ID AOXA_HUMAN Reviewed; 1338 AA. AC Q06278; O14765; Q53RR8; Q53TV3; Q9BYF0; Q9UPG6; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 27-MAR-2024, entry version 215. DE RecName: Full=Aldehyde oxidase {ECO:0000312|HGNC:HGNC:553}; DE EC=1.2.3.1 {ECO:0000269|PubMed:22996261, ECO:0000269|PubMed:26322824}; DE AltName: Full=Aldehyde oxidase 1; DE AltName: Full=Azaheterocycle hydroxylase {ECO:0000305|PubMed:7786031, ECO:0000305|PubMed:9224775}; DE EC=1.17.3.- {ECO:0000269|PubMed:7786031, ECO:0000269|PubMed:9224775}; GN Name=AOX1 {ECO:0000312|HGNC:HGNC:553}; Synonyms=AO; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=8248161; DOI=10.1073/pnas.90.22.10690; RA Wright R.M., Vaitaitis G.M., Wilson C.M., Repine T.B., Terada L.S., RA Repine J.E.; RT "cDNA cloning, characterization, and tissue-specific expression of human RT xanthine dehydrogenase/xanthine oxidase."; RL Proc. Natl. Acad. Sci. U.S.A. 90:10690-10694(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Wright R.M., Weigel L.K., Varella-Garcia M., Vaitaitis G., Repine J.E.; RT "Molecular cloning, refined chromosomal mapping, and structural analysis of RT the human gene encoding aldehyde oxidase (AOX1), a candidate for the ALS2 RT gene."; RL Redox Rep. 3:135-144(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=11302742; DOI=10.1006/bbrc.2001.4719; RA Ichida K., Matsumura T., Sakuma R., Hosoya T., Nishino T.; RT "Mutation of human molybdenum cofactor sulfurase gene is responsible to RT classical xanthinuria type II."; RL Biochem. Biophys. Res. Commun. 282:1194-1200(2001). RN [4] 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; 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 [7] RP FUNCTION AS AZAHETEROCYCLE OXIDASE, AND SUBSTRATE SPECIFICITY. RX PubMed=7786031; DOI=10.1006/abbi.1995.1320; RA Beedham C., Critchley D.J., Rance D.J.; RT "Substrate specificity of human liver aldehyde oxidase toward substituted RT quinazolines and phthalazines: a comparison with hepatic enzyme from guinea RT pig, rabbit, and baboon."; RL Arch. Biochem. Biophys. 319:481-490(1995). RN [8] RP FUNCTION AS AZAHETEROCYCLE OXIDASE, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=9224775; RA Rashidi M.R., Smith J.A., Clarke S.E., Beedham C.; RT "In vitro oxidation of famciclovir and 6-deoxypenciclovir by aldehyde RT oxidase from human, guinea pig, rabbit, and rat liver."; RL Drug Metab. Dispos. 25:805-813(1997). RN [9] RP INDUCTION. RX PubMed=17022944; DOI=10.1016/j.bbrc.2006.09.101; RA Neumeier M., Weigert J., Schaeffler A., Weiss T.S., Schmidl C., RA Buettner R., Bollheimer C., Aslanidis C., Schoelmerich J., Buechler C.; RT "Aldehyde oxidase 1 is highly abundant in hepatic steatosis and is down- RT regulated by adiponectin and fenofibric acid in hepatocytes in vitro."; RL Biochem. Biophys. Res. Commun. 350:731-735(2006). RN [10] RP REVIEW, NOMENCLATURE, AND TISSUE SPECIFICITY. RX PubMed=18066686; DOI=10.1007/s00018-007-7398-y; RA Garattini E., Fratelli M., Terao M.; RT "Mammalian aldehyde oxidases: genetics, evolution and biochemistry."; RL Cell. Mol. Life Sci. 65:1019-1048(2008). RN [11] RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION. RX PubMed=18671973; DOI=10.1016/j.febslet.2008.07.034; RA Weigert J., Neumeier M., Bauer S., Mages W., Schnitzbauer A.A., Obed A., RA Groeschl B., Hartmann A., Schaeffler A., Aslanidis C., Schoelmerich J., RA Buechler C.; RT "Small-interference RNA-mediated knock-down of aldehyde oxidase 1 in 3T3-L1 RT cells impairs adipogenesis and adiponectin release."; RL FEBS Lett. 582:2965-2972(2008). RN [12] RP FUNCTION AS DRUG-METABOLIZING ENZYME, SUBSTRATE SPECIFICITY, TISSUE RP SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=20444863; DOI=10.1124/dmd.110.033555; RA Zientek M., Jiang Y., Youdim K., Obach R.S.; RT "In vitro-in vivo correlation for intrinsic clearance for drugs metabolized RT by human aldehyde oxidase."; RL Drug Metab. Dispos. 38:1322-1327(2010). RN [13] RP FUNCTION AS DRUG-METABOLIZING ENZYME, ACTIVITY REGULATION, SUBSTRATE RP SPECIFICITY, AND TISSUE SPECIFICITY. RX PubMed=22031625; DOI=10.1124/dmd.111.042861; RA Hutzler J.M., Yang Y.S., Albaugh D., Fullenwider C.L., Schmenk J., RA Fisher M.B.; RT "Characterization of aldehyde oxidase enzyme activity in cryopreserved RT human hepatocytes."; RL Drug Metab. Dispos. 40:267-275(2012). RN [14] RP FUNCTION AS DRUG-METABOLIZING ENZYME, ACTIVITY REGULATION, SUBSTRATE RP SPECIFICITY, AND TISSUE SPECIFICITY. RX PubMed=22522748; DOI=10.1124/dmd.112.045195; RA Strelevitz T.J., Orozco C.C., Obach R.S.; RT "Hydralazine as a selective probe inactivator of aldehyde oxidase in human RT hepatocytes: estimation of the contribution of aldehyde oxidase to RT metabolic clearance."; RL Drug Metab. Dispos. 40:1441-1448(2012). RN [15] RP REVIEW. RX PubMed=22335465; DOI=10.1517/17425255.2012.663352; RA Garattini E., Terao M.; RT "The role of aldehyde oxidase in drug metabolism."; RL Expert Opin. Drug Metab. Toxicol. 8:487-503(2012). RN [16] RP FUNCTION AS AZAHETEROCYCLE OXIDASE, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=22996261; DOI=10.1124/dmd.112.048546; RA Barr J.T., Jones J.P.; RT "Evidence for substrate-dependent inhibition profiles for human liver RT aldehyde oxidase."; RL Drug Metab. Dispos. 41:24-29(2013). RN [17] RP FUNCTION AS DRUG-METABOLIZING ENZYME, SUBSTRATE SPECIFICITY, TISSUE RP SPECIFICITY, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=23857892; DOI=10.1124/dmd.113.053082; RA Fu C., Di L., Han X., Soderstrom C., Snyder M., Troutman M.D., Obach R.S., RA Zhang H.; RT "Aldehyde oxidase 1 (AOX1) in human liver cytosols: quantitative RT characterization of AOX1 expression level and activity relationship."; RL Drug Metab. Dispos. 41:1797-1804(2013). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1068, AND IDENTIFICATION BY RP 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 [19] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH FAD; IRON-SULFUR RP (2FE-2S); MOLYBDOPTERIN; AN INHIBITOR AND SUBSTRATE, SUBUNIT, CATALYTIC RP ACTIVITY, ACTIVITY REGULATION, FUNCTION, AND COFACTOR. RX PubMed=26322824; DOI=10.1038/nchembio.1895; RA Coelho C., Foti A., Hartmann T., Santos-Silva T., Leimkuhler S., RA Romao M.J.; RT "Structural insights into xenobiotic and inhibitor binding to human RT aldehyde oxidase."; RL Nat. Chem. Biol. 11:779-783(2015). RN [20] RP X-RAY CRYSTALLOGRAPHY (3.39 ANGSTROMS) OF VARIANT LEU-1271 IN COMPLEX WITH RP FAD; IRON-SULFUR (2FE-2S) AND MOLYBDOPTERIN, CHARACTERIZATION OF VARIANT RP LEU-1271, FUNCTION, SUBUNIT, COFACTOR, MUTAGENESIS OF CYS-44 AND GLY-1269, RP AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=26842593; DOI=10.1124/dmd.115.068395; RA Foti A., Hartmann T., Coelho C., Santos-Silva T., Romao M.J., RA Leimkuhler S.; RT "Optimization of the Expression of Human Aldehyde Oxidase for RT Investigations of Single-Nucleotide Polymorphisms."; RL Drug Metab. Dispos. 44:1277-1285(2016). RN [21] RP VARIANTS CYS-802; HIS-921; SER-1135; LEU-1271 AND ARG-1297, RP CHARACTERIZATION OF VARIANTS CYS-802; HIS-921; SER-1135 AND ARG-1297, RP FUNCTION AS OXIDASE, HOMODIMER, COFACTOR, SUBSTRATE SPECIFICITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=22279051; DOI=10.1124/dmd.111.043828; RA Hartmann T., Terao M., Garattini E., Teutloff C., Alfaro J.F., Jones J.P., RA Leimkuehler S.; RT "The impact of single nucleotide polymorphisms on human aldehyde oxidase."; RL Drug Metab. Dispos. 40:856-864(2012). CC -!- FUNCTION: Oxidase with broad substrate specificity, oxidizing aromatic CC azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium CC and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, CC pyridoxal, and vanillin. Plays a key role in the metabolism of CC xenobiotics and drugs containing aromatic azaheterocyclic substituents. CC Participates in the bioactivation of prodrugs such as famciclovir, CC catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, CC which is a potent antiviral agent. Is probably involved in the CC regulation of reactive oxygen species homeostasis. May be a prominent CC source of superoxide generation via the one-electron reduction of CC molecular oxygen. May also catalyze nitric oxide (NO) production via CC the reduction of nitrite to NO with NADH or aldehyde as electron donor. CC May play a role in adipogenesis. {ECO:0000269|PubMed:20444863, CC ECO:0000269|PubMed:22031625, ECO:0000269|PubMed:22279051, CC ECO:0000269|PubMed:22522748, ECO:0000269|PubMed:22996261, CC ECO:0000269|PubMed:23857892, ECO:0000269|PubMed:26322824, CC ECO:0000269|PubMed:7786031, ECO:0000269|PubMed:9224775}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2; CC Xref=Rhea:RHEA:16829, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, CC ChEBI:CHEBI:29067; EC=1.2.3.1; Evidence={ECO:0000269|PubMed:22996261, CC ECO:0000269|PubMed:26322824}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O2 + retinal = H(+) + H2O2 + retinoate; CC Xref=Rhea:RHEA:56736, ChEBI:CHEBI:15035, ChEBI:CHEBI:15036, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240; Evidence={ECO:0000250|UniProtKB:O54754}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000269|PubMed:22279051, ECO:0000269|PubMed:26322824, CC ECO:0000269|PubMed:26842593}; CC Note=Binds 2 [2Fe-2S] clusters per subunit. CC {ECO:0000269|PubMed:22279051, ECO:0000269|PubMed:26322824}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:22279051, ECO:0000269|PubMed:26322824}; CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:22279051, CC ECO:0000269|PubMed:26322824}; CC -!- COFACTOR: CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; CC Evidence={ECO:0000269|PubMed:22279051, ECO:0000269|PubMed:26322824, CC ECO:0000269|PubMed:26842593}; CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. CC {ECO:0000269|PubMed:22279051, ECO:0000269|PubMed:26322824}; CC -!- ACTIVITY REGULATION: Is very potently inhibited by raloxifene CC (PubMed:26842593). Also inhibited by estradiol, ethinyl estradiol, CC hydralazine, menadione, isovanillin and thioridazine. Not inhibited by CC allopurinol, a xanthine dehydrogenase potent inhibitor CC (PubMed:22031625, PubMed:22522748, PubMed:22996261, PubMed:9224775, CC PubMed:26322824). {ECO:0000269|PubMed:22031625, CC ECO:0000269|PubMed:22522748, ECO:0000269|PubMed:22996261, CC ECO:0000269|PubMed:26322824, ECO:0000269|PubMed:26842593, CC ECO:0000269|PubMed:9224775}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=4.6 uM for benzaldehyde (in the presence of 2,6-dichlorophenol CC indophenol as electron acceptor) {ECO:0000269|PubMed:26842593}; CC KM=45.18 uM for benzaldehyde (in the presence of ferricyanide as CC electron acceptor) {ECO:0000269|PubMed:26842593}; CC KM=1.3 uM for phthalazine (at 25 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:22279051}; CC KM=8.96 uM for phthalazine (in the presence of 2,6-dichlorophenol CC indophenol as electron acceptor) {ECO:0000269|PubMed:26842593}; CC KM=125.7 uM for phthalazine (in the presence of ferricyanide as CC electron acceptor) {ECO:0000269|PubMed:26842593}; CC KM=0.78 uM for phenanthridine (in the pres 2,6-dichlorophenol CC indophenol as electron acceptor) {ECO:0000269|PubMed:26842593}; CC KM=25.5 uM for phenanthridine (in the presence of ferricyanide as CC electron acceptor) {ECO:0000269|PubMed:26842593}; CC KM=26.53 uM for phenanthridine (in the presence of molecular oxygen CC as electron acceptor) {ECO:0000269|PubMed:26842593}; CC KM=3.9 uM for phenanthridine (at 25 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:22279051}; CC KM=5.2 uM for chloroquinazolinone (at 25 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:22279051}; CC KM=0.42 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH 7) CC {ECO:0000269|PubMed:9224775}; CC KM=0.15 mM for famciclovir (at 37 degrees Celsius and pH 7) CC {ECO:0000269|PubMed:9224775}; CC KM=6.3 uM for N-[(2-dimethylamino)ethyl]acridine-4-carboxamide (at 37 CC degrees Celsius and pH 7.4) {ECO:0000269|PubMed:22996261}; CC Vmax=16 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate CC {ECO:0000269|PubMed:9224775}; CC Vmax=61 nmol/min/mg enzyme with famciclovir as substrate CC {ECO:0000269|PubMed:9224775}; CC Vmax=2.3 nmol/min/mg enzyme with CC N-[(2-dimethylamino)ethyl]acridine-4-carboxamide as substrate CC {ECO:0000269|PubMed:22996261}; CC Note=kcat is 6.4 min(-1) for benzaldehyde oxidation, 5.6 min(-1) for CC phthalazine oxidation, 12.2 min(-1) for phenanthridine oxidation and CC 5.6 min(-1) for chloroquinazolinone oxidation. CC {ECO:0000269|PubMed:22279051}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26322824, CC ECO:0000269|PubMed:26842593}. CC -!- INTERACTION: CC Q06278; Q06278: AOX1; NbExp=2; IntAct=EBI-3926368, EBI-3926368; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18671973, CC ECO:0000269|PubMed:20444863, ECO:0000269|PubMed:23857892}. CC -!- TISSUE SPECIFICITY: Abundant in liver, expressed in adipose tissue and CC at lower levels in lung, skeletal muscle, pancreas. In contrast to CC mice, no significant gender difference in AOX1 expression level (at CC protein level). {ECO:0000269|PubMed:18066686, CC ECO:0000269|PubMed:18671973, ECO:0000269|PubMed:20444863, CC ECO:0000269|PubMed:22031625, ECO:0000269|PubMed:22522748, CC ECO:0000269|PubMed:23857892, ECO:0000269|PubMed:8248161}. CC -!- DEVELOPMENTAL STAGE: Not detected in preadipocytes but strongly induced CC in mature adipocytes. {ECO:0000269|PubMed:18671973}. CC -!- INDUCTION: In liver, is down-regulated by adiponectin and by the PPARA CC agonist, fenofibric acid. {ECO:0000269|PubMed:17022944}. CC -!- MISCELLANEOUS: AOX genes evolved from a xanthine oxidoreductase CC ancestral precursor via a series of gene duplication and CC suppression/deletion events. Different animal species contain a CC different complement of AOX genes encoding an equivalent number of AOX CC isoenzymes. In mammals, the two extremes are represented by certain CC rodents such as mice and rats, which are endowed with 4 AOX genes, and CC by humans, whose genome is characterized by a single active gene CC (PubMed:22335465). {ECO:0000305|PubMed:22335465}. CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family. CC {ECO:0000305}. CC -!- CAUTION: Was originally thought to be a xanthine dehydrogenase. CC {ECO:0000305|PubMed:8248161}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA96650.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAB83966.1; Type=Frameshift; 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; L11005; AAA96650.1; ALT_FRAME; mRNA. DR EMBL; AF017060; AAB83966.1; ALT_FRAME; Genomic_DNA. DR EMBL; AF009441; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009442; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009443; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009444; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009445; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009446; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009447; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009448; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009449; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009450; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009451; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009452; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009453; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009454; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009455; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009456; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009457; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009458; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009459; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009460; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009461; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009462; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009463; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009464; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009465; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009466; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009467; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009468; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009469; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009470; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009471; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009472; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009473; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF009474; AAB83966.1; JOINED; Genomic_DNA. DR EMBL; AF010260; AAB83968.1; -; Genomic_DNA. DR EMBL; AB046692; BAB40305.1; -; mRNA. DR EMBL; AC007163; AAX93285.1; -; Genomic_DNA. DR EMBL; AC080164; AAY24265.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70209.1; -; Genomic_DNA. DR EMBL; BC117179; AAI17180.1; -; mRNA. DR EMBL; BC117181; AAI17182.1; -; mRNA. DR CCDS; CCDS33360.1; -. DR PIR; A49634; A49634. DR RefSeq; NP_001150.3; NM_001159.3. DR PDB; 4UHW; X-ray; 2.60 A; A=1-1338. DR PDB; 4UHX; X-ray; 2.70 A; A=1-1338. DR PDB; 5EPG; X-ray; 3.39 A; A=1-1338. DR PDB; 6Q6Q; X-ray; 3.10 A; A=1-1338. DR PDB; 7OPN; X-ray; 2.60 A; A/B=1-1338. DR PDB; 7ORC; X-ray; 2.70 A; A/B=1-1338. DR PDB; 8EMT; EM; 2.92 A; A/B=1-1338. DR PDBsum; 4UHW; -. DR PDBsum; 4UHX; -. DR PDBsum; 5EPG; -. DR PDBsum; 6Q6Q; -. DR PDBsum; 7OPN; -. DR PDBsum; 7ORC; -. DR PDBsum; 8EMT; -. DR AlphaFoldDB; Q06278; -. DR EMDB; EMD-28264; -. DR SMR; Q06278; -. DR BioGRID; 106813; 11. DR DIP; DIP-61698N; -. DR IntAct; Q06278; 5. DR STRING; 9606.ENSP00000363832; -. DR BindingDB; Q06278; -. DR ChEMBL; CHEMBL3257; -. DR DrugBank; DB00437; Allopurinol. DR DrugBank; DB00513; Aminocaproic acid. DR DrugBank; DB00484; Brimonidine. DR DrugBank; DB11791; Capmatinib. DR DrugBank; DB00924; Cyclobenzaprine. DR DrugBank; DB03516; Eniluracil. DR DrugBank; DB00426; Famciclovir. DR DrugBank; DB12466; Favipiravir. DR DrugBank; DB09054; Idelalisib. DR DrugBank; DB09078; Lenvatinib. DR DrugBank; DB00170; Menadione. DR DrugBank; DB01033; Mercaptopurine. DR DrugBank; DB00563; Methotrexate. DR DrugBank; DB08840; N-methylnicotinamide. DR DrugBank; DB00157; NADH. DR DrugBank; DB00339; Pyrazinamide. DR DrugBank; DB00481; Raloxifene. DR DrugBank; DB04827; Urethane. DR DrugBank; DB00962; Zaleplon. DR DrugBank; DB00246; Ziprasidone. DR DrugBank; DB00909; Zonisamide. DR DrugCentral; Q06278; -. DR GuidetoPHARMACOLOGY; 3186; -. DR iPTMnet; Q06278; -. DR PhosphoSitePlus; Q06278; -. DR BioMuta; AOX1; -. DR DMDM; 215273968; -. DR EPD; Q06278; -. DR jPOST; Q06278; -. DR MassIVE; Q06278; -. DR MaxQB; Q06278; -. DR PaxDb; 9606-ENSP00000363832; -. DR PeptideAtlas; Q06278; -. DR ProteomicsDB; 58430; -. DR Antibodypedia; 34105; 267 antibodies from 28 providers. DR DNASU; 316; -. DR Ensembl; ENST00000374700.7; ENSP00000363832.2; ENSG00000138356.14. DR GeneID; 316; -. DR KEGG; hsa:316; -. DR MANE-Select; ENST00000374700.7; ENSP00000363832.2; NM_001159.4; NP_001150.3. DR UCSC; uc002uvx.4; human. DR AGR; HGNC:553; -. DR CTD; 316; -. DR DisGeNET; 316; -. DR GeneCards; AOX1; -. DR HGNC; HGNC:553; AOX1. DR HPA; ENSG00000138356; Group enriched (adrenal gland, liver). DR MIM; 602841; gene. DR neXtProt; NX_Q06278; -. DR OpenTargets; ENSG00000138356; -. DR PharmGKB; PA24842; -. DR VEuPathDB; HostDB:ENSG00000138356; -. DR eggNOG; KOG0430; Eukaryota. DR GeneTree; ENSGT00950000183114; -. DR HOGENOM; CLU_001681_1_2_1; -. DR InParanoid; Q06278; -. DR OMA; QCRWKVG; -. DR OrthoDB; 5485853at2759; -. DR PhylomeDB; Q06278; -. DR TreeFam; TF353036; -. DR BioCyc; MetaCyc:ENSG00000138356-MONOMER; -. DR BRENDA; 1.2.3.1; 2681. DR PathwayCommons; Q06278; -. DR Reactome; R-HSA-964975; Vitamin B6 activation to pyridoxal phosphate. DR SABIO-RK; Q06278; -. DR SignaLink; Q06278; -. DR BioGRID-ORCS; 316; 14 hits in 1150 CRISPR screens. DR ChiTaRS; AOX1; human. DR GeneWiki; Aldehyde_oxidase_1; -. DR GenomeRNAi; 316; -. DR Pharos; Q06278; Tchem. DR PRO; PR:Q06278; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q06278; Protein. DR Bgee; ENSG00000138356; Expressed in right adrenal gland cortex and 162 other cell types or tissues. DR ExpressionAtlas; Q06278; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB. DR GO; GO:0004031; F:aldehyde oxidase activity; IDA:UniProtKB. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB. DR GO; GO:0043546; F:molybdopterin cofactor binding; IDA:UniProtKB. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1. DR Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1. DR Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4. DR Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1. DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1. DR InterPro; IPR002888; 2Fe-2S-bd. DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf. DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b. DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf. DR InterPro; IPR016208; Ald_Oxase/xanthine_DH-like. DR InterPro; IPR014313; Aldehyde_oxidase. DR InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1. DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2. DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf. DR InterPro; IPR012675; Beta-grasp_dom_sf. DR InterPro; IPR005107; CO_DH_flav_C. DR InterPro; IPR036683; CO_DH_flav_C_dom_sf. DR InterPro; IPR016166; FAD-bd_PCMH. DR InterPro; IPR036318; FAD-bd_PCMH-like_sf. DR InterPro; IPR016167; FAD-bd_PCMH_sub1. DR InterPro; IPR016169; FAD-bd_PCMH_sub2. DR InterPro; IPR002346; Mopterin_DH_FAD-bd. DR InterPro; IPR022407; OxRdtase_Mopterin_BS. DR NCBIfam; TIGR02969; mam_aldehyde_ox; 1. DR PANTHER; PTHR11908:SF86; ALDEHYDE OXIDASE; 1. DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1. DR Pfam; PF01315; Ald_Xan_dh_C; 1. DR Pfam; PF03450; CO_deh_flav_C; 1. DR Pfam; PF00941; FAD_binding_5; 1. DR Pfam; PF00111; Fer2; 1. DR Pfam; PF01799; Fer2_2; 1. DR Pfam; PF02738; MoCoBD_1; 1. DR Pfam; PF20256; MoCoBD_2; 1. DR PIRSF; PIRSF000127; Xanthine_DH; 1. DR SMART; SM01008; Ald_Xan_dh_C; 1. DR SMART; SM01092; CO_deh_flav_C; 1. DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1. DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1. DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1. DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1. DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51387; FAD_PCMH; 1. DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1. DR Genevisible; Q06278; HS. PE 1: Evidence at protein level; KW 2Fe-2S; 3D-structure; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur; KW Lipid metabolism; Metal-binding; Molybdenum; Oxidoreductase; KW Phosphoprotein; Reference proteome. FT CHAIN 1..1338 FT /note="Aldehyde