UCI9; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 245. DE RecName: Full=Aldo-keto reductase family 1 member B1; DE EC=1.1.1.300 {ECO:0000269|PubMed:12732097}; DE EC=1.1.1.372 {ECO:0000269|PubMed:10510318, ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:8245005}; DE EC=1.1.1.54 {ECO:0000269|PubMed:10510318, ECO:0000269|PubMed:21329684}; DE AltName: Full=Aldehyde reductase; DE AltName: Full=Aldose reductase; DE Short=AR; DE EC=1.1.1.21 {ECO:0000269|PubMed:8245005}; GN Name=AKR1B1; Synonyms=ALDR1, ALR2 {ECO:0000303|PubMed:17368668}; 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], AND PARTIAL PROTEIN SEQUENCE. RX PubMed=2498333; DOI=10.1016/s0021-9258(18)60566-6; RA Bohren K.M., Bullock B., Wermuth B., Gabbay K.H.; RT "The aldo-keto reductase superfamily. cDNAs and deduced amino acid RT sequences of human aldehyde and aldose reductases."; RL J. Biol. Chem. 264:9547-9551(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX PubMed=2504709; DOI=10.1016/s0021-9258(18)63766-4; RA Chung S., Lamendola J.; RT "Cloning and sequence determination of human placental aldose reductase RT gene."; RL J. Biol. Chem. 264:14775-14777(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fetus; RX PubMed=2510130; DOI=10.1093/nar/17.20.8368; RA Graham A., Hedge P.J., Powell S.J., Riley J., Brown L., Gammack A., RA Carey F., Markham A.F.; RT "Nucleotide sequence of cDNA for human aldose reductase."; RL Nucleic Acids Res. 17:8368-8368(1989). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC TISSUE=Placenta; RX PubMed=2111143; DOI=10.1089/dna.1990.9.149; RA Grundmann U., Bohn H., Obermeier R., Amann E.; RT "Cloning and prokaryotic expression of a biologically active human RT placental aldose reductase."; RL DNA Cell Biol. 9:149-157(1990). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2112546; DOI=10.1016/s0021-9258(19)38740-x; RA Nishimura C., Matsuura Y., Kokai Y., Akera T., Carper D., Morjana N., RA Lyons C., Flynn T.G.; RT "Cloning and expression of human aldose reductase."; RL J. Biol. Chem. 265:9788-9792(1990). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1901857; DOI=10.1016/s0021-9258(20)89582-9; RA Graham A., Brown L., Hedge P.J., Gammack A.J., Markham A.F.; RT "Structure of the human aldose reductase gene."; RL J. Biol. Chem. 266:6872-6877(1991). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9195951; DOI=10.1074/jbc.272.26.16431; RA Ko B.C.B., Ruepp B., Bohren K.M., Gabbay K.H., Chung S.S.; RT "Identification and characterization of multiple osmotic response sequences RT in the human aldose reductase gene."; RL J. Biol. Chem. 272:16431-16437(1997). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lymphoma; RX PubMed=14996095; DOI=10.1111/j.1365-2133.2004.05651.x; RA Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.; RT "SEREX identification of new tumour-associated antigens in cutaneous T-cell RT lymphoma."; RL Br. J. Dermatol. 150:252-258(2004). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [13] 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 [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Eye, and Urinary bladder; 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 [15] RP PROTEIN SEQUENCE OF 131-162, AND TISSUE SPECIFICITY. RX PubMed=8435445; DOI=10.1016/0167-4889(93)90218-e; RA Ferraretto A., Negri A., Giuliani A., De Grada L., Fuhrman Conti A.M., RA Ronchi S.; RT "Aldose reductase is involved in long-term adaptation of EUE cells to RT hyperosmotic stress."; RL Biochim. Biophys. Acta 1175:283-288(1993). RN [16] RP PROTEIN SEQUENCE OF 244-275. RX PubMed=2492527; DOI=10.1016/s0021-9258(19)81699-x; RA Morjana N.A., Lyons C., Flynn T.G.; RT "Aldose reductase from human psoas muscle. Affinity labeling of an active RT site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'- RT adenosine."; RL J. Biol. Chem. 264:2912-2919(1989). RN [17] RP PROTEIN SEQUENCE OF 276-294, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Vishwanath V.; RL Submitted (MAR-2007) to UniProtKB. RN [18] RP PROTEIN SEQUENCE OF 298-316, AND ACTIVITY REGULATION. RX PubMed=8343525; DOI=10.1016/0167-4838(93)90258-s; RA Liu S.Q., Bhatnagar A., Ansari N.H., Srivastava S.K.; RT "Identification of the reactive cysteine residue in human placenta aldose RT reductase."; RL Biochim. Biophys. Acta 1164:268-272(1993). RN [19] RP PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT ALA-2. RC TISSUE=Muscle; RX PubMed=8281941; DOI=10.1111/j.1432-1033.1993.tb18445.x; RA Jaquinod M., Potier N., Klarskov K., Reymann J.-M., Sorokine O., RA Kieffer S., Barth P., Andriantomanga V., Biellmann J.-F., RA van Dorsselaer A.; RT "Sequence of pig lens aldose reductase and electrospray mass spectrometry RT of non-covalent and covalent complexes."; RL Eur. J. Biochem. 