ADH1B_HUMAN
ID ADH1B_HUMAN Reviewed; 375 AA.
AC P00325; A8MYN5; B4DRS9; B4DVC3; Q13711; Q4ZGI9; Q96KI7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=All-trans-retinol dehydrogenase [NAD(+)] ADH1B {ECO:0000305};
DE EC=1.1.1.105 {ECO:0000269|PubMed:16787387};
DE AltName: Full=Alcohol dehydrogenase 1B;
DE AltName: Full=Alcohol dehydrogenase subunit beta;
GN Name=ADH1B {ECO:0000312|HGNC:HGNC:250}; Synonyms=ADH2;
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 VARIANT ARG-48.
RX PubMed=2986130; DOI=10.1073/pnas.82.9.2703;
RA Ikuta T., Fujiyoshi T., Kurachi K., Yoshida A.;
RT "Molecular cloning of a full-length cDNA for human alcohol dehydrogenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2703-2707(1985).
RN [2]
RP ERRATUM OF PUBMED:2986130.
RA Ikuta T., Fujiyoshi T., Kurachi K., Yoshida A.;
RL Proc. Natl. Acad. Sci. U.S.A. 82:5578-5578(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-48.
RX PubMed=3000832; DOI=10.1016/0014-5793(86)80111-9;
RA Heden L.-O., Hoeoeg J.-O., Larsson K., Lake M., Lagerholm E., Holmgren A.,
RA Vallee B.L., Joernvall H., von Bahr-Lindstroem H.;
RT "cDNA clones coding for the beta-subunit of human liver alcohol
RT dehydrogenase have differently sized 3'-non-coding regions.";
RL FEBS Lett. 194:327-332(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-48.
RX PubMed=2935533; DOI=10.1016/s0021-9258(17)35892-1;
RA Duester G., Smith M., Bilanchone V., Hatfield G.W.;
RT "Molecular analysis of the human class I alcohol dehydrogenase gene family
RT and nucleotide sequence of the gene encoding the beta subunit.";
RL J. Biol. Chem. 261:2027-2033(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2935875; DOI=10.1073/pnas.83.3.634;
RA Ikuta T., Szeto S., Yoshida A.;
RT "Three human alcohol dehydrogenase subunits: cDNA structure and molecular
RT and evolutionary divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:634-638(1986).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-48.
RA Yokoyama S., Yokoyama R., Rotwein P.;
RT "Molecular characterization of cDNA clones encoding the human alcohol
RT dehydrogenase beta 1 and the evolutionary relationship to the other class I
RT subunits alpha and gamma.";
RL Jpn. J. Genet. 62:241-256(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-57 AND CYS-370, AND
RP POLYMORPHISM.
RC TISSUE=Liver;
RX PubMed=2679216; DOI=10.1111/j.1530-0277.1989.tb00383.x;
RA Carr L.G., Xu Y., Ho W.H., Edenberg H.J.;
RT "Nucleotide sequence of the ADH2(3) gene encoding the human alcohol
RT dehydrogenase beta 3 subunit.";
RL Alcohol. Clin. Exp. Res. 13:594-596(1989).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND POLYMORPHISM.
RX PubMed=2547609; DOI=10.1111/j.1432-1033.1989.tb14931.x;
RA Matsuo Y., Yokoyama R., Yokoyama S.;
RT "The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by
RT only one nucleotide.";
RL Eur. J. Biochem. 183:317-320(1989).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Polin L., Hey-Chi H.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-48; SER-60 AND CYS-370.
RG NIEHS SNPs program;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ARG-48.
RC TISSUE=Small intestine;
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 [12]
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 [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-48.
RC TISSUE=Testis;
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 [14]
RP PROTEIN SEQUENCE OF 2-375, CLEAVAGE OF INITIATOR METHIONINE, AND
RP ACETYLATION AT SER-2.
RX PubMed=6391920; DOI=10.1111/j.1432-1033.1984.tb08573.x;
RA Hempel J., Buhler R., Kaiser R., Holmquist B., de Zalenski C.,
RA von Wartburg J.-P., Vallee B.L., Joernvall H.;
RT "Human liver alcohol dehydrogenase. 1. The primary structure of the beta 1
RT beta 1 isoenzyme.";
RL Eur. J. Biochem. 145:437-445(1984).
RN [15]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-57.
RX PubMed=3397059; DOI=10.1016/0888-7543(88)90004-3;
RA Xu Y.L., Carr L.G., Bosron W.F., Li T.K., Edenberg H.J.;
RT "Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci
RT following DNA sequence amplification.";
RL Genomics 2:209-214(1988).
RN [16]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-86, AND VARIANT ARG-48.
RA Osier M., Speed W.C., Seaman M.I., Kidd K.K.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [17]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL 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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND TYR-35, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP VARIANT ARG-48, AND POLYMORPHISM.
RX PubMed=6374651; DOI=10.1073/pnas.81.10.3024;
RA Joernvall H., Hempel J., Vallee B.L., Bosron W.F., Li T.-K.;
RT "Human liver alcohol dehydrogenase: amino acid substitution in the beta 2
RT beta 2 Oriental isozyme explains functional properties, establishes an
RT active site structure, and parallels mutational exchanges in the yeast
RT enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:3024-3028(1984).
RN [21]
RP VARIANT CYS-370, AND POLYMORPHISM.
RX PubMed=3619918; DOI=10.1016/0006-291x(87)90779-0;
RA Burnell J.C., Carr L.G., Dwulet F.E., Edenberg H.J., Li T.-K., Bosron W.F.;
RT "The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a
RT Cys for Arg-369 substitution which decreases NAD(H) binding.";
RL Biochem. Biophys. Res. Commun. 146:1127-1133(1987).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=1896463; DOI=10.1073/pnas.88.18.8149;
RA Hurley T.D., Bosron W.F., Hamilton J.A., Amzel L.M.;
RT "Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects
RT of non-active-site substitutions.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8149-8153(1991).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
RX PubMed=8201622; DOI=10.1006/jmbi.1994.1382;
RA Hurley T.D., Bosron W.F., Stone C.L., Amzel L.M.;
RT "Structures of three human beta alcohol dehydrogenase variants.
RT Correlations with their functional differences.";
RL J. Mol. Biol. 239:415-429(1994).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=8663387; DOI=10.1074/jbc.271.29.17057;
RA Davis G.J., Bosron W.F., Stone C.L., Owusu-Dekyi K., Hurley T.D.;
RT "X-ray structure of human beta3beta3 alcohol dehydrogenase. The
RT contribution of ionic interactions to coenzyme binding.";
RL J. Biol. Chem. 271:17057-17061(1996).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=11274460; DOI=10.1110/ps.45001;
RA Niederhut M.S., Gibbons B.J., Perez-Miller S., Hurley T.D.;
RT "Three-dimensional structures of the three human class I alcohol
RT dehydrogenases.";
RL Protein Sci. 10:697-706(2001).
RN [26]
RP POLYMORPHISM.
RX PubMed=10733556; DOI=10.1053/he.2000.5978;
RA Borras E., Coutelle C., Rosell A., Fernandez-Muixi F., Broch M., Crosas B.,
RA Hjelmqvist L., Lorenzo A., Gutierrez C., Santos M., Szczepanek M.,
RA Heilig M., Quattrocchi P., Farres J., Vidal F., Richart C., Mach T.,
RA Bogdal J., Joernvall H., Seitz H.K., Couzigou P., Pares X.;
RT "Genetic polymorphism of alcohol dehydrogenase in Europeans: the ADH2*2
RT allele decreases the risk for alcoholism and is associated with ADH3*1.";
RL Hepatology 31:984-989(2000).
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation of all-trans-retinol
CC and its derivatives such as all-trans-4-hydroxyretinol and may
CC participate in retinoid metabolism (PubMed:15369820, PubMed:16787387).
CC In vitro can also catalyzes the NADH-dependent reduction of all-trans-
CC retinal and its derivatives such as all-trans-4-oxoretinal
CC (PubMed:15369820, PubMed:16787387). Catalyzes in the oxidative
CC direction with higher efficiency (PubMed:16787387). Has the same
CC affinity for all-trans-4-hydroxyretinol and all-trans-4-oxoretinal
CC (PubMed:15369820). {ECO:0000269|PubMed:15369820,
CC ECO:0000269|PubMed:16787387}.
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:16787387};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21285;
CC Evidence={ECO:0000305|PubMed:16787387};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4 uM for all-trans-4-hydroxyretinol (in allele ADH1B*1)
CC {ECO:0000269|PubMed:15369820};
CC KM=25 uM for all-trans-4-oxoretinal (in allele ADH1B*1)
CC {ECO:0000269|PubMed:15369820};
CC KM=11 uM for all-trans-4-hydroxyretinol (in allele ADH1B*2)
CC {ECO:0000269|PubMed:15369820};
CC KM=27 uM for all-trans-4-oxoretinal (in allele ADH1B*2)
CC {ECO:0000269|PubMed:15369820};
CC KM=24 uM for all-trans-3,4-didehydroretinol(in allele ADH1B*2)
CC {ECO:0000269|PubMed:15369820};
CC KM=25 uM for all-trans-3,4-didehydroretinal(in allele ADH1B*2)
CC {ECO:0000269|PubMed:15369820};
CC KM=0.4 uM for all-trans-retinaldehyde (in allele ADH1B*2)
CC {ECO:0000269|PubMed:16787387};
CC KM=0.3 uM for all-trans-retinol (in allele ADH1B*2)
CC {ECO:0000269|PubMed:16787387};
CC -!- SUBUNIT: Dimer of identical or non-identical chains of three types;
CC alpha, beta and gamma.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P00325-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P00325-2; Sequence=VSP_054847;
CC -!- POLYMORPHISM: Three alleles are known: ADH1B*1 (ADH2*1) corresponding
CC to variant beta-1, ADH1B*2 (ADH2*2) corresponding to variant beta-2,
CC ADH1B*3 (ADH2*3) corresponding to variant beta-3. The sequence shown is
CC that of allele ADH1B*2. The ADH1B*2 allele frequency in orientals is
CC approximately 75%, whereas it is less than 5% in most Caucasian
CC populations. The ADH1B*2 allele is associated with a lower risk of
CC alcoholism. ADH1B variations have been associated with protection
CC against alcohol dependence and alcohol-related aerodigestive tract
CC cancer [MIM:103720]. {ECO:0000269|PubMed:10733556,
CC ECO:0000269|PubMed:2547609, ECO:0000269|PubMed:2679216,
CC ECO:0000269|PubMed:3619918, ECO:0000269|PubMed:6374651}.
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. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/adh1b/";
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; M24317; AAA51884.1; -; mRNA.
DR EMBL; X03350; CAA27056.1; -; mRNA.
DR EMBL; M24316; AAB59496.1; -; Genomic_DNA.
DR EMBL; M24308; AAB59496.1; JOINED; Genomic_DNA.
DR EMBL; M24309; AAB59496.1; JOINED; Genomic_DNA.
DR EMBL; M24310; AAB59496.1; JOINED; Genomic_DNA.
DR EMBL; M24311; AAB59496.1; JOINED; Genomic_DNA.
DR EMBL; M24312; AAB59496.1; JOINED; Genomic_DNA.
DR EMBL; M24313; AAB59496.1; JOINED; Genomic_DNA.
DR EMBL; M24314; AAB59496.1; JOINED; Genomic_DNA.
DR EMBL; D00137; BAA00084.1; -; mRNA.
DR EMBL; L38290; AAB48003.1; -; Genomic_DNA.
DR EMBL; L38283; AAB48003.1; JOINED; Genomic_DNA.
DR EMBL; L38284; AAB48003.1; JOINED; Genomic_DNA.
DR EMBL; L38285; AAB48003.1; JOINED; Genomic_DNA.
DR EMBL; L38286; AAB48003.1; JOINED; Genomic_DNA.
DR EMBL; L38287; AAB48003.1; JOINED; Genomic_DNA.
DR EMBL; L38288; AAB48003.1; JOINED; Genomic_DNA.
DR EMBL; L38289; AAB48003.1; JOINED; Genomic_DNA.
DR EMBL; X15447; CAA33487.1; -; Genomic_DNA.
DR EMBL; X15448; CAA33487.1; JOINED; Genomic_DNA.
DR EMBL; X15449; CAA33487.1; JOINED; Genomic_DNA.
DR EMBL; X15450; CAA33487.1; JOINED; Genomic_DNA.
DR EMBL; X15451; CAA33487.1; JOINED; Genomic_DNA.
DR EMBL; X15452; CAA33487.1; JOINED; Genomic_DNA.
DR EMBL; X15453; CAA33487.1; JOINED; Genomic_DNA.
DR EMBL; X15454; CAA33487.1; JOINED; Genomic_DNA.
DR EMBL; X15455; CAA33487.1; JOINED; Genomic_DNA.
DR EMBL; AF153821; AAD37446.1; -; mRNA.
DR EMBL; DQ017646; AAY22180.1; -; Genomic_DNA.
DR EMBL; AK301018; BAG62635.1; -; mRNA.
DR EMBL; AC097530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033009; AAH33009.1; -; mRNA.
DR EMBL; M21692; AAA51592.1; -; mRNA.
DR EMBL; AF040967; AAB96912.1; -; Genomic_DNA.
DR CCDS; CCDS34033.1; -. [P00325-1]
DR CCDS; CCDS68761.1; -. [P00325-2]
DR PIR; A23607; DEHUAB.
DR RefSeq; NP_000659.2; NM_000668.5.
DR RefSeq; NP_001273579.1; NM_001286650.1.
DR PDB; 1DEH; X-ray; 2.20 A; A/B=2-375.
DR PDB; 1HDX; X-ray; 2.50 A; A/B=2-375.
DR PDB; 1HDY; X-ray; 2.50 A; A/B=2-375.
DR PDB; 1HDZ; X-ray; 2.50 A; A/B=2-375.
DR PDB; 1HSZ; X-ray; 2.20 A; A/B=2-375.
DR PDB; 1HTB; X-ray; 2.40 A; A/B=2-375.
DR PDB; 1U3U; X-ray; 1.60 A; A/B=2-375.
DR PDB; 1U3V; X-ray; 1.65 A; A/B=2-375.
DR PDB; 3HUD; X-ray; 3.20 A; A/B=2-375.
DR PDBsum; 1DEH; -.
DR PDBsum; 1HDX; -.
DR PDBsum; 1HDY; -.
DR PDBsum; 1HDZ; -.
DR PDBsum; 1HSZ; -.
DR PDBsum; 1HTB; -.
DR PDBsum; 1U3U; -.
DR PDBsum; 1U3V; -.
DR PDBsum; 3HUD; -.
DR AlphaFoldDB; P00325; -.
DR SMR; P00325; -.
DR BioGRID; 106637; 8.
DR IntAct; P00325; 11.
DR MINT; P00325; -.
DR STRING; 9606.ENSP00000306606; -.
DR BindingDB; P00325; -.
DR ChEMBL; CHEMBL3284; -.
DR DrugBank; DB02721; 4-Iodopyrazole.
DR DrugBank; DB03703; Cyclohexanol.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB01213; Fomepizole.
DR DrugBank; DB09462; Glycerin.
DR DrugBank; DB02481; N-Benzylformamide.
DR DrugBank; DB04105; N-Heptylformamide.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR DrugCentral; P00325; -.
DR SwissLipids; SLP:000001880; -.
DR iPTMnet; P00325; -.
DR PhosphoSitePlus; P00325; -.
DR BioMuta; ADH1B; -.
DR DMDM; 113394; -.
DR EPD; P00325; -.
DR jPOST; P00325; -.
DR MassIVE; P00325; -.
DR PaxDb; P00325; -.
DR PeptideAtlas; P00325; -.
DR PRIDE; P00325; -.
DR ProteomicsDB; 2413; -.
DR ProteomicsDB; 51228; -. [P00325-1]
DR Antibodypedia; 14861; 308 antibodies from 32 providers.
DR DNASU; 125; -.
DR Ensembl; ENST00000305046.13; ENSP00000306606.8; ENSG00000196616.14. [P00325-1]
DR Ensembl; ENST00000506651.5; ENSP00000425998.2; ENSG00000196616.14. [P00325-2]
DR Ensembl; ENST00000625860.2; ENSP00000486614.1; ENSG00000196616.14. [P00325-2]
DR Ensembl; ENST00000639454.1; ENSP00000491622.1; ENSG00000196616.14. [P00325-1]
DR GeneID; 125; -.
DR KEGG; hsa:125; -.
DR MANE-Select; ENST00000305046.13; ENSP00000306606.8; NM_000668.6; NP_000659.2.
DR UCSC; uc011cei.3; human. [P00325-1]
DR CTD; 125; -.
DR DisGeNET; 125; -.
DR GeneCards; ADH1B; -.
DR HGNC; HGNC:250; ADH1B.
DR HPA; ENSG00000196616; Tissue enhanced (adipose tissue, liver).
DR MalaCards; ADH1B; -.
DR MIM; 103720; gene+phenotype.
DR neXtProt; NX_P00325; -.
DR OpenTargets; ENSG00000196616; -.
DR PharmGKB; PA24571; -.
DR VEuPathDB; HostDB:ENSG00000196616; -.
DR eggNOG; KOG0022; Eukaryota.
DR GeneTree; ENSGT00940000155234; -.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; P00325; -.
DR OrthoDB; 664798at2759; -.
DR PhylomeDB; P00325; -.
DR TreeFam; TF300429; -.
DR BioCyc; MetaCyc:MON66-321; -.
DR PathwayCommons; P00325; -.
DR Reactome; R-HSA-71384; Ethanol oxidation.
DR SABIO-RK; P00325; -.
DR SignaLink; P00325; -.
DR BioGRID-ORCS; 125; 4 hits in 1033 CRISPR screens.
DR ChiTaRS; ADH1B; human.
DR EvolutionaryTrace; P00325; -.
DR GeneWiki; ADH1B; -.
DR GenomeRNAi; 125; -.
DR Pharos; P00325; Tclin.
DR PRO; PR:P00325; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P00325; protein.
DR Bgee; ENSG00000196616; Expressed in right lobe of liver and 170 other tissues.
DR ExpressionAtlas; P00325; baseline and differential.
DR Genevisible; P00325; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IDA:UniProtKB.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006069; P:ethanol oxidation; 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 InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Lipid metabolism; Metal-binding; NAD;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6391920"
FT CHAIN 2..375
FT /note="All-trans-retinol dehydrogenase [NAD(+)] ADH1B"
FT /id="PRO_0000160661"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 200..205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 293..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:6391920"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 35
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054847"
FT VARIANT 48
FT /note="H -> R (in dbSNP:rs1229984)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2935533,
FT ECO:0000269|PubMed:2986130, ECO:0000269|PubMed:3000832,
FT ECO:0000269|Ref.10, ECO:0000269|Ref.16, ECO:0000269|Ref.6"
FT /id="VAR_000426"
FT VARIANT 57
FT /note="N -> K (in dbSNP:rs1041969)"
FT /evidence="ECO:0000269|PubMed:2679216,
FT ECO:0000269|PubMed:3397059"
FT /id="VAR_019322"
FT VARIANT 60
FT /note="T -> S (in dbSNP:rs6413413)"
FT /evidence="ECO:0000269|Ref.10"
FT /id="VAR_019323"
FT VARIANT 370
FT /note="R -> C (in beta-3/Indianapolis; allele ADH1B*3;
FT decreased NAD(H) binding; dbSNP:rs2066702)"
FT /evidence="ECO:0000269|PubMed:2679216,
FT ECO:0000269|PubMed:3619918, ECO:0000269|Ref.10"
FT /id="VAR_000427"
FT CONFLICT 8
FT /note="I -> M (in Ref. 15; AAA51592)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="Missing (in Ref. 14; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="P -> K (in Ref. 15; AAA51592)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="V -> VV (in Ref. 8; CAA33487)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="I -> V (in Ref. 11; BAG62635)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="F -> K (in Ref. 1; AAA51884)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="E -> V (in Ref. 15; AAA51592)"
FT /evidence="ECO:0000305"
FT CONFLICT 338..344
FT /note="Missing (in Ref. 11; BAG62635)"
FT /evidence="ECO:0000305"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1HDY"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1U3U"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:1U3U"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:1U3U"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:1U3U"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 325..337
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1U3U"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:1U3U"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:1U3U"
SQ SEQUENCE 375 AA; 39835 MW; 2C5104F834950B1A CRC64;
MSTAGKVIKC KAAVLWEVKK PFSIEDVEVA PPKAYEVRIK MVAVGICHTD DHVVSGNLVT
PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRVCKNPESN YCLKNDLGNP
RGTLQDGTRR FTCRGKPIHH FLGTSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG
YGSAVNVAKV TPGSTCAVFG LGGVGLSAVM GCKAAGAARI IAVDINKDKF AKAKELGATE
CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPASQ
NLSINPMLLL TGRTWKGAVY GGFKSKEGIP KLVADFMAKK FSLDALITHV LPFEKINEGF
DLLHSGKSIR TVLTF