oxidase" FT /id="PRO_0000166104" FT DOMAIN 5..92 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT DOMAIN 236..421 FT /note="FAD-binding PCMH-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718" FT ACT_SITE 1270 FT /note="Proton acceptor; for azaheterocycle hydroxylase FT activity" FT /evidence="ECO:0000250|UniProtKB:O54754" FT BINDING 44 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0007744|PDB:4UHW" FT BINDING 49 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 52 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 74 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 113 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0007744|PDB:4UHW, ECO:0007744|PDB:4UHX" FT BINDING 114 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 117 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 149 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 151 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 151 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 264..271 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 345 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0007744|PDB:4UHW, ECO:0007744|PDB:4UHX" FT BINDING 354 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 358 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:5EPG" FT BINDING 367 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 411 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 806..807 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 1047 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 1088..1091 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 1203 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0000269|PubMed:26842593, ECO:0007744|PDB:4UHW, FT ECO:0007744|PDB:4UHX, ECO:0007744|PDB:5EPG" FT BINDING 1268 FT /ligand="Mo-molybdopterin" FT /ligand_id="ChEBI:CHEBI:71302" FT /evidence="ECO:0000269|PubMed:26322824, FT ECO:0007744|PDB:4UHX" FT MOD_RES 1068 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VARIANT 314 FT /note="Q -> R (in dbSNP:rs58185012)" FT /id="VAR_061136" FT VARIANT 802 FT /note="R -> C (decreases homodimerization but nearly no FT effect on kinetic parameters; dbSNP:rs41309768)" FT /evidence="ECO:0000269|PubMed:22279051" FT /id="VAR_047517" FT VARIANT 921 FT /note="R -> H (increases homodimerization; abolishes FT enzymatic activity on phenanthridine; decreases turnover FT number with benzaldehyde, phtalazine and FT chloroquinazolinone as substrate, while nearly no effect on FT the KM; dbSNP:rs56199635)" FT /evidence="ECO:0000269|PubMed:22279051" FT /id="VAR_070256" FT VARIANT 1135 FT /note="N -> S (increases homodimerization and turnover FT number with phenanthridine as substrate; nearly no effect FT on kinetic parameters with benzaldehyde, phtalazine and FT chloroquinazolinone as substrate; dbSNP:rs55754655)" FT /evidence="ECO:0000269|PubMed:22279051" FT /id="VAR_070257" FT VARIANT 1271 FT /note="S -> L (no effect on dimerization; no effect on FT oxidase activity; dbSNP:rs141786030)" FT /evidence="ECO:0000269|PubMed:22279051, FT ECO:0000269|PubMed:26842593" FT /id="VAR_070258" FT VARIANT 1297 FT /note="H -> R (increases homodimerization and turnover FT number with phenanthridine as substrate; nearly no effect FT on kinetic parameters with benzaldehyde, phtalazine and FT chloroquinazolinone as substrate; dbSNP:rs3731722)" FT /evidence="ECO:0000269|PubMed:22279051" FT /id="VAR_047518" FT MUTAGEN 44 FT /note="C->W: Disrupts protein stability." FT /evidence="ECO:0000269|PubMed:26842593" FT MUTAGEN 1269 FT /note="G->R: No effect on dimerization. Loss of oxidase FT activity." FT /evidence="ECO:0000269|PubMed:26842593" FT CONFLICT 41 FT /note="K -> P (in Ref. 1; AAA96650 and 2; AAB83966)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="T -> P (in Ref. 1; AAA96650 and 2; AAB83966)" FT /evidence="ECO:0000305" FT CONFLICT 152 FT /note="T -> H (in Ref. 1; AAA96650 and 2; AAB83966)" FT /evidence="ECO:0000305" FT CONFLICT 227 FT /note="E -> D (in Ref. 1; AAA96650 and 2; AAB83966)" FT /evidence="ECO:0000305" FT CONFLICT 251 FT /note="E -> D (in Ref. 1; AAA96650)" FT /evidence="ECO:0000305" FT CONFLICT 418 FT /note="Y -> I (in Ref. 1; AAA96650 and 2; AAB83966)" FT /evidence="ECO:0000305" FT CONFLICT 501 FT /note="V -> L (in Ref. 2; AAB83966)" FT /evidence="ECO:0000305" FT CONFLICT 627 FT /note="I -> N (in Ref. 2; AAB83966)" FT /evidence="ECO:0000305" FT CONFLICT 929 FT /note="A -> V (in Ref. 1; AAA96650 and 2; AAB83966)" FT /evidence="ECO:0000305" FT CONFLICT 1019 FT /note="G -> A (in Ref. 1; AAA96650 and 2; AAB83966)" FT /evidence="ECO:0000305" FT STRAND 6..11 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 14..20 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 27..33 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 45..49 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 53..60 FT /evidence="ECO:0007829|PDB:4UHW" FT TURN 61..64 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 65..72 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 73..75 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 78..81 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 89..92 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:4UHX" FT HELIX 101..108 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 113..117 FT /evidence="ECO:0007829|PDB:8EMT" FT HELIX 118..131 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 137..143 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 155..162 FT /evidence="ECO:0007829|PDB:4UHW" FT TURN 163..165 FT /evidence="ECO:0007829|PDB:7OPN" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 212..214 FT /evidence="ECO:0007829|PDB:4UHX" FT HELIX 220..226 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 234..237 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 242..245 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 249..258 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 271..277 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 292..295 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 297..299 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 301..307 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 312..325 FT /evidence="ECO:0007829|PDB:4UHW" FT TURN 328..330 FT /evidence="ECO:0007829|PDB:7OPN" FT HELIX 332..343 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 347..352 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 355..361 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 369..374 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 378..382 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 387..391 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 394..397 FT /evidence="ECO:0007829|PDB:4UHW" FT TURN 401..403 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 410..417 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 423..430 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 432..437 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 440..448 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 451..453 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 458..469 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 474..480 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 484..486 FT /evidence="ECO:0007829|PDB:7OPN" FT HELIX 487..498 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 512..537 FT /evidence="ECO:0007829|PDB:4UHW" FT TURN 539..541 FT /evidence="ECO:0007829|PDB:4UHW" FT TURN 547..549 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 550..552 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 562..566 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 572..574 FT /evidence="ECO:0007829|PDB:4UHX" FT HELIX 589..593 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 600..602 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 610..616 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 620..628 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 630..633 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 638..642 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 644..646 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 648..650 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 651..663 FT /evidence="ECO:0007829|PDB:7OPN" FT STRAND 666..668 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 674..682 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 683..690 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 694..699 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 709..711 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 721..726 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 728..731 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 732..734 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 736..745 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 756..762 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 769..773 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 778..789 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 793..795 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 796..801 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 812..828 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 832..835 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 838..844 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 851..859 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 865..878 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 884..893 FT /evidence="ECO:0007829|PDB:4UHW" FT TURN 894..897 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 901..911 FT /evidence="ECO:0007829|PDB:4UHW" FT TURN 921..924 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 925..943 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 947..954 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 958..961 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 967..969 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 971..984 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 986..999 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1001..1016 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1019..1021 FT /evidence="ECO:0007829|PDB:7OPN" FT HELIX 1022..1024 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1026..1032 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1034..1036 FT /evidence="ECO:0007829|PDB:8EMT" FT STRAND 1038..1043 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1047..1049 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 1051..1062 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 1067..1069 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1070..1072 FT /evidence="ECO:0007829|PDB:8EMT" FT TURN 1077..1079 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1088..1090 FT /evidence="ECO:0007829|PDB:6Q6Q" FT HELIX 1091..1115 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1118..1120 FT /evidence="ECO:0007829|PDB:6Q6Q" FT HELIX 1122..1131 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1137..1142 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1148..1150 FT /evidence="ECO:0007829|PDB:4UHW" FT TURN 1151..1154 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1155..1157 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1160..1174 FT /evidence="ECO:0007829|PDB:4UHW" FT TURN 1175..1177 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1180..1190 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 1197..1215 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 1232..1234 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 1241..1243 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1246..1252 FT /evidence="ECO:0007829|PDB:4UHW" FT STRAND 1259..1261 FT /evidence="ECO:0007829|PDB:8EMT" FT HELIX 1262..1264 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 1271..1276 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 1277..1293 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 1308..1314 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 1318..1322 FT /evidence="ECO:0007829|PDB:4UHW" FT HELIX 1328..1330 FT /evidence="ECO:0007829|PDB:4UHW" SQ SEQUENCE 1338 AA; 147918 MW; 2AB5E543F18C9261 CRC64; MDRASELLFY VNGRKVIEKN VDPETMLLPY LRKKLRLTGT KYGCGGGGCG ACTVMISRYN PITKRIRHHP ANACLIPICS LYGAAVTTVE GIGSTHTRIH PVQERIAKCH GTQCGFCTPG MVMSIYTLLR NHPEPTLDQL TDALGGNLCR CTGYRPIIDA CKTFCKTSGC CQSKENGVCC LDQGINGLPE FEEGSKTSPK LFAEEEFLPL DPTQELIFPP ELMIMAEKQS QRTRVFGSER MMWFSPVTLK ELLEFKFKYP QAPVIMGNTS VGPEVKFKGV FHPVIISPDR IEELSVVNHA YNGLTLGAGL SLAQVKDILA DVVQKLPEEK TQMYHALLKH LGTLAGSQIR NMASLGGHII SRHPDSDLNP ILAVGNCTLN LLSKEGKRQI PLNEQFLSKC PNADLKPQEI LVSVNIPYSR KWEFVSAFRQ AQRQENALAI VNSGMRVFFG EGDGIIRELC ISYGGVGPAT ICAKNSCQKL IGRHWNEQML DIACRLILNE VSLLGSAPGG KVEFKRTLII SFLFKFYLEV SQILKKMDPV HYPSLADKYE SALEDLHSKH HCSTLKYQNI GPKQHPEDPI GHPIMHLSGV KHATGEAIYC DDMPLVDQEL FLTFVTSSRA HAKIVSIDLS EALSMPGVVD IMTAEHLSDV NSFCFFTEAE KFLATDKVFC VGQLVCAVLA DSEVQAKRAA KRVKIVYQDL EPLILTIEES IQHNSSFKPE RKLEYGNVDE AFKVVDQILE GEIHMGGQEH FYMETQSMLV VPKGEDQEMD VYVSTQFPKY IQDIVASTLK LPANKVMCHV RRVGGAFGGK VLKTGIIAAV TAFAANKHGR AVRCVLERGE DMLITGGRHP YLGKYKAGFM NDGRILALDM EHYSNAGASL DESLFVIEMG LLKMDNAYKF PNLRCRGWAC RTNLPSNTAF RGFGFPQAAL ITESCITEVA AKCGLSPEKV RIINMYKEID QTPYKQEINA KNLIQCWREC MAMSSYSLRK VAVEKFNAEN YWKKKGLAMV PLKFPVGLGS RAAGQAAALV HIYLDGSVLV THGGIEMGQG VHTKMIQVVS RELRMPMSNV HLRGTSTETV PNANISGGSV VADLNGLAVK DACQTLLKRL EPIISKNPKG TWKDWAQTAF DESINLSAVG YFRGYESDMN WEKGEGQPFE YFVYGAACSE VEIDCLTGDH KNIRTDIVMD VGCSINPAID IGQIEGAFIQ GMGLYTIEEL NYSPQGILHT RGPDQYKIPA ICDMPTELHI ALLPPSQNSN TLYSSKGLGE SGVFLGCSVF FAIHDAVSAA RQERGLHGPL TLNSPLTPEK IRMACEDKFT KMIPRDEPGS YVPWNVPI //