218:893-903(1993). RN [20] RP CATALYTIC ACTIVITY. RX PubMed=1936586; DOI=10.2337/diab.40.10.1233; RA Hamada Y., Kitoh R., Raskin P.; RT "Crucial role of aldose reductase activity and plasma glucose level in RT sorbitol accumulation in erythrocytes from diabetic patients."; RL Diabetes 40:1233-1240(1991). RN [21] RP MUTAGENESIS OF ASP-44; TYR-49; LYS-78 AND HIS-111, AND CATALYTIC ACTIVITY. RX PubMed=8245005; DOI=10.1016/s0021-9258(19)74444-5; RA Tarle I., Borhani D.W., Wilson D.K., Quiocho F.A., Petrash J.M.; RT "Probing the active site of human aldose reductase. Site-directed RT mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110."; RL J. Biol. Chem. 268:25687-25693(1993). RN [22] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY. RX PubMed=10510318; DOI=10.1042/bj3430487; RA O'Connor T., Ireland L.S., Harrison D.J., Hayes J.D.; RT "Major differences exist in the function and tissue-specific expression of RT human aflatoxin B1 aldehyde reductase and the principal human aldo-keto RT reductase AKR1 family members."; RL Biochem. J. 343:487-504(1999). RN [23] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, RP ACTIVITY REGULATION, AND FUNCTION. RX PubMed=12732097; DOI=10.1042/bj20021818; RA Crosas B., Hyndman D.J., Gallego O., Martras S., Pares X., Flynn T.G., RA Farres J.; RT "Human aldose reductase and human small intestine aldose reductase are RT efficient retinal reductases: consequences for retinoid metabolism."; RL Biochem. J. 373:973-979(2003). RN [24] 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 [25] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND SUBSTRATE RP SPECIFICITY. 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). RN [26] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, RP AND FUNCTION. RX PubMed=21329684; DOI=10.1016/j.cbi.2011.02.004; RA Shen Y., Zhong L., Johnson S., Cao D.; RT "Human aldo-keto reductases 1B1 and 1B10: a comparative study on their RT enzyme activity toward electrophilic carbonyl compounds."; RL Chem. Biol. Interact. 191:192-198(2011). RN [27] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, RP AND FUNCTION. RX PubMed=21329680; DOI=10.1016/j.cbi.2011.02.007; RA Ruiz F.X., Moro A., Gallego O., Ardevol A., Rovira C., Petrash J.M., RA Pares X., Farres J.; RT "Human and rodent aldo-keto reductases from the AKR1B subfamily and their RT specificity with retinaldehyde."; RL Chem. Biol. Interact. 191:199-205(2011). RN [28] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [29] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-95; LYS-222 AND LYS-263, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [30] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [31] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS). RX PubMed=1621098; DOI=10.1126/science.1621098; RA Wilson D.K., Bohren K.M., Gabbay K.H., Quiocho F.A.; RT "An unlikely sugar substrate site in the 1.65 A structure of the human RT aldose reductase holoenzyme implicated in diabetic complications."; RL Science 257:81-84(1992). RN [32] RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS). RX PubMed=1447221; DOI=10.2210/pdb1abn/pdb; RA Borhani D.W., Harter T.M., Pertrash J.M.; RT "The crystal structure of the aldose reductase.NADPH binary complex."; RL J. Biol. Chem. 267:24841-24847(1992). RN [33] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX PubMed=8234324; DOI=10.1073/pnas.90.21.9847; RA Wilson D.K., Tarle I., Petrash J.M., Quiocho F.A.; RT "Refined 1.8-A structure of human aldose reductase complexed with the RT potent inhibitor zopolrestat."; RL Proc. Natl. Acad. Sci. U.S.A. 90:9847-9851(1993). RN [34] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX PubMed=9405046; DOI=10.1021/bi9717136; RA Harrison D.H., Bohren K.M., Petsko G.A., Ringe D., Gabbay K.H.; RT "The alrestatin double-decker: binding of two inhibitor molecules to human RT aldose reductase reveals a new specificity determinant."; RL Biochemistry 36:16134-16140(1997). RN [35] RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC RP INHIBITOR, AND ACTIVE SITE. RX PubMed=15272156; DOI=10.1107/s0907444904011370; RA Ruiz F., Hazemann I., Mitschler A., Joachimiak A., Schneider T., RA Karplus M., Podjarny A.; RT "The crystallographic structure of the aldose reductase-IDD552 complex RT shows direct proton donation from tyrosine 48."; RL Acta Crystallogr. D 60:1347-1354(2004). RN [36] RP X-RAY CRYSTALLOGRAPHY (0.66 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC RP INHIBITOR. RX PubMed=15146478; DOI=10.1002/prot.20015; RA Howard E.I., Sanishvili R., Cachau R.E., Mitschler A., Chevrier B., RA Barth P., Lamour V., Van Zandt M., Sibley E., Bon C., Moras D., RA Schneider T.R., Joachimiak A., Podjarny A.; RT "Ultrahigh resolution drug design I: details of interactions in human RT aldose reductase-inhibitor complex at 0.66 A."; RL Proteins 55:792-804(2004). RN [37] RP X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE RP ANALOG. RX PubMed=16337231; DOI=10.1016/j.jmb.2005.10.067; RA Steuber H., Zentgraf M., Podjarny A., Heine A., Klebe G.; RT "High-resolution crystal structure of aldose reductase complexed with the RT novel sulfonyl-pyridazinone inhibitor exhibiting an alternative active site RT anchoring group."; RL J. Mol. Biol. 356:45-56(2006). RN [38] RP X-RAY CRYSTALLOGRAPHY (0.82 ANGSTROMS) IN COMPLEX WITH NADP. RX PubMed=17505104; DOI=10.1107/s0907444907011997; RA Biadene M., Hazemann I., Cousido A., Ginell S., Joachimiak A., RA Sheldrick G.M., Podjarny A., Schneider T.R.; RT "The atomic resolution structure of human aldose reductase reveals that RT rearrangement of a bound ligand allows the opening of the safety-belt RT loop."; RL Acta Crystallogr. D 63:665-672(2007). RN [39] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC RP INHIBITOR. RX PubMed=17418233; DOI=10.1016/j.jmb.2007.03.021; RA Steuber H., Zentgraf M., La Motta C., Sartini S., Heine A., Klebe G.; RT "Evidence for a novel binding site conformer of aldose reductase in ligand- RT bound state."; RL J. Mol. Biol. 369:186-197(2007). RN [40] RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC RP INHIBITOR. RX PubMed=17368668; DOI=10.1016/j.jmb.2006.12.004; RA Steuber H., Heine A., Klebe G.; RT "Structural and thermodynamic study on aldose reductase: nitro-substituted RT inhibitors with strong enthalpic binding contribution."; RL J. Mol. Biol. 368:618-638(2007). 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, monosacharides, bile acids and CC xenobiotics substrates. Key enzyme in the polyol pathway, catalyzes CC reduction of glucose to sorbitol during hyperglycemia (PubMed:1936586). CC Reduces steroids and their derivatives and prostaglandins. Displays low CC enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis- CC retinal (PubMed:12732097, PubMed:19010934, PubMed:8343525). Catalyzes CC the reduction of diverse phospholipid aldehydes such as 1-palmitoyl-2- CC (5-oxovaleroyl)-sn -glycero-3-phosphoethanolamin (POVPC) and related CC phospholipid aldehydes that are generated from the oxydation of CC phosphotidylcholine and phosphatdyleethanolamides (PubMed:17381426). CC Plays a role in detoxifying dietary and lipid-derived unsaturated CC carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, CC trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS- CC carbonyls) (PubMed:21329684). {ECO:0000269|PubMed:12732097, CC ECO:0000269|PubMed:17381426, ECO:0000269|PubMed:19010934, CC ECO:0000269|PubMed:1936586, ECO:0000269|PubMed:21329684, CC ECO:0000269|PubMed:8343525}. 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:8245005}; 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:12732097, CC ECO:0000269|PubMed:21329680}; 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:12732097, ECO:0000269|PubMed:21329680}; 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:0000269|PubMed:12732097}; 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:0000269|PubMed:10510318, CC ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:1936586, CC ECO:0000269|PubMed:21329680, ECO:0000269|PubMed:8245005}; 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:0000269|PubMed:10510318, CC ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:1936586, CC ECO:0000269|PubMed:21329680, ECO:0000269|PubMed:8245005}; 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:0000269|PubMed:21329684}; 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:21329684}; 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:0000269|PubMed:21329684}; 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:0000269|PubMed:21329684}; 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:0000269|PubMed:10510318, ECO:0000269|PubMed:21329684}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NADP(+) + pyridine 3-methanol = H(+) + NADPH + pyridine-3- CC carbaldehyde; Xref=Rhea:RHEA:58776, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28345, ChEBI:CHEBI:45213, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:12732097}; 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 -!- ACTIVITY REGULATION: Cys-299 may regulate the kinetic and inhibition CC properties of the enzyme, but does not participate in catalysis CC (PubMed:8343525). Tolrestat inhibits retinal reduction CC (PubMed:12732097). {ECO:0000269|PubMed:12732097, CC ECO:0000269|PubMed:8343525}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=44 uM for D,L-glyceraldehyde {ECO:0000269|PubMed:12732097}; CC KM=76000 uM for glucose {ECO:0000269|PubMed:12732097}; CC KM=14 uM for pyridine-3-carbaldehyde {ECO:0000269|PubMed:12732097}; CC KM=10 uM for all-trans-retinal {ECO:0000269|PubMed:12732097}; CC KM=12 uM for 9-cis-retinal {ECO:0000269|PubMed:12732097}; CC KM=14 uM for 13-cis-retinal {ECO:0000269|PubMed:12732097}; CC KM=8.8 uM for CC 1-O-palmitoyl-2-O-(5-oxovaleryl)-sn-glycero-3-phosphocholine (POVPC) CC {ECO:0000269|PubMed:17381426}; CC KM=16 uM for CC 1-hexadecanoyl-2-(7-oxoheptanoyl)-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:17381426}; CC KM=13 uM for CC 1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:17381426}; CC KM=11 uM for CC 1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphoethanolamine CC {ECO:0000269|PubMed:17381426}; CC KM=884 uM for acrolein {ECO:0000269|PubMed:21329684}; CC KM=9643 uM for 3-methyl-2-butenal {ECO:0000269|PubMed:21329684}; CC KM=878 uM for (E)-2-hexenal {ECO:0000269|PubMed:21329684}; CC KM=905 uM for (E,E)-2,4-hexadienal {ECO:0000269|PubMed:21329684}; CC KM=716 uM for 4-hydroxynonenal {ECO:0000269|PubMed:21329684}; CC KM=122 uM for GS-(E)-4-hexenal {ECO:0000269|PubMed:21329684}; CC KM=7 uM for GS-hexenal {ECO:0000269|PubMed:21329684}; CC KM=5 uM for GS-4-hydroxynonenal {ECO:0000269|PubMed:21329684}; CC KM=1.9 uM for prostaglandin H2 {ECO:0000269|PubMed:19010934}; CC Vmax=26 nmol/min/mg enzyme for prostaglandin H2 CC {ECO:0000269|PubMed:19010934}; CC Note=kcat is 15 min(-1) for all-trans-retinal as substrate. kcat is CC 30 min(-1) for 9-cis-retinal as substrate. kcat is 94 min(-1) for CC 13-cis-retinal as substrate (PubMed:12732097). kcat is 11 min(-1) for CC acrolein as substrate. kcat is 31 min(-1) for 3-methyl-2-butenal as CC substrate. kcat is 41 min(-1) for (E)-2-hexenal as substrate. kcat is CC 43 min(-1) for (E,E)-2,4-hexadienal as substrate. kcat is 50 min(-1) CC for 4-hydroxynonenal as substrate. kcat is 16 min(-1) for CC GS-(E)-4-hexenal as substrate. kcat is 16 min(-1) for GS-hexenal as CC substrate. kcat is 13 min(-1) for GS-4-hydroxynonenal as substrate CC (PubMed:21329684). kcat is 31 min(-1) for D,L-glyceraldehyde CC (PubMed:21329680). {ECO:0000269|PubMed:12732097, CC ECO:0000269|PubMed:21329680, ECO:0000269|PubMed:21329684}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15146478, CC ECO:0000269|PubMed:15272156, ECO:0000269|PubMed:16337231, CC ECO:0000269|PubMed:17368668, ECO:0000269|PubMed:17418233, CC ECO:0000269|PubMed:17505104}. CC -!- INTERACTION: CC P15121; Q9BUY7: EFCAB11; NbExp=3; IntAct=EBI-1052491, EBI-18688654; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Highly expressed in embryonic epithelial cells CC (EUE) in response to osmotic stress. {ECO:0000269|PubMed:8435445}. 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; J04795; AAA51713.1; -; mRNA. DR EMBL; J05017; AAA51714.1; -; mRNA. DR EMBL; X15414; CAA33460.1; -; mRNA. DR EMBL; M34720; AAA35560.1; -; mRNA. DR EMBL; M34721; AAA35561.1; -; Genomic_DNA. DR EMBL; J05474; AAA51715.1; -; mRNA. DR EMBL; M59783; AAA51712.1; -; Genomic_DNA. DR EMBL; M59856; AAA51712.1; JOINED; Genomic_DNA. DR EMBL; AF032455; AAB88851.1; -; Genomic_DNA. DR EMBL; AF328729; AAN09721.1; -; mRNA. DR EMBL; AK313439; BAG36230.1; -; mRNA. DR EMBL; CR450351; CAG29347.1; -; mRNA. DR EMBL; CR542203; CAG47000.1; -; mRNA. DR EMBL; BT019859; AAV38662.1; -; mRNA. DR EMBL; CH236950; EAL24070.1; -; Genomic_DNA. DR EMBL; CH471070; EAW83814.1; -; Genomic_DNA. DR EMBL; BC000260; AAH00260.1; -; mRNA. DR EMBL; BC005387; AAH05387.1; -; mRNA. DR EMBL; BC010391; AAH10391.1; -; mRNA. DR CCDS; CCDS5831.1; -. DR PIR; A39763; A39763. DR RefSeq; NP_001619.1; NM_001628.3. DR PDB; 1ABN; X-ray; 2.40 A; A=2-316. DR PDB; 1ADS; X-ray; 1.65 A; A=2-316. DR PDB; 1AZ1; X-ray; 1.80 A; A=2-316. DR PDB; 1AZ2; X-ray; 2.90 A; A=2-316. DR PDB; 1EF3; X-ray; 2.80 A; A/B=2-316. DR PDB; 1EL3; X-ray; 1.70 A; A=1-316. DR PDB; 1IEI; X-ray; 2.50 A; A=1-316. DR PDB; 1MAR; X-ray; 1.80 A; A=2-316. DR PDB; 1PWL; X-ray; 1.10 A; A=1-316. DR PDB; 1PWM; X-ray; 0.92 A; A=1-316. DR PDB; 1T40; X-ray; 1.80 A; A=1-316. DR PDB; 1T41; X-ray; 1.05 A; A=1-316. DR PDB; 1US0; X-ray; 0.66 A; A=1-316. DR PDB; 1X96; X-ray; 1.40 A; A=1-316. DR PDB; 1X97; X-ray; 1.40 A; A=1-316. DR PDB; 1X98; X-ray; 1.30 A; A=1-316. DR PDB; 1XGD; X-ray; 2.10 A; A=2-316. DR PDB; 1Z3N; X-ray; 1.04 A; A=1-316. DR PDB; 1Z89; X-ray; 1.43 A; A=1-316. DR PDB; 1Z8A; X-ray; 0.95 A; A=1-316. DR PDB; 2ACQ; X-ray; 1.76 A; A=2-316. DR PDB; 2ACR; X-ray; 1.76 A; A=2-316. DR PDB; 2ACS; X-ray; 1.76 A; A=2-316. DR PDB; 2ACU; X-ray; 1.76 A; A=2-316. DR PDB; 2AGT; X-ray; 1.00 A; A=1-316. DR PDB; 2DUX; X-ray; 1.60 A; A=1-316. DR PDB; 2DUZ; X-ray; 1.60 A; A=1-316. DR PDB; 2DV0; X-ray; 1.62 A; A=1-316. DR PDB; 2F2K; X-ray; 1.94 A; A=1-316. DR PDB; 2FZ8; X-ray; 1.48 A; A=1-316. DR PDB; 2FZ9; X-ray; 1.60 A; A=1-316. DR PDB; 2FZB; X-ray; 1.50 A; A=6-316. DR PDB; 2FZD; X-ray; 1.08 A; A=6-316. DR PDB; 2HV5; X-ray; 1.59 A; A=1-316. DR PDB; 2HVN; X-ray; 1.58 A; A=1-316. DR PDB; 2HVO; X-ray; 1.65 A; A=1-316. DR PDB; 2I16; X-ray; 0.81 A; A=1-316. DR PDB; 2I17; X-ray; 0.81 A; A=1-316. DR PDB; 2IKG; X-ray; 1.43 A; A=1-316. DR PDB; 2IKH; X-ray; 1.55 A; A=1-316. DR PDB; 2IKI; X-ray; 1.47 A; A=1-316. DR PDB; 2IKJ; X-ray; 1.55 A; A=1-316. DR PDB; 2INE; X-ray; 1.90 A; A=2-316. DR PDB; 2INZ; X-ray; 1.95 A; A=2-316. DR PDB; 2IPW; X-ray; 2.00 A; A=2-316. DR PDB; 2IQ0; X-ray; 1.95 A; A=2-316. DR PDB; 2IQD; X-ray; 2.00 A; A=2-316. DR PDB; 2IS7; X-ray; 1.70 A; A=2-316. DR PDB; 2ISF; X-ray; 2.00 A; A=2-316. DR PDB; 2J8T; X-ray; 0.82 A; A=6-316. DR PDB; 2NVC; X-ray; 1.65 A; A=1-316. DR PDB; 2NVD; X-ray; 1.55 A; A=1-316. DR PDB; 2PD5; X-ray; 1.60 A; A=1-316. DR PDB; 2PD9; X-ray; 1.55 A; A=1-316. DR PDB; 2PDB; X-ray; 1.60 A; A=1-316. DR PDB; 2PDC; X-ray; 1.65 A; A=1-316. DR PDB; 2PDF; X-ray; 1.56 A; A=1-316. DR PDB; 2PDG; X-ray; 1.42 A; A=1-316. DR PDB; 2PDH; X-ray; 1.45 A; A=1-316. DR PDB; 2PDI; X-ray; 1.55 A; A=1-316. DR PDB; 2PDJ; X-ray; 1.57 A; A=1-316. DR PDB; 2PDK; X-ray; 1.55 A; A=1-316. DR PDB; 2PDL; X-ray; 1.47 A; A=1-316. DR PDB; 2PDM; X-ray; 1.75 A; A=1-316. DR PDB; 2PDN; X-ray; 1.70 A; A=1-316. DR PDB; 2PDP; X-ray; 1.65 A; A=1-316. DR PDB; 2PDQ; X-ray; 1.73 A; A=1-316. DR PDB; 2PDU; X-ray; 1.55 A; A=1-316. DR PDB; 2PDW; X-ray; 1.55 A; A=1-316. DR PDB; 2PDX; X-ray; 1.65 A; A=1-316. DR PDB; 2PDY; X-ray; 1.65 A; A=1-316. DR PDB; 2PEV; X-ray; 0.90 A; A=1-316. DR PDB; 2PF8; X-ray; 0.85 A; A=1-316. DR PDB; 2PFH; X-ray; 0.85 A; A=1-316. DR PDB; 2PZN; X-ray; 1.00 A; A=1-316. DR PDB; 2QXW; X-ray; 0.80 A; A=1-316. DR PDB; 2R24; X-ray; 1.75 A; A=1-316. DR PDB; 3BCJ; X-ray; 0.78 A; A=1-316. DR PDB; 3DN5; X-ray; 1.45 A; A=1-316. DR PDB; 3G5E; X-ray; 1.80 A; A=1-316. DR PDB; 3GHR; X-ray; 1.00 A; A=1-316. DR PDB; 3GHS; X-ray; 1.00 A; A=1-316. DR PDB; 3GHT; X-ray; 1.10 A; A=1-316. DR PDB; 3GHU; X-ray; 1.20 A; A=1-316. DR PDB; 3LBO; X-ray; 1.10 A; A=1-316. DR PDB; 3LD5; X-ray; 1.27 A; A=1-316. DR PDB; 3LEN; X-ray; 1.21 A; A=1-316. DR PDB; 3LEP; X-ray; 0.99 A; A=1-316. DR PDB; 3LQG; X-ray; 1.35 A; A=1-316. DR PDB; 3LQL; X-ray; 1.13 A; A=1-316. DR PDB; 3LZ3; X-ray; 1.03 A; A=1-316. DR PDB; 3LZ5; X-ray; 0.95 A; A=1-316. DR PDB; 3M0I; X-ray; 1.07 A; A=1-316. DR PDB; 3M4H; X-ray; 0.94 A; A=1-316. DR PDB; 3M64; X-ray; 1.30 A; A=1-316. DR PDB; 3MB9; X-ray; 1.65 A; A=1-316. DR PDB; 3MC5; X-ray; 1.14 A; A=1-316. DR PDB; 3ONB; X-ray; 1.45 A; A=2-316. DR PDB; 3ONC; X-ray; 1.06 A; A=2-316. DR PDB; 3P2V; X-ray; 1.69 A; A=1-316. DR PDB; 3Q65; X-ray; 2.09 A; A/B=1-316. DR PDB; 3Q67; X-ray; 1.55 A; A/B=1-316. DR PDB; 3RX2; X-ray; 1.90 A; A=1-316. DR PDB; 3RX3; X-ray; 1.90 A; A=1-316. DR PDB; 3RX4; X-ray; 2.00 A; A=1-316. DR PDB; 3S3G; X-ray; 1.80 A; A=1-316. DR PDB; 3T42; X-ray; 1.28 A; A=1-316. DR PDB; 3U2C; X-ray; 1.00 A; A=1-316. DR PDB; 3V35; X-ray; 1.90 A; A=1-316. DR PDB; 3V36; X-ray; 2.00 A; A=1-316. DR PDB; 4GCA; X-ray; 0.90 A; A=2-316. DR PDB; 4GQ0; X-ray; 2.10 A; A=1-316. DR PDB; 4IGS; X-ray; 0.85 A; A=1-316. DR PDB; 4JIR; X-ray; 2.00 A; A=1-316. DR PDB; 4LAU; X-ray; 0.84 A; A=1-316. DR PDB; 4LAZ; X-ray; 0.85 A; A=1-316. DR PDB; 4LB3; X-ray; 0.80 A; A=1-316. DR PDB; 4LB4; X-ray; 0.80 A; A=1-316. DR PDB; 4LBR; X-ray; 0.80 A; A=1-316. DR PDB; 4LBS; X-ray; 0.76 A; A=1-316. DR PDB; 4NKC; X-ray; 1.12 A; A=2-316. DR PDB; 4PR4; X-ray; 1.06 A; A=2-316. DR PDB; 4PRR; X-ray; 1.01 A; A=2-316. DR PDB; 4PRT; X-ray; 0.96 A; A=1-316. DR PDB; 4PUU; X-ray; 1.14 A; A=1-316. DR PDB; 4PUW; X-ray; 1.12 A; A=1-316. DR PDB; 4Q7B; X-ray; 1.19 A; A=2-316. DR PDB; 4QBX; X-ray; 0.98 A; A=1-316. DR PDB; 4QR6; X-ray; 1.05 A; A=1-316. DR PDB; 4QX4; X-ray; 1.26 A; A=1-316. DR PDB; 4QXI; X-ray; 0.87 A; A=1-316. DR PDB; 4RPQ; X-ray; 1.20 A; A=2-316. DR PDB; 4XZH; X-ray; 1.00 A; A/B=1-316. DR PDB; 4XZI; X-ray; 2.45 A; A=1-316. DR PDB; 4YS1; X-ray; 1.07 A; A=1-316. DR PDB; 4YU1; X-ray; 1.02 A; A=1-316. DR PDB; 5HA7; X-ray; 1.65 A; A/B=1-316. DR PDB; 5OU0; X-ray; 0.94 A; A=1-316. DR PDB; 5OUJ; X-ray; 0.96 A; A=1-316. DR PDB; 5OUK; X-ray; 0.96 A; A=1-316. DR PDB; 6F7R; X-ray; 0.92 A; A=1-316. DR PDB; 6F81; X-ray; 0.97 A; A=1-316. DR PDB; 6F82; X-ray; 1.03 A; A=1-316. DR PDB; 6F84; X-ray; 1.09 A; A=1-316. DR PDB; 6F8O; X-ray; 1.17 A; A=1-316. DR PDB; 6SYW; X-ray; 0.93 A; A=1-316. DR PDB; 6T27; X-ray; 1.11 A; A=1-316. DR PDB; 6T3P; X-ray; 0.97 A; A=1-316. DR PDB; 6T5G; X-ray; 1.28 A; A=1-316. DR PDB; 6T7Q; X-ray; 1.01 A; A=1-316. DR PDB; 6TD8; X-ray; 0.97 A; A=1-316. DR PDB; 6TUC; X-ray; 1.06 A; A=1-316. DR PDB; 6TUF; X-ray; 1.15 A; A=1-316. DR PDB; 6TXP; X-ray; 0.95 A; A=1-316. DR PDB; 6XUM; X-ray; 0.97 A; A=1-316. DR PDB; 6Y03; X-ray; 1.69 A; A=1-316. DR PDB; 6Y1P; X-ray; 0.94 A; A=1-316. DR PDB; 8A4N; X-ray; 0.93 A; A=1-316. DR PDB; 8AE9; X-ray; 0.95 A; A=1-316. DR PDB; 8AQG; X-ray; 0.95 A; A=1-313. DR PDB; 8AQP; X-ray; 0.96 A; A=1-316. DR PDB; 8AUU; X-ray; 0.95 A; A=1-316. DR PDB; 8B34; X-ray; 0.97 A; A=1-316. DR PDB; 8B3N; X-ray; 1.03 A; A=1-316. DR PDB; 8B3R; X-ray; 0.96 A; A=1-316. DR PDB; 8B66; X-ray; 0.95 A; A=1-316. DR PDB; 8BJL; X-ray; 0.97 A; A=1-316. DR PDBsum; 1ABN; -. DR PDBsum; 1ADS; -. DR PDBsum; 1AZ1; -. DR PDBsum; 1AZ2; -. DR PDBsum; 1EF3; -. DR PDBsum; 1EL3; -. DR PDBsum; 1IEI; -. DR PDBsum; 1MAR; -. DR PDBsum; 1PWL; -. DR PDBsum; 1PWM; -. DR PDBsum; 1T40; -. DR PDBsum; 1T41; -. DR PDBsum; 1US0; -. DR PDBsum; 1X96; -. DR PDBsum; 1X97; -. DR PDBsum; 1X98; -. DR PDBsum; 1XGD; -. DR PDBsum; 1Z3N; -. DR PDBsum; 1Z89; -. DR PDBsum; 1Z8A; -. DR PDBsum; 2ACQ; -. DR PDBsum; 2ACR; -. DR PDBsum; 2ACS; -. DR PDBsum; 2ACU; -. DR PDBsum; 2AGT; -. DR PDBsum; 2DUX; -. DR PDBsum; 2DUZ; -. DR PDBsum; 2DV0; -. DR PDBsum; 2F2K; -. DR PDBsum; 2FZ8; -. DR PDBsum; 2FZ9; -. DR PDBsum; 2FZB; -. DR PDBsum; 2FZD; -. DR PDBsum; 2HV5; -. DR PDBsum; 2HVN; -. DR PDBsum; 2HVO; -. DR PDBsum; 2I16; -. DR PDBsum; 2I17; -. DR PDBsum; 2IKG; -. DR PDBsum; 2IKH; -. DR PDBsum; 2IKI; -. DR PDBsum; 2IKJ; -. DR PDBsum; 2INE; -. DR PDBsum; 2INZ; -. DR PDBsum; 2IPW; -. DR PDBsum; 2IQ0; -. DR PDBsum; 2IQD; -. DR PDBsum; 2IS7; -. DR PDBsum; 2ISF; -. DR PDBsum; 2J8T; -. DR PDBsum; 2NVC; -. DR PDBsum; 2NVD; -. DR PDBsum; 2PD5; -. DR PDBsum; 2PD9; -. DR PDBsum; 2PDB; -. DR PDBsum; 2PDC; -. DR PDBsum; 2PDF; -. DR PDBsum; 2PDG; -. DR PDBsum; 2PDH; -. DR PDBsum; 2PDI; -. DR PDBsum; 2PDJ; -. DR PDBsum; 2PDK; -. DR PDBsum; 2PDL; -. DR PDBsum; 2PDM; -. DR PDBsum; 2PDN; -. DR PDBsum; 2PDP; -. DR PDBsum; 2PDQ; -. DR PDBsum; 2PDU; -. DR PDBsum; 2PDW; -. DR PDBsum; 2PDX; -. DR PDBsum; 2PDY; -. DR PDBsum; 2PEV; -. DR PDBsum; 2PF8; -. DR PDBsum; 2PFH; -. DR PDBsum; 2PZN; -. DR PDBsum; 2QXW; -. DR PDBsum; 2R24; -. DR PDBsum; 3BCJ; -. DR PDBsum; 3DN5; -. DR PDBsum; 3G5E; -. DR PDBsum; 3GHR; -. DR PDBsum; 3GHS; -. DR PDBsum; 3GHT; -. DR PDBsum; 3GHU; -. DR PDBsum; 3LBO; -. DR PDBsum; 3LD5; -. DR PDBsum; 3LEN; -. DR PDBsum; 3LEP; -. DR PDBsum; 3LQG; -. DR PDBsum; 3LQL; -. DR PDBsum; 3LZ3; -. DR PDBsum; 3LZ5; -. DR PDBsum; 3M0I; -. DR PDBsum; 3M4H; -. DR PDBsum; 3M64; -. DR PDBsum; 3MB9; -. DR PDBsum; 3MC5; -. DR PDBsum; 3ONB; -. DR PDBsum; 3ONC; -. DR PDBsum; 3P2V; -. DR PDBsum; 3Q65; -. DR PDBsum; 3Q67; -. DR PDBsum; 3RX2; -. DR PDBsum; 3RX3; -. DR PDBsum; 3RX4; -. DR PDBsum; 3S3G; -. DR PDBsum; 3T42; -. DR PDBsum; 3U2C; -. DR PDBsum; 3V35; -. DR PDBsum; 3V36; -. DR PDBsum; 4GCA; -. DR PDBsum; 4GQ0; -. DR PDBsum; 4IGS; -. DR PDBsum; 4JIR; -. DR PDBsum; 4LAU; -. DR PDBsum; 4LAZ; -. DR PDBsum; 4LB3; -. DR PDBsum; 4LB4; -. DR PDBsum; 4LBR; -. DR PDBsum; 4LBS; -. DR PDBsum; 4NKC; -. DR PDBsum; 4PR4; -. DR PDBsum; 4PRR; -. DR PDBsum; 4PRT; -. DR PDBsum; 4PUU; -. DR PDBsum; 4PUW; -. DR PDBsum; 4Q7B; -. DR PDBsum; 4QBX; -. DR PDBsum; 4QR6; -. DR PDBsum; 4QX4; -. DR PDBsum; 4QXI; -. DR PDBsum; 4RPQ; -. DR PDBsum; 4XZH; -. DR PDBsum; 4XZI; -. DR PDBsum; 4YS1; -. DR PDBsum; 4YU1; -. DR PDBsum; 5HA7; -. DR PDBsum; 5OU0; -. DR PDBsum; 5OUJ; -. DR PDBsum; 5OUK; -. DR PDBsum; 6F7R; -. DR PDBsum; 6F81; -. DR PDBsum; 6F82; -. DR PDBsum; 6F84; -. DR PDBsum; 6F8O; -. DR PDBsum; 6SYW; -. DR PDBsum; 6T27; -. DR PDBsum; 6T3P; -. DR PDBsum; 6T5G; -. DR PDBsum; 6T7Q; -. DR PDBsum; 6TD8; -. DR PDBsum; 6TUC; -. DR PDBsum; 6TUF; -. DR PDBsum; 6TXP; -. DR PDBsum; 6XUM; -. DR PDBsum; 6Y03; -. DR PDBsum; 6Y1P; -. DR PDBsum; 8A4N; -. DR PDBsum; 8AE9; -. DR PDBsum; 8AQG; -. DR PDBsum; 8AQP; -. DR PDBsum; 8AUU; -. DR PDBsum; 8B34; -. DR PDBsum; 8B3N; -. DR PDBsum; 8B3R; -. DR PDBsum; 8B66; -. DR PDBsum; 8BJL; -. DR AlphaFoldDB; P15121; -. DR SASBDB; P15121; -. DR SMR; P15121; -. DR BioGRID; 106732; 76. DR IntAct; P15121; 14. DR MINT; P15121; -. DR STRING; 9606.ENSP00000285930; -. DR BindingDB; P15121; -. DR ChEMBL; CHEMBL1900; -. DR DrugBank; DB07028; (2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC ACID. DR DrugBank; DB07030; (5-CHLORO-2-{[(3-NITROBENZYL)AMINO]CARBONYL}PHENOXY)ACETIC ACID. DR DrugBank; DB07450; (R)-minalrestat. DR DrugBank; DB02101; (S,R)-fidarestat. DR DrugBank; DB08449; 2-(3-((4,5,7-trifluorobenzo[d]thiazol-2-yl)methyl)-1H-pyrrolo[2,3-b]pyridin-1-yl)acetic acid. DR DrugBank; DB08000; 2-(CARBOXYMETHYL)-1-OXO-1,2-DIHYDRONAPHTHO[1,2-D]ISOTHIAZOLE-4-CARBOXYLIC ACID 3,3-DIOXIDE. DR DrugBank; DB07139; 3-[5-(3-nitrophenyl)thiophen-2-yl]propanoic acid. DR DrugBank; DB07498; 4-[3-(3-NITROPHENYL)-1,2,4-OXADIAZOL-5-YL]BUTANOIC ACID. DR DrugBank; DB02007; alpha-D-glucose 6-phosphate. DR DrugBank; DB02020; Alrestatin. DR DrugBank; DB11859; Brexanolone. DR DrugBank; DB02994; Cacodylic acid. DR DrugBank; DB04272; Citric acid. DR DrugBank; DB07187; CP-744809. DR DrugBank; DB00694; Daunorubicin. DR DrugBank; DB06246; Exisulind. DR DrugBank; DB01039; Fenofibrate. DR DrugBank; DB02021; Fidarestat. DR DrugBank; DB16707; Gavorestat. DR DrugBank; DB00143; Glutathione. DR DrugBank; DB02834; IDD552. DR DrugBank; DB08084; IDD594. DR DrugBank; DB01689; Inhibitor Idd 384. DR DrugBank; DB07063; Lidorestat. DR DrugBank; DB06077; Lumateperone. DR DrugBank; DB02518; N-Acetylalanine. DR DrugBank; DB00157; NADH. DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate. DR DrugBank; DB05383; Pimagedine. DR DrugBank; DB05533; QR-333. DR DrugBank; DB05327; Ranirestat. DR DrugBank; DB02712; Sorbinil. DR DrugBank; DB00605; Sulindac. DR DrugBank; DB02383; Tolrestat. DR DrugBank; DB02132; Zenarestat. DR DrugBank; DB08772; Zopolrestat. DR DrugBank; DB07093; {3-[(5-CHLORO-1,3-BENZOTHIAZOL-2-YL)METHYL]-2,4-DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-YL}ACETIC ACID. DR DrugBank; DB07999; {4-[(CARBOXYMETHOXY)CARBONYL]-3,3-DIOXIDO-1-OXONAPHTHO[1,2-D]ISOTHIAZOL-2(1H)-YL}ACETIC ACID. DR DrugBank; DB08098; {[5-(5-nitro-2-furyl)-1,3,4-oxadiazol-2-yl]thio}acetic acid. DR DrugCentral; P15121; -. DR GuidetoPHARMACOLOGY; 2768; -. DR SwissLipids; SLP:000001112; -. DR GlyGen; P15121; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P15121; -. DR PhosphoSitePlus; P15121; -. DR SwissPalm; P15121; -. DR BioMuta; AKR1B1; -. DR DMDM; 113596; -. DR DOSAC-COBS-2DPAGE; P15121; -. DR REPRODUCTION-2DPAGE; IPI00413641; -. DR REPRODUCTION-2DPAGE; P15121; -. DR EPD; P15121; -. DR jPOST; P15121; -. DR MassIVE; P15121; -. DR MaxQB; P15121; -. DR PaxDb; 9606-ENSP00000285930; -. DR PeptideAtlas; P15121; -. DR ProteomicsDB; 53108; -. DR Pumba; P15121; -. DR TopDownProteomics; P15121; -. DR Antibodypedia; 4365; 667 antibodies from 42 providers. DR CPTC; P15121; 3 antibodies. DR DNASU; 231; -. DR Ensembl; ENST00000285930.9; ENSP00000285930.3; ENSG00000085662.14. DR GeneID; 231; -. DR KEGG; hsa:231; -. DR MANE-Select; ENST00000285930.9; ENSP00000285930.3; NM_001628.4; NP_001619.1. DR UCSC; uc003vrp.2; human. DR AGR; HGNC:381; -. DR CTD; 231; -. DR DisGeNET; 231; -. DR GeneCards; AKR1B1; -. DR HGNC; HGNC:381; AKR1B1. DR HPA; ENSG00000085662; Tissue enriched (adrenal). DR MIM; 103880; gene. DR neXtProt; NX_P15121; -. DR OpenTargets; ENSG00000085662; -. DR PharmGKB; PA24675; -. DR VEuPathDB; HostDB:ENSG00000085662; -. DR eggNOG; KOG1577; Eukaryota. DR GeneTree; ENSGT00940000153272; -. DR HOGENOM; CLU_023205_0_0_1; -. DR InParanoid; P15121; -. DR OMA; EIYLRWC; -. DR OrthoDB; 890110at2759; -. DR PhylomeDB; P15121; -. DR TreeFam; TF106492; -. DR BioCyc; MetaCyc:HS01502-MONOMER; -. DR BRENDA; 1.1.1.188; 2681. DR BRENDA; 1.1.1.21; 2681. DR PathwayCommons; P15121; -. DR Reactome; R-HSA-196108; Pregnenolone biosynthesis. DR Reactome; R-HSA-5652227; Fructose biosynthesis. DR SABIO-RK; P15121; -. DR SignaLink; P15121; -. DR BioGRID-ORCS; 231; 19 hits in 1179 CRISPR screens. DR ChiTaRS; AKR1B1; human. DR EvolutionaryTrace; P15121; -. DR GeneWiki; AKR1B1; -. DR GenomeRNAi; 231; -. DR Pharos; P15121; Tclin. DR PRO; PR:P15121; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P15121; Protein. DR Bgee; ENSG00000085662; Expressed in right adrenal gland cortex and 211 other cell types or tissues. DR ExpressionAtlas; P15121; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:UniProtKB. DR GO; GO:0047655; F:allyl-alcohol dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB. DR GO; GO:0043795; F:glyceraldehyde oxidoreductase activity; IDA:UniProtKB. DR GO; GO:0047956; F:glycerol dehydrogenase [NADP+] activity; IEA:RHEA. DR GO; GO:0047939; F:L-glucuronate reductase activity; IEA:Ensembl. 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; IDA:UniProtKB. DR GO; GO:0006700; P:C21-steroid hormone biosynthetic process; TAS:Reactome. DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc. DR GO; GO:0071475; P:cellular hyperosmotic salinity response; IDA:UniProtKB. DR GO; GO:0044597; P:daunorubicin metabolic process; IMP:UniProtKB. DR GO; GO:0044598; P:doxorubicin metabolic process; IMP:UniProtKB. DR GO; GO:0002070; P:epithelial cell maturation; IEA:Ensembl. DR GO; GO:0046370; P:fructose biosynthetic process; TAS:Reactome. DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:Ensembl. DR GO; GO:0072205; P:metanephric collecting duct development; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0035809; P:regulation of urine volume; IEA:Ensembl. DR GO; GO:0003091; P:renal water homeostasis; IEA:Ensembl. DR GO; GO:0001523; P:retinoid metabolic process; IMP:UniProtKB. DR CDD; cd19107; AKR_AKR1B1-19; 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; IPR023210; NADP_OxRdtase_dom. DR InterPro; IPR036812; NADP_OxRdtase_dom_sf. DR PANTHER; PTHR11732:SF294; ALDO-KETO REDUCTASE FAMILY 1 MEMBER B1; 1. 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. DR UCD-2DPAGE; P15121; -. DR Genevisible; P15121; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Lipid metabolism; NADP; Oxidoreductase; Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8281941, FT ECO:0007744|PubMed:19413330" FT CHAIN 2..316 FT /note="Aldo-keto reductase family 1 member B1" FT /id="PRO_0000124623" FT ACT_SITE 49 FT /note="Proton donor" FT /evidence="ECO:0000269|PubMed:15272156" FT BINDING 10..19 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000255" FT BINDING 111 FT /ligand="substrate" FT BINDING 211..273 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15146478, FT ECO:0000269|PubMed:15272156, ECO:0000269|PubMed:16337231, FT ECO:0000269|PubMed:17368668, ECO:0000269|PubMed:17418233, FT ECO:0000269|PubMed:17505104" FT SITE 78 FT /note="Lowers pKa of active site Tyr" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:8281941, FT ECO:0007744|PubMed:19413330" FT MOD_RES 3 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07943" FT MOD_RES 95 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 222 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 263 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VARIANT 15 FT /note="I -> F (in dbSNP:rs5054)" FT /id="VAR_014743" FT VARIANT 42 FT /note="H -> L (in dbSNP:rs5056)" FT /id="VAR_014744" FT VARIANT 73 FT /note="L -> V (in dbSNP:rs5057)" FT /id="VAR_014745" FT VARIANT 90 FT /note="K -> E (in dbSNP:rs2229542)" FT /id="VAR_048213" FT VARIANT 204 FT /note="G -> S (in dbSNP:rs5061)" FT /id="VAR_014746" FT VARIANT 288 FT /note="T -> I (in dbSNP:rs5062)" FT /id="VAR_014747" FT MUTAGEN 44 FT /note="D->N: Reduced glyceraldehyde oxidoreductase FT activity." FT /evidence="ECO:0000269|PubMed:8245005" FT MUTAGEN 49 FT /note="Y->F: Complete loss of glyceraldehyde oxidoreductase FT activity." FT /evidence="ECO:0000269|PubMed:8245005" FT MUTAGEN 78 FT /note="K->M: Reduced glyceraldehyde oxidoreductase FT activity." FT /evidence="ECO:0000269|PubMed:8245005" FT MUTAGEN 111 FT /note="H->N: Reduced glyceraldehyde oxidoreductase FT activity." FT /evidence="ECO:0000269|PubMed:8245005" FT CONFLICT 5 FT /note="L -> I (in Ref. 2; AAA51714)" FT /evidence="ECO:0000305" FT CONFLICT 114 FT /note="T -> I (in Ref. 10; CAG47000)" FT /evidence="ECO:0000305" FT CONFLICT 117 FT /note="K -> R (in Ref. 10; CAG29347)" FT /evidence="ECO:0000305" FT CONFLICT 142 FT /note="W -> R (in Ref. 14; AAH05387)" FT /evidence="ECO:0000305" FT CONFLICT 172 FT /note="N -> S (in Ref. 10; CAG29347)" FT /evidence="ECO:0000305" FT CONFLICT 270..272 FT /note="IAE -> EAA (in Ref. 16; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 307 FT /note="H -> M (in Ref. 18; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 3..6 FT /evidence="ECO:0007829|PDB:1US0" FT STRAND 12..16 FT /evidence="ECO:0007829|PDB:1US0" FT HELIX 25..38 FT /evidence="ECO:0007829|PDB:1US0" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:1US0" FT HELIX 47..49 FT /evidence="ECO:0007829|PDB:1US0" FT HELIX 52..64 FT /evidence="ECO:0007829|PDB:1US0" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:1US0" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:1US0" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:1US0" FT TURN 86..88 FT /evidence="ECO:0007829|PDB:1US0" FT HELIX 89..100 FT /evidence="ECO:0007829|PDB:1US0" FT STRAND 105..113 FT /evidence="ECO:0007829|PDB:1US0" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:2PDC" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:3U2C" FT HELIX 138..150 FT /evidence="ECO:0007829|PDB:1US0" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:1US0" FT STRAND 157..161 FT /evidence="ECO:0007829|PDB:1US0" FT HELIX 164..171 FT /evidence="ECO:0007829|PDB:1US0" FT STRAND 181..186 FT /evidence="ECO:0007829|PDB:1US0" FT HELIX 194..202 FT /evidence="ECO:0007829|PDB:1US0" FT STRAND 206..211 FT /evidence="ECO:0007829|PDB:1US0" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:2ACQ" FT TURN 228..230 FT /evidence="ECO:0007829|PDB:1US0" FT HELIX 232..241 FT /evidence="ECO:0007829|PDB:1US0" FT HELIX 245..255 FT /evidence="ECO:0007829|PDB:1US0" FT STRAND 259..261 FT /evidence="ECO:0007829|PDB:1XGD" FT HELIX 267..274 FT /evidence="ECO:0007829|PDB:1US0" FT HELIX 283..290 FT /evidence="ECO:0007829|PDB:1US0" FT HELIX 302..304 FT /evidence="ECO:0007829|PDB:1US0" FT STRAND 307..309 FT /evidence="ECO:0007829|PDB:1IEI" FT STRAND 311..314 FT /evidence="ECO:0007829|PDB:3U2C" SQ SEQUENCE 316 AA; 35853 MW; 1852E8616B5DCEAE CRC64; MASRLLLNNG AKMPILGLGT WKSPPGQVTE AVKVAIDVGY RHIDCAHVYQ NENEVGVAIQ EKLREQVVKR EELFIVSKLW CTYHEKGLVK GACQKTLSDL KLDYLDLYLI HWPTGFKPGK EFFPLDESGN VVPSDTNILD TWAAMEELVD EGLVKAIGIS NFNHLQVEMI LNKPGLKYKP AVNQIECHPY LTQEKLIQYC QSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK HNKTTAQVLI RFPMQRNLVV IPKSVTPERI AENFKVFDFE LSSQDMTTLL SYNRNWRVCA LLSCTSHKDY PFHEEF //