ID AL3A2_HUMAN Reviewed; 485 AA. AC P51648; Q6I9T3; Q93011; Q96J37; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 223. DE RecName: Full=Aldehyde dehydrogenase family 3 member A2; DE EC=1.2.1.3 {ECO:0000269|PubMed:18035827, ECO:0000269|PubMed:18182499, ECO:0000269|PubMed:22633490, ECO:0000269|PubMed:25047030, ECO:0000269|PubMed:9133646, ECO:0000269|PubMed:9662422}; DE EC=1.2.1.94 {ECO:0000269|PubMed:18035827}; DE AltName: Full=Aldehyde dehydrogenase 10 {ECO:0000303|PubMed:9070922}; DE AltName: Full=Fatty aldehyde dehydrogenase; DE AltName: Full=Microsomal aldehyde dehydrogenase; GN Name=ALDH3A2; GN Synonyms=ALDH10 {ECO:0000303|PubMed:9070922}, FALDH GN {ECO:0000303|PubMed:9027499}; 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), PARTIAL PROTEIN SEQUENCE, VARIANTS RP SLS, AND INVOLVEMENT IN SLS. RX PubMed=8528251; DOI=10.1038/ng0196-52; RA de Laurenzi V., Rogers G.R., Hamrock D.J., Marekov L.N., Steinert P.M., RA Compton J.G., Markova N., Rizzo W.B.; RT "Sjogren-Larsson syndrome is caused by mutations in the fatty aldehyde RT dehydrogenase gene."; RL Nat. Genet. 12:52-57(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2). RX PubMed=9027499; DOI=10.1006/geno.1996.4501; RA Rogers G.R., Markova N.G., De Laurenzi V., Rizzo W.B., Compton J.G.; RT "Genomic organization and expression of the human fatty aldehyde RT dehydrogenase gene (FALDH)."; RL Genomics 39:127-135(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=9070922; DOI=10.1006/geno.1996.4547; RA Chang C., Yoshida A.; RT "Human fatty aldehyde dehydrogenase gene (ALDH10): organization and tissue- RT dependent expression."; RL Genomics 40:80-85(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis, 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 MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 2). RC TISSUE=Skin; 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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND TISSUE SPECIFICITY. RX PubMed=9133646; DOI=10.1016/s0304-4165(96)00126-2; RA Kelson T.L., Secor McVoy J.R., Rizzo W.B.; RT "Human liver fatty aldehyde dehydrogenase: microsomal localization, RT purification, and biochemical characterization."; RL Biochim. Biophys. Acta 1335:99-110(1997). RN [9] RP CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=9662422; DOI=10.1016/s0014-5793(98)00574-2; RA Verhoeven N.M., Jakobs C., Carney G., Somers M.P., Wanders R.J., RA Rizzo W.B.; RT "Involvement of microsomal fatty aldehyde dehydrogenase in the alpha- RT oxidation of phytanic acid."; RL FEBS Lett. 429:225-228(1998). RN [10] RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=18035827; DOI=10.1080/14756360701425360; RA Lloyd M.D., Boardman K.D., Smith A., van den Brink D.M., Wanders R.J., RA Threadgill M.D.; RT "Characterisation of recombinant human fatty aldehyde dehydrogenase: RT implications for Sjoegren-Larsson syndrome."; RL J. Enzym. Inhib. Med. Chem. 22:584-590(2007). RN [11] RP CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=18182499; DOI=10.1096/fj.07-099150; RA Sanders R.J., Ofman R., Dacremont G., Wanders R.J., Kemp S.; RT "Characterization of the human omega-oxidation pathway for omega-hydroxy- RT very-long-chain fatty acids."; RL FASEB J. 22:2064-2071(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=22633490; DOI=10.1016/j.molcel.2012.04.033; RA Nakahara K., Ohkuni A., Kitamura T., Abe K., Naganuma T., Ohno Y., RA Zoeller R.A., Kihara A.; RT "The Sjogren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of RT the sphingosine 1-phosphate degradation pathway."; RL Mol. Cell 46:461-471(2012). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, 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 [16] {ECO:0007744|PDB:4QGK} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-460, FUNCTION, CATALYTIC RP ACTIVITY, TOPOLOGY, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF ASN-112; RP GLU-207; CYS-241; GLU-331; TYR-410 AND 445-GLN--TYR-485. RX PubMed=25047030; DOI=10.1038/ncomms5439; RA Keller M.A., Zander U., Fuchs J.E., Kreutz C., Watschinger K., Mueller T., RA Golderer G., Liedl K.R., Ralser M., Krautler B., Werner E.R., Marquez J.A.; RT "A gatekeeper helix determines the substrate specificity of Sjogren-Larsson RT Syndrome enzyme fatty aldehyde dehydrogenase."; RL Nat. Commun. 5:4439-4439(2014). RN [17] RP VARIANT SLS SER-315. RX PubMed=9254849; DOI=10.1007/s004390050490; RA Sillen A., Jagell S., Wadelius C.; RT "A missense mutation in the FALDH gene identified in Sjogren-Larsson RT syndrome patients originating from the northern part of Sweden."; RL Hum. Genet. 100:201-203(1997). RN [18] RP VARIANTS SLS ARG-106; TRP-226; ASN-245; SER-315; LEU-365 AND ARG-412. RX PubMed=9829906; RX DOI=10.1002/(sici)1098-1004(1998)12:6<377::aid-humu3>3.0.co;2-i; RA Sillen A., Anton-Lamprecht I., Braun-Quentin C., Kraus C.S., Sayli B.S., RA Ayuso C., Jagell S., Kuester W., Wadelius C.; RT "Spectrum of mutations and sequence variants in the FALDH gene in patients RT with Sjoegren-Larsson syndrome."; RL Hum. Mutat. 12:377-384(1998). RN [19] RP VARIANTS SLS PHE-45; ASP-64; ARG-106; LEU-114; LEU-121; ARG-184; MET-184; RP ALA-185; CYS-228; TYR-237; ASN-245; ASN-266; ASN-279; SER-315; ILE-328; RP LEU-365; ARG-406; TYR-411; ASN-415; SER-419; HIS-423 AND GLU-447. RX PubMed=10577908; DOI=10.1086/302681; RA Rizzo W.B., Carney G., Lin Z.; RT "The molecular basis of Sjoegren-Larsson syndrome: mutation analysis of the RT fatty aldehyde dehydrogenase gene."; RL Am. J. Hum. Genet. 65:1547-1560(1999). RN [20] RP VARIANT SLS SER-386. RX PubMed=10792573; DOI=10.1046/j.1523-1747.2000.00960-5.x; RA Aoki N., Suzuki H., Ito K., Ito M.; RT "A novel point mutation of the FALDH gene in a Japanese family with RT Sjoegren-Larsson syndrome."; RL J. Invest. Dermatol. 114:1065-1066(2000). CC -!- FUNCTION: Catalyzes the oxidation of medium and long chain aliphatic CC aldehydes to fatty acids. Active on a variety of saturated and CC unsaturated aliphatic aldehydes between 6 and 24 carbons in length CC (PubMed:18035827, PubMed:18182499, PubMed:22633490, PubMed:25047030, CC PubMed:9133646, PubMed:9662422). Responsible for conversion of the CC sphingosine 1-phosphate (S1P) degradation product hexadecenal to CC hexadecenoic acid (PubMed:22633490). {ECO:0000269|PubMed:18035827, CC ECO:0000269|PubMed:18182499, ECO:0000269|PubMed:22633490, CC ECO:0000269|PubMed:25047030, ECO:0000269|PubMed:9133646, CC ECO:0000269|PubMed:9662422}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an aldehyde + NAD(+) + H2O = a carboxylate + NADH + 2 H(+); CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000269|PubMed:18035827, CC ECO:0000269|PubMed:18182499, ECO:0000269|PubMed:22633490, CC