ID ADH7_HUMAN Reviewed; 386 AA. AC P40394; A2RRB6; A8MVN9; B2R760; B4DWV6; Q13713; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 23-MAR-2010, sequence version 2. DT 24-JAN-2024, entry version 203. DE RecName: Full=All-trans-retinol dehydrogenase [NAD(+)] ADH7 {ECO:0000305}; DE EC=1.1.1.105 {ECO:0000269|PubMed:15369820, ECO:0000269|PubMed:16787387}; DE AltName: Full=Alcohol dehydrogenase class 4 mu/sigma chain; DE EC=1.1.1.1 {ECO:0000269|PubMed:9600267}; DE AltName: Full=Alcohol dehydrogenase class IV mu/sigma chain; DE AltName: Full=Gastric alcohol dehydrogenase; DE AltName: Full=Omega-hydroxydecanoate dehydrogenase ADH7 {ECO:0000305}; DE EC=1.1.1.66 {ECO:0000269|PubMed:9600267}; DE AltName: Full=Retinol dehydrogenase; GN Name=ADH7 {ECO:0000312|HGNC:HGNC:256}; 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). RC TISSUE=Stomach; RX PubMed=7925371; DOI=10.1111/j.1432-1033.1994.00549.x; RA Farres J., Moreno A., Crosas B., Peralba J.M., Allali-Hassani A., RA Hjelmqvist L., Joernvall H., Pares X.; RT "Alcohol dehydrogenase of class IV (sigma sigma-ADH) from human stomach. RT cDNA sequence and structure/function relationships."; RL Eur. J. Biochem. 224:549-557(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Stomach; RX PubMed=8195208; DOI=10.1016/s0021-9258(17)40724-1; RA Satre M.A., Zgombic-Knight M., Duester G.; RT "The complete structure of human class IV alcohol dehydrogenase (retinol RT dehydrogenase) determined from the ADH7 gene."; RL J. Biol. Chem. 269:15606-15612(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7876191; DOI=10.1074/jbc.270.9.4305; RA Zgombic-Knight M., Foglio M.H., Duester G.; RT "Genomic structure and expression of the ADH7 gene encoding human class IV RT alcohol dehydrogenase, the form most efficient for retinol metabolism in RT vitro."; RL J. Biol. Chem. 270:4305-4311(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Esophagus, and Trachea; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 NUCLEOTIDE SEQUENCE [MRNA] OF 13-386 (ISOFORM 1), AND ZINC-BINDING SITES. RC TISSUE=Stomach; RX PubMed=8082805; DOI=10.1016/0014-5793(94)00895-7; RA Yokoyama S., Matsuo Y., Ramsbotham R., Yokoyama R.; RT "Molecular characterization of a class IV human alcohol dehydrogenase gene RT (ADH7)."; RL FEBS Lett. 351:411-415(1994). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-386 (ISOFORM 1). RC TISSUE=Stomach; RX PubMed=7876099; DOI=10.1074/jbc.270.8.3625; RA Kedishvili N.Y., Bosron W.F., Stone C.L., Hurley T.D., Peggs C.F., RA Thomasson H.R., Popov K.M., Carr L.G., Edenberg H.J., Li T.K.; RT "Expression and kinetic characterization of recombinant human stomach RT alcohol dehydrogenase. Active-site amino acid sequence explains substrate RT specificity compared with liver isozymes."; RL J. Biol. Chem. 270:3625-3630(1995). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-386. RC TISSUE=Foreskin; RX PubMed=8824810; DOI=10.1006/geno.1996.0040; RA Yokoyama H., Baraona E., Lieber C.S.; RT "Molecular cloning and chromosomal localization of the ADH7 gene encoding RT human class IV (sigma) ADH."; RL Genomics 31:243-245(1996). RN [11] RP PROTEIN SEQUENCE OF 24-33; 53-58; 74-92; 97-123; 147-154 AND 181-186. RX PubMed=1592118; DOI=10.1016/0014-5793(92)80479-z; RA Pares X., Cederlund E., Moreno A., Saubi N., Hoeoeg J.-O., Joernvall H.; RT "Class IV alcohol dehydrogenase (the gastric enzyme). Structural analysis RT of human sigma sigma-ADH reveals class IV to be variable and confirms the RT presence of a fifth mammalian alcohol dehydrogenase class."; RL FEBS Lett. 303:69-72(1992). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 239-311 (ISOFORM 1). RC TISSUE=Stomach; RX PubMed=7771649; DOI=10.1111/j.1530-0277.1995.tb01490.x; RA Cheung B., Anderson J.K., Holmes R.S., Beacham I.R.; RT "Human stomach class IV alcohol dehydrogenase: molecular genetic RT analysis."; RL Alcohol. Clin. Exp. Res. 19:185-186(1995). RN [13] RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY RP REGULATION. RX PubMed=9600267; DOI=10.1016/s0014-5793(98)00374-3; RA Allali-Hassani A., Peralba J.M., Martras S., Farres J., Pares X.; RT "Retinoids, omega-hydroxyfatty acids and cytotoxic aldehydes as RT physiological substrates, and H2-receptor antagonists as pharmacological RT inhibitors, of human class IV alcohol dehydrogenase."; RL FEBS Lett. 426:362-366(1998). RN [14] RP CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=15369820; DOI=10.1016/j.abb.2004.07.002; RA Martras S., Alvarez R., Gallego O., Dominguez M., de Lera A.R., Farres J., RA Pares X.; RT "Kinetics of human alcohol dehydrogenase with ring-oxidized retinoids: RT effect of Tween 80."; RL Arch. Biochem. Biophys. 430:210-217(2004). RN [15] RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16787387; DOI=10.1042/bj20051988; RA Gallego O., Belyaeva O.V., Porte S., Ruiz F.X., Stetsenko A.V., RA Shabrova E.V., Kostereva N.V., Farres J., Pares X., Kedishvili N.Y.; RT "Comparative functional analysis of human medium-chain dehydrogenases, RT short-chain dehydrogenases/reductases and aldo-keto reductases with RT retinoids."; RL Biochem. J. 399:101-109(2006). RN [16] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 14-386. RX PubMed=9228021; DOI=10.1074/jbc.272.30.18558; RA Xie P., Parsons S.H., Speckhard D.C., Bosron W.F., Hurley T.D.; RT "X-ray structure of human class IV sigmasigma alcohol dehydrogenase. RT Structural basis for substrate specificity."; RL J. Biol. Chem. 272:18558-18563(1997). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 14-386 IN COMPLEX WITH NAD AND RP ZINC IONS. RX PubMed=10631979; DOI=10.1110/ps.8.12.2639; RA Xie P.T., Hurley T.D.; RT "Methionine-141 directly influences the binding of 4-methylpyrazole in RT human sigma sigma alcohol dehydrogenase."; RL Protein Sci. 8:2639-2644(1999). CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation of all-trans-retinol, CC alcohol, and omega-hydroxy fatty acids and their derivatives CC (PubMed:15369820, PubMed:16787387, PubMed:9600267). Oxidizes CC preferentially all trans-retinol, all-trans-4-hydroxyretinol, 9-cis- CC retinol, 2-hexenol, and long chain omega-hydroxy fatty acids such as CC juniperic acid (PubMed:15369820, PubMed:16787387, PubMed:9600267). In CC vitro can also catalyzes the NADH-dependent reduction of all-trans- CC retinal and aldehydes and their derivatives (PubMed:15369820, CC PubMed:16787387, PubMed:9600267). Reduces preferentially all trans- CC retinal, all-trans-4-oxoretinal and hexanal (PubMed:15369820, CC PubMed:16787387). Catalyzes in the oxidative direction with higher CC efficiency (PubMed:16787387, PubMed:15369820). Therefore may CC participate in retinoid metabolism, fatty acid omega-oxidation, and CC elimination of cytotoxic aldehydes produced by lipid peroxidation CC (PubMed:9600267, PubMed:15369820, PubMed:16787387). CC {ECO:0000269|PubMed:15369820, ECO:0000269|PubMed:16787387, CC ECO:0000269|PubMed:9600267}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; CC Evidence={ECO:0000269|PubMed:9600267}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10737; CC Evidence={ECO:0000305|PubMed:9600267}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10738; CC Evidence={ECO:0000305|PubMed:9600267}; CC -!- CATALYTIC ACTIVITY: CC Reaction=10-hydroxydecanoate + NAD(+) = 10-oxodecanoate + H(+) + NADH; CC Xref=Rhea:RHEA:20880, ChEBI:CHEBI:11305, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58022; EC=1.1.1.66; CC Evidence={ECO:0000269|PubMed:9600267}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20881; CC Evidence={ECO:0000305|PubMed:9600267}; CC -!- CATALYTIC ACTIVITY: CC Reaction=all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH; CC Xref=Rhea:RHEA:21284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC EC=1.1.1.105; Evidence={ECO:0000269|PubMed:15369820, CC ECO:0000269|PubMed:16787387, ECO:0000269|PubMed:9600267}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21285; CC Evidence={ECO:0000305|PubMed:16787387}; CC -!- CATALYTIC ACTIVITY: CC Reaction=9-cis-retinol + NAD(+) = 9-cis-retinal + H(+) + NADH; CC Xref=Rhea:RHEA:42052, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273; CC Evidence={ECO:0000269|PubMed:9600267}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42053; CC Evidence={ECO:0000305|PubMed:9600267}; CC -!- CATALYTIC ACTIVITY: CC Reaction=all-trans-3,4-didehydroretinol + NAD(+) = all-trans-3,4- CC didehydroretinal + H(+) + NADH; Xref=Rhea:RHEA:55940, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28537, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:132246; CC Evidence={ECO:0000269|PubMed:15369820}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55941; CC Evidence={ECO:0000305|PubMed:15369820}; CC -!- CATALYTIC ACTIVITY: CC Reaction=all-trans-4-hydroxyretinol + NAD(+) = all-trans-4- CC hydroxyretinal + H(+) + NADH; Xref=Rhea:RHEA:55936, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:132259, ChEBI:CHEBI:139346; CC Evidence={ECO:0000269|PubMed:15369820}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55937; CC Evidence={ECO:0000305|PubMed:15369820}; CC -!- CATALYTIC ACTIVITY: CC Reaction=all-trans-4-oxoretinol + NAD(+) = all-trans-4-oxoretinal + CC H(+) + NADH; Xref=Rhea:RHEA:60632, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:44597, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:139347; Evidence={ECO:0000269|PubMed:15369820}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:60634; CC Evidence={ECO:0000305|PubMed:15369820}; CC -!- CATALYTIC ACTIVITY: CC Reaction=12-hydroxydodecanoate + NAD(+) = 12-oxododecanoate + H(+) + CC NADH; Xref=Rhea:RHEA:60980, ChEBI:CHEBI:15378, ChEBI:CHEBI:36204, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:144067; CC Evidence={ECO:0000269|PubMed:9600267}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60981; CC Evidence={ECO:0000305|PubMed:9600267}; CC -!- CATALYTIC ACTIVITY: CC Reaction=16-hydroxyhexadecanoate + NAD(+) = 16-oxohexadecanoate + H(+) CC + NADH; Xref=Rhea:RHEA:60984, ChEBI:CHEBI:15378, ChEBI:CHEBI:55329, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:144068; CC Evidence={ECO:0000269|PubMed:9600267}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60985; CC Evidence={ECO:0000305|PubMed:9600267}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexan-1-ol + NAD(+) = H(+) + hexanal + NADH; CC Xref=Rhea:RHEA:60972, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:87393, ChEBI:CHEBI:88528; CC Evidence={ECO:0000269|PubMed:9600267}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60973; CC Evidence={ECO:0000305|PubMed:9600267}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:60974; CC Evidence={ECO:0000305|PubMed:9600267}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-hex-2-en-1-ol + NAD(+) = (E)-hex-2-enal + H(+) + NADH; CC Xref=Rhea:RHEA:60988, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:141205; CC Evidence={ECO:0000269|PubMed:9600267}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60989; CC Evidence={ECO:0000305|PubMed:9600267}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:60990; CC Evidence={ECO:0000305|PubMed:9600267}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-4-hydroxynon-2-en-1-ol + NAD(+) = (E)-4-hydroxynon-2-enal CC + H(+) + NADH; Xref=Rhea:RHEA:60976, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58968, CC ChEBI:CHEBI:142617; Evidence={ECO:0000269|PubMed:9600267}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:60978; CC Evidence={ECO:0000305|PubMed:9600267}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:10631979}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:10631979}; CC -!- ACTIVITY REGULATION: Retinol oxidation is inhibited by the detergent CC Tween 80 (PubMed:15369820). Ethanol inhibits both all-trans-retinol and CC 9-cis-retinol oxidation (PubMed:9600267). 13-cis-retinol is an CC effective competitive inhibitor of the 9-cis-retinol oxidation CC (PubMed:9600267). All-trans-retinoic acid is a powerful inhibitor of CC all-trans-retinol oxidation (PubMed:9600267). 13-cis-retinoic acid is a CC powerful inhibitor of all-trans-retinol oxidation (PubMed:9600267). CC Cimetidine competitively inhibited ethanol oxidation (PubMed:9600267). CC {ECO:0000269|PubMed:15369820, ECO:0000269|PubMed:9600267}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=23 uM for all-trans-retinol {ECO:0000269|PubMed:15369820}; CC KM=15 uM for all-trans-4-hydroxyretinol CC {ECO:0000269|PubMed:15369820}; CC KM=28 uM for all-trans-3,4-didehydroretinol CC {ECO:0000269|PubMed:15369820}; CC KM=34 uM for all-trans-retinal {ECO:0000269|PubMed:15369820, CC ECO:0000269|PubMed:9600267}; CC KM=17 uM for all-trans-4-oxoretinal {ECO:0000269|PubMed:15369820}; CC KM=26 uM for all-trans-3,4-didehydroretinal CC {ECO:0000269|PubMed:15369820}; CC KM=0.3 uM for all-trans-retinol {ECO:0000269|PubMed:16787387}; CC KM=0.8 uM for all-trans-retinal {ECO:0000269|PubMed:16787387}; CC KM=0.1 mM for 10-OH-decanoic acid (with 0.1 M sodium phosphate at pH CC 7.5) {ECO:0000269|PubMed:9600267}; CC KM=0.17 mM for 12-OH-dodecanoic acid (with 0.1 M sodium phosphate at CC pH 7.5) {ECO:0000269|PubMed:9600267}; CC KM=0.07 mM for 12-OH-dodecanoic acid (with 0.1 M glycine/NaOH at pH CC 10) {ECO:0000269|PubMed:9600267}; CC KM=0.035 mM for 16-OH-hexadecanoic acid (with 0.1 M glycine/NaOH at CC pH 10) {ECO:0000269|PubMed:9600267}; CC KM=0.14 mM for hexanol (with 0.1 M sodium phosphate at pH 7.5) CC {ECO:0000269|PubMed:9600267}; CC KM=0.02 mM for hexanal (with 0.1 M sodium phosphate at pH 7.5) CC {ECO:0000269|PubMed:9600267}; CC KM=0.017 mM for 2-hexenol (with 0.1 M sodium phosphate at pH 7.5) CC {ECO:0000269|PubMed:9600267}; CC KM=0.025 mM for 2-hexenal (with 0.1 M sodium phosphate at pH 7.5) CC {ECO:0000269|PubMed:9600267}; CC KM=0.038 mM for 4-hydroxynonenal (with 0.1 M sodium phosphate at pH CC 7.5) {ECO:0000269|PubMed:9600267}; CC KM=15 uM for all-trans-retinol {ECO:0000269|PubMed:9600267}; CC KM=36 uM for 9-cis-retinol {ECO:0000269|PubMed:9600267}; CC KM=21 uM for 9-cis-retinal {ECO:0000269|PubMed:9600267}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10631979}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P40394-1; Sequence=Displayed; CC Name=2; CC IsoId=P40394-2; Sequence=VSP_043093; CC -!- TISSUE SPECIFICITY: Preferentially expressed in stomach. CC -!- MISCELLANEOUS: There are 7 different ADH's isozymes in human: three CC belongs to class-I: alpha, beta, and gamma, one to class-II: pi, one to CC class-III: chi, one to class-IV: ADH7 and one to class-V: ADH6. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Class-IV subfamily. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-13 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA19002.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAC51351.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAG35707.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA53960.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA53961.1; Type=Erroneous initiation; Evidence={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; X76342; CAA53961.1; ALT_INIT; mRNA. DR EMBL; X76342; CAA53960.1; ALT_INIT; mRNA. DR EMBL; U07821; AAA19002.1; ALT_INIT; mRNA. DR EMBL; U16293; AAC51351.1; ALT_INIT; Genomic_DNA. DR EMBL; U16286; AAC51351.1; JOINED; Genomic_DNA. DR EMBL; U16287; AAC51351.1; JOINED; Genomic_DNA. DR EMBL; U16288; AAC51351.1; JOINED; Genomic_DNA. DR EMBL; U16289; AAC51351.1; JOINED; Genomic_DNA. DR EMBL; U16290; AAC51351.1; JOINED; Genomic_DNA. DR EMBL; U16291; AAC51351.1; JOINED; Genomic_DNA. DR EMBL; U16292; AAC51351.1; JOINED; Genomic_DNA. DR EMBL; AK301696; BAG63168.1; -; mRNA. DR EMBL; AK312854; BAG35707.1; ALT_INIT; mRNA. DR EMBL; AP001960; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471057; EAX06101.1; -; Genomic_DNA. DR EMBL; BC131512; AAI31513.1; -; mRNA. DR EMBL; L33179; AAA59211.1; -; mRNA. DR EMBL; U09623; AAA82165.1; -; mRNA. DR EMBL; L47166; AAB38424.1; -; Genomic_DNA. DR EMBL; S77168; AAB34478.1; -; mRNA. DR CCDS; CCDS54781.1; -. [P40394-2] DR PIR; A55878; DEHUAS. DR RefSeq; NP_000664.2; NM_000673.4. DR RefSeq; NP_001159976.1; NM_001166504.1. [P40394-2] DR PDB; 1AGN; X-ray; 3.00 A; A/B/C/D=14-386. DR PDB; 1D1S; X-ray; 2.50 A; A/B/C/D=14-386. DR PDB; 1D1T; X-ray; 2.40 A; A/B/C/D=14-386. DR PDBsum; 1AGN; -. DR PDBsum; 1D1S; -. DR PDBsum; 1D1T; -. DR AlphaFoldDB; P40394; -. DR SMR; P40394; -. DR BioGRID; 106643; 13. DR IntAct; P40394; 2. DR STRING; 9606.ENSP00000420269; -. DR BindingDB; P40394; -. DR ChEMBL; CHEMBL3867; -. DR DrugBank; DB00898; Ethanol. DR DrugBank; DB00157; NADH. DR SwissLipids; SLP:000001879; -. DR iPTMnet; P40394; -. DR PhosphoSitePlus; P40394; -. DR BioMuta; ADH7; -. DR DMDM; 292495000; -. DR jPOST; P40394; -. DR MassIVE; P40394; -. DR PaxDb; 9606-ENSP00000420269; -. DR PeptideAtlas; P40394; -. DR PRIDE; P40394; -. DR ProteomicsDB; 55365; -. [P40394-1] DR ProteomicsDB; 55366; -. [P40394-2] DR Pumba; P40394; -. DR Antibodypedia; 25891; 396 antibodies from 31 providers. DR DNASU; 131; -. DR Ensembl; ENST00000209665.8; ENSP00000209665.4; ENSG00000196344.12. [P40394-1] DR Ensembl; ENST00000476959.5; ENSP00000420269.1; ENSG00000196344.12. [P40394-2] DR GeneID; 131; -. DR KEGG; hsa:131; -. DR UCSC; uc003huv.2; human. [P40394-1] DR AGR; HGNC:256; -. DR CTD; 131; -. DR DisGeNET; 131; -. DR GeneCards; ADH7; -. DR HGNC; HGNC:256; ADH7. DR HPA; ENSG00000196344; Tissue enriched (esophagus). DR MIM; 600086; gene. DR neXtProt; NX_P40394; -. DR OpenTargets; ENSG00000196344; -. DR PharmGKB; PA24577; -. DR VEuPathDB; HostDB:ENSG00000196344; -. DR eggNOG; KOG0022; Eukaryota. DR GeneTree; ENSGT00940000162708; -. DR InParanoid; P40394; -. DR OrthoDB; 1077476at2759; -. DR PhylomeDB; P40394; -. DR TreeFam; TF300429; -. DR PathwayCommons; P40394; -. DR Reactome; R-HSA-71384; Ethanol oxidation. DR SignaLink; P40394; -. DR BioGRID-ORCS; 131; 8 hits in 1151 CRISPR screens. DR EvolutionaryTrace; P40394; -. DR GeneWiki; ADH7; -. DR GenomeRNAi; 131; -. DR Pharos; P40394; Tchem. DR PRO; PR:P40394; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P40394; Protein. DR Bgee; ENSG00000196344; Expressed in lower esophagus mucosa and 111 other cell types or tissues. DR ExpressionAtlas; P40394; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; TAS:UniProtKB. DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IDA:UniProtKB. DR GO; GO:0004031; F:aldehyde oxidase activity; IDA:UniProtKB. DR GO; GO:0035276; F:ethanol binding; IDA:UniProtKB. DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IDA:UniProtKB. DR GO; GO:0050153; F:omega-hydroxydecanoate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0048019; F:receptor antagonist activity; IDA:UniProtKB. DR GO; GO:0019841; F:retinol binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0006069; P:ethanol oxidation; IDA:UniProtKB. DR GO; GO:0010430; P:fatty acid omega-oxidation; IDA:UniProtKB. DR GO; GO:0009617; P:response to bacterium; IDA:UniProtKB. DR GO; GO:0045471; P:response to ethanol; IDA:UniProtKB. DR GO; GO:0042573; P:retinoic acid metabolic process; IBA:GO_Central. DR GO; GO:0001523; P:retinoid metabolic process; IDA:UniProtKB. DR GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central. DR CDD; cd08299; alcohol_DH_class_I_II_IV; 1. DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR013149; ADH-like_C. DR InterPro; IPR013154; ADH-like_N. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1. DR PANTHER; PTHR43880:SF2; ALL-TRANS-RETINOL DEHYDROGENASE [NAD(+)] ADH7; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; GroES-like; 2. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00059; ADH_ZINC; 1. DR Genevisible; P40394; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing; KW Lipid metabolism; Metal-binding; NAD; Oxidoreductase; Reference proteome; KW Zinc. FT CHAIN 1..386 FT /note="All-trans-retinol dehydrogenase [NAD(+)] ADH7" FT /id="PRO_0000160691" FT BINDING 59 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT BINDING 60..64 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT BINDING 80 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT BINDING 110 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT BINDING 113 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT BINDING 116 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT BINDING 124 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT BINDING 186 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT BINDING 211..216 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT BINDING 235 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT BINDING 240 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT BINDING 281..283 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT BINDING 304..306 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT BINDING 329..331 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT BINDING 381 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10631979, FT ECO:0007744|PDB:1AGN, ECO:0007744|PDB:1D1S, FT ECO:0007744|PDB:1D1T" FT VAR_SEQ 1..18 FT /note="MFAEIQIQDKDRMGTAGK -> MKCLVSRHTVRETLDMVFQRMSVEAG (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043093" FT VARIANT 92 FT /note="G -> A (in dbSNP:rs1573496)" FT /id="VAR_024364" FT CONFLICT 9 FT /note="D -> E (in Ref. 2; AAA19002)" FT /evidence="ECO:0000305" FT CONFLICT 32 FT /note="Q -> R (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 83 FT /note="T -> R (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 110 FT /note="C -> V (in Ref. 10; AAB38424)" FT /evidence="ECO:0000305" FT CONFLICT 150..151 FT /note="HH -> GR (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 160..161 FT /note="EY -> VI (in Ref. 10; AAB38424)" FT /evidence="ECO:0000305" FT CONFLICT 169 FT /note="V -> E (in Ref. 10; AAB38424)" FT /evidence="ECO:0000305" FT CONFLICT 175 FT /note="A -> T (in Ref. 4; BAG35707)" FT /evidence="ECO:0000305" FT CONFLICT 217 FT /note="L -> V (in Ref. 10; AAB38424)" FT /evidence="ECO:0000305" FT STRAND 20..29 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 35..41 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 48..57 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 60..67 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:1AGN" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 81..89 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 101..104 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 114..117 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 142..150 FT /evidence="ECO:0007829|PDB:1D1T" FT TURN 153..155 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 158..165 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 178..181 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 182..185 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 187..196 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 206..210 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 214..225 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 229..234 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 238..240 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 241..247 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 250..253 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 262..270 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 276..279 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 284..291 FT /evidence="ECO:0007829|PDB:1D1T" FT TURN 296..298 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 300..303 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 313..315 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 318..321 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 325..328 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 331..333 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 336..347 FT /evidence="ECO:0007829|PDB:1D1T" FT TURN 348..350 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 355..357 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 358..363 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 364..366 FT /evidence="ECO:0007829|PDB:1D1T" FT HELIX 367..375 FT /evidence="ECO:0007829|PDB:1D1T" FT STRAND 380..385 FT /evidence="ECO:0007829|PDB:1D1T" SQ SEQUENCE 386 AA; 41481 MW; E34C959778ED6817 CRC64; MFAEIQIQDK DRMGTAGKVI KCKAAVLWEQ KQPFSIEEIE VAPPKTKEVR IKILATGICR TDDHVIKGTM VSKFPVIVGH EATGIVESIG EGVTTVKPGD KVIPLFLPQC RECNACRNPD GNLCIRSDIT GRGVLADGTT RFTCKGKPVH HFMNTSTFTE YTVVDESSVA KIDDAAPPEK VCLIGCGFST GYGAAVKTGK VKPGSTCVVF GLGGVGLSVI MGCKSAGASR IIGIDLNKDK FEKAMAVGAT ECISPKDSTK PISEVLSEMT GNNVGYTFEV IGHLETMIDA LASCHMNYGT SVVVGVPPSA KMLTYDPMLL FTGRTWKGCV FGGLKSRDDV PKLVTEFLAK KFDLDQLITH VLPFKKISEG FELLNSGQSI RTVLTF //