ADH7_HUMAN
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 03-AUG-2022, entry version 195.
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};
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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. [P40394-1]
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; 11.
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; P40394; -.
DR PeptideAtlas; P40394; -.
DR PRIDE; P40394; -.
DR ProteomicsDB; 55365; -. [P40394-1]
DR ProteomicsDB; 55366; -. [P40394-2]
DR Antibodypedia; 25891; 369 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 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; 664798at2759; -.
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 1072 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 109 other tissues.
DR ExpressionAtlas; P40394; baseline and differential.
DR Genevisible; P40394; HS.
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 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; IPR028635; Zinc_ADH_IV.
DR PANTHER; PTHR43880:SF2; PTHR43880:SF2; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 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; 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