ECO:0000269|PubMed:25047030, ECO:0000269|PubMed:9133646, CC ECO:0000269|PubMed:9662422}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a fatty aldehyde + NAD(+) + H2O = a fatty acid + NADH + 2 CC H(+); Xref=Rhea:RHEA:49832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28868, ChEBI:CHEBI:35746, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:18035827, CC ECO:0000269|PubMed:22633490, ECO:0000269|PubMed:25047030, CC ECO:0000269|PubMed:9133646, ECO:0000269|PubMed:9662422}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-hexadecenal + NAD(+) + H2O = (E)-hexadec-2-enoate + NADH CC + 2 H(+); Xref=Rhea:RHEA:36135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17585, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:72745; Evidence={ECO:0000269|PubMed:22633490}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexadecanoate + NADH + 2 H(+) = hexadecanal + NAD(+) + H2O; CC Xref=Rhea:RHEA:33739, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17600, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:18035827, CC ECO:0000269|PubMed:22633490}; CC -!- CATALYTIC ACTIVITY: CC Reaction=22-oxodocosanoate + NAD(+) + H2O = docosanedioate + NADH + 2 CC H(+); Xref=Rhea:RHEA:39015, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76298, CC ChEBI:CHEBI:76299; Evidence={ECO:0000269|PubMed:18182499}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2,6,10,14-tetramethylpentadecanal + NAD(+) + H2O = 2,6,10,14- CC tetramethylpentadecanoate + NADH + 2 H(+); Xref=Rhea:RHEA:44016, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:49189, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:77268; CC Evidence={ECO:0000269|PubMed:9662422}; CC -!- CATALYTIC ACTIVITY: CC Reaction=octadecanal + NAD(+) + H2O = octadecanoate + NADH + 2 H(+); CC Xref=Rhea:RHEA:44020, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17034, ChEBI:CHEBI:25629, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:18035827, CC ECO:0000269|PubMed:9662422}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoate + NADH + 2 H(+) = dodecanal + NAD(+) + H2O; CC Xref=Rhea:RHEA:44168, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:18262, ChEBI:CHEBI:27836, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:18035827, CC ECO:0000269|PubMed:25047030}; CC -!- CATALYTIC ACTIVITY: CC Reaction=decanal + NAD(+) + H2O = decanoate + NADH + 2 H(+); CC Xref=Rhea:RHEA:44104, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:27689, ChEBI:CHEBI:31457, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:18035827, CC ECO:0000269|PubMed:9133646}; CC -!- CATALYTIC ACTIVITY: CC Reaction=tetradecanal + NAD(+) + H2O = tetradecanoate + NADH + 2 H(+); CC Xref=Rhea:RHEA:44172, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:84067; Evidence={ECO:0000269|PubMed:18035827, CC ECO:0000269|PubMed:9133646}; CC -!- CATALYTIC ACTIVITY: CC Reaction=octanal + NAD(+) + H2O = octanoate + NADH + 2 H(+); CC Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:18035827, CC ECO:0000269|PubMed:25047030, ECO:0000269|PubMed:9133646}; CC -!- CATALYTIC ACTIVITY: CC Reaction=heptanal + NAD(+) + H2O = heptanoate + NADH + 2 H(+); CC Xref=Rhea:RHEA:44108, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32362, ChEBI:CHEBI:34787, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:18035827}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesal + NAD(+) + H2O = (2E,6E)-farnesoate + NADH + CC 2 H(+); Xref=Rhea:RHEA:24216, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15894, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:83276; EC=1.2.1.94; CC Evidence={ECO:0000269|PubMed:18035827}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=50 uM for hexanal {ECO:0000269|PubMed:9133646}; CC KM=32 uM for octanal {ECO:0000269|PubMed:9133646}; CC KM=23 uM for decanal {ECO:0000269|PubMed:9133646}; CC KM=3.8 uM for decanal {ECO:0000269|PubMed:18035827}; CC KM=19 uM for dodecanal {ECO:0000269|PubMed:9133646}; CC KM=13.6 uM for dodecanal {ECO:0000269|PubMed:18035827}; CC KM=23 uM for tetradecanal {ECO:0000269|PubMed:9133646}; CC KM=10.3 uM for tetradecanal {ECO:0000269|PubMed:18035827}; CC KM=8.3 uM for hexadecanal {ECO:0000269|PubMed:18035827}; CC KM=32 uM for hexadecanal {ECO:0000269|PubMed:9133646}; CC KM=21 uM for octadecanal {ECO:0000269|PubMed:9133646}; CC KM=20 uM for octadecanal {ECO:0000269|PubMed:18035827}; CC KM=23 uM for farnesal {ECO:0000269|PubMed:18035827}; CC KM=280 uM for NAD {ECO:0000269|PubMed:9133646}; CC KM=180 uM for NAD {ECO:0000269|PubMed:18035827}; CC KM=8700 uM for NADP {ECO:0000269|PubMed:9133646}; CC Vmax=29 umol/min/mg enzyme with hexanal {ECO:0000269|PubMed:9133646}; CC Vmax=63 umol/min/mg enzyme with octanal {ECO:0000269|PubMed:9133646}; CC Vmax=73 umol/min/mg enzyme with decanal {ECO:0000269|PubMed:9133646}; CC Vmax=2.3 umol/min/mg enzyme with decanal CC {ECO:0000269|PubMed:18035827}; CC Vmax=45 umol/min/mg enzyme with dodecanal CC {ECO:0000269|PubMed:9133646}; CC Vmax=2.3 umol/min/mg enzyme with dodecanal CC {ECO:0000269|PubMed:18035827}; CC Vmax=40 umol/min/mg enzyme with hexadecanal CC {ECO:0000269|PubMed:9133646}; CC Vmax=0.9 umol/min/mg enzyme with hexadecanal CC {ECO:0000269|PubMed:18035827}; CC Vmax=46 umol/min/mg enzyme with octadecanal CC {ECO:0000269|PubMed:9133646}; CC Vmax=1.6 umol/min/mg enzyme with octadecanal CC {ECO:0000269|PubMed:18035827}; CC Vmax=42 umol/min/mg enzyme with tetradecanal CC {ECO:0000269|PubMed:9133646}; CC Vmax=0.9 umol/min/mg enzyme with tetradecanal CC {ECO:0000269|PubMed:18035827}; CC Vmax=0.97 umol/min/mg enzyme with farnesal CC {ECO:0000269|PubMed:18035827}; CC Vmax=1.3 umol/min/mg enzyme with NAD {ECO:0000269|PubMed:18035827}; CC Note=kcat is 2.18 sec(-1) for decanal as substrate. kcat is 2.23 CC sec(-1) for dodecanal as substrate. kcat is 0.86 sec(-1) for CC tetradecanal as substrate. kcat is 0.95 sec(-1) for hexadecanal as CC substrate. kcat is 1.52 sec(-1) for octadecanal as substrate. kcat is CC 0.93 sec(-1) for farnesal as substrate. kcat is 1.28 sec(-1) for NAD CC as substrate. {ECO:0000269|PubMed:18035827}; CC pH dependence: CC Optimum pH is 9.8. {ECO:0000269|PubMed:18035827, CC ECO:0000269|PubMed:9133646}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25047030}. CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:9133646}; CC Single-pass membrane protein {ECO:0000305|PubMed:25047030, CC ECO:0000305|PubMed:9133646}. Endoplasmic reticulum membrane CC {ECO:0000305|PubMed:9133646}; Single-pass membrane protein CC {ECO:0000305|PubMed:25047030, ECO:0000305|PubMed:9133646}; Cytoplasmic CC side {ECO:0000250|UniProtKB:P30839}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P51648-1; Sequence=Displayed; CC Name=2; CC IsoId=P51648-2; Sequence=VSP_001283; CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level). CC {ECO:0000269|PubMed:9133646}. CC -!- DISEASE: Sjoegren-Larsson syndrome (SLS) [MIM:270200]: An autosomal CC recessive neurocutaneous disorder characterized by a combination of CC severe intellectual disability, spastic di- or tetraplegia and CC congenital ichthyosis. Ichthyosis is usually evident at birth with CC varying degrees of erythema and scaling, neurologic symptoms appear in CC the first or second year of life. Most patients have an IQ of less than CC 60. Additional clinical features include glistening white spots on the CC retina, seizures, short stature and speech defects. CC {ECO:0000269|PubMed:10577908, ECO:0000269|PubMed:10792573, CC ECO:0000269|PubMed:8528251, ECO:0000269|PubMed:9254849, CC ECO:0000269|PubMed:9829906}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {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; L47162; AAB01003.1; -; mRNA. DR EMBL; U75296; AAC50966.1; -; Genomic_DNA. DR EMBL; U75286; AAC50966.1; JOINED; Genomic_DNA. DR EMBL; U75287; AAC50966.1; JOINED; Genomic_DNA. DR EMBL; U75288; AAC50966.1; JOINED; Genomic_DNA. DR EMBL; U75289; AAC50966.1; JOINED; Genomic_DNA. DR EMBL; U75290; AAC50966.1; JOINED; Genomic_DNA. DR EMBL; U75291; AAC50966.1; JOINED; Genomic_DNA. DR EMBL; U75292; AAC50966.1; JOINED; Genomic_DNA. DR EMBL; U75293; AAC50966.1; JOINED; Genomic_DNA. DR EMBL; U75294; AAC50966.1; JOINED; Genomic_DNA. DR EMBL; U75295; AAC50965.1; -; Genomic_DNA. DR EMBL; U75286; AAC50965.1; JOINED; Genomic_DNA. DR EMBL; U75287; AAC50965.1; JOINED; Genomic_DNA. DR EMBL; U75288; AAC50965.1; JOINED; Genomic_DNA. DR EMBL; U75289; AAC50965.1; JOINED; Genomic_DNA. DR EMBL; U75290; AAC50965.1; JOINED; Genomic_DNA. DR EMBL; U75291; AAC50965.1; JOINED; Genomic_DNA. DR EMBL; U75292; AAC50965.1; JOINED; Genomic_DNA. DR EMBL; U75293; AAC50965.1; JOINED; Genomic_DNA. DR EMBL; U75294; AAC50965.1; JOINED; Genomic_DNA. DR EMBL; U46689; AAC51121.1; -; mRNA. DR EMBL; AK292381; BAF85070.1; -; mRNA. DR EMBL; AK315096; BAG37560.1; -; mRNA. DR EMBL; CR457422; CAG33703.1; -; mRNA. DR EMBL; CH471212; EAW50898.1; -; Genomic_DNA. DR EMBL; BC002430; AAH02430.1; -; mRNA. DR CCDS; CCDS11210.1; -. [P51648-1] DR CCDS; CCDS32589.1; -. [P51648-2] DR RefSeq; NP_000373.1; NM_000382.3. [P51648-1] DR RefSeq; NP_001026976.1; NM_001031806.2. [P51648-2] DR RefSeq; NP_001356065.1; NM_001369136.1. [P51648-2] DR RefSeq; NP_001356066.1; NM_001369137.2. [P51648-2] DR RefSeq; NP_001356067.1; NM_001369138.2. [P51648-1] DR RefSeq; NP_001356068.1; NM_001369139.1. [P51648-1] DR PDB; 4QGK; X-ray; 2.10 A; A/B=1-460. DR AlphaFoldDB; P51648; -. DR SMR; P51648; -. DR BioGRID; 106726; 383. DR FunCoup; P51648; 3062. DR IntAct; P51648; 187. DR MINT; P51648; -. DR NDEx; IQUERY-CP-ALDH3A2; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000345774; -. DR ChEMBL; CHEMBL4295779; -. DR DrugBank; DB14174; Dipentamethylenethiuram disulfide. DR DrugBank; DB00822; Disulfiram. DR DrugBank; DB00157; NADH. DR DrugBank; DB12612; Ozanimod. DR SwissLipids; SLP:000000198; -. DR GlyGen; P51648; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P51648; -. DR PhosphoSitePlus; P51648; -. DR SwissPalm; P51648; -. DR BioMuta; ALDH3A2; -. DR DMDM; 1706379; -. DR jPOST; P51648; -. DR MassIVE; P51648; -. DR PaxDb; 9606-ENSP00000345774; -. DR PeptideAtlas; P51648; -. DR ProteomicsDB; 56356; -. [P51648-1] DR ProteomicsDB; 56357; -. [P51648-2] DR Pumba; P51648; -. DR Antibodypedia; 2232; 490 antibodies from 35 providers. DR DNASU; 224; -. DR Ensembl; ENST00000176643.11; ENSP00000176643.6; ENSG00000072210.20. [P51648-1] DR Ensembl; ENST00000339618.8; ENSP00000345774.4; ENSG00000072210.20. [P51648-2] DR Ensembl; ENST00000579855.5; ENSP00000463637.1; ENSG00000072210.20. [P51648-1] DR Ensembl; ENST00000581518.6; ENSP00000461916.2; ENSG00000072210.20. [P51648-1] DR Ensembl; ENST00000672357.1; ENSP00000500092.1; ENSG00000072210.20. [P51648-1] DR Ensembl; ENST00000877756.1; ENSP00000547815.1; ENSG00000072210.20. [P51648-1] DR Ensembl; ENST00000877757.1; ENSP00000547816.1; ENSG00000072210.20. [P51648-1] DR GeneID; 224; -. DR KEGG; hsa:224; -. DR MANE-Select; ENST00000176643.11; ENSP00000176643.6; NM_000382.3; NP_000373.1. DR UCSC; uc002gwa.2; human. [P51648-1] DR AGR; HGNC:403; -. DR ClinPGx; PA24698; -. DR CTD; 224; -. DR DisGeNET; 224; -. DR GeneCards; ALDH3A2; -. DR HGNC; HGNC:403; ALDH3A2. DR HPA; ENSG00000072210; Tissue enhanced (liver). DR MalaCards; ALDH3A2; -. DR MIM; 270200; phenotype. DR MIM; 609523; gene. DR OpenTargets; ENSG00000072210; -. DR Orphanet; 816; Sjoegren-Larsson syndrome. DR VEuPathDB; HostDB:ENSG00000072210; -. DR eggNOG; KOG2456; Eukaryota. DR GeneTree; ENSGT00940000157944; -. DR HOGENOM; CLU_005391_3_0_1; -. DR InParanoid; P51648; -. DR OMA; KMFGDNP; -. DR OrthoDB; 440325at2759; -. DR PAN-GO; P51648; 5 GO annotations based on evolutionary models. DR PhylomeDB; P51648; -. DR BioCyc; MetaCyc:HS01061-MONOMER; -. DR BRENDA; 1.2.1.48; 2681. DR PathwayCommons; P51648; -. DR Reactome; R-HSA-389599; Alpha-oxidation of phytanate. [P51648-2] DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import. [P51648-2] DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane. [P51648-1] DR Reactome; R-HSA-9696270; RND2 GTPase cycle. DR Reactome; R-HSA-9696273; RND1 GTPase cycle. DR Reactome; R-HSA-9845614; Sphingolipid catabolism. [P51648-1] DR SABIO-RK; P51648; -. DR SignaLink; P51648; -. DR SIGNOR; P51648; -. DR Agora; ENSG00000072210; -. DR BioGRID-ORCS; 224; 8 hits in 1167 CRISPR screens. DR CD-CODE; DEE660B4; Stress granule. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; ALDH3A2; human. DR EvolutionaryTrace; P51648; -. DR GenomeRNAi; 224; -. DR Pharos; P51648; Tbio. DR PRO; PR:P51648; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P51648; protein. DR Bgee; ENSG00000072210; Expressed in adrenal tissue and 207 other cell types or tissues. DR ExpressionAtlas; P51648; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005778; C:peroxisomal membrane; TAS:Reactome. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IBA:GO_Central. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB. DR GO; GO:0120553; F:farnesal dehydrogenase (NAD+) activity; EXP:UniProtKB. DR GO; GO:0102673; F:fatty aldehyde dehydrogenase (NAD+) activity; EXP:UniProtKB. DR GO; GO:0050061; F:long-chain fatty aldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB. DR GO; GO:0046577; F:long-chain-alcohol oxidase activity; IDA:UniProtKB. DR GO; GO:0052814; F:medium-chain fatty aldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0006081; P:aldehyde metabolic process; IDA:UniProtKB. DR GO; GO:0007417; P:central nervous system development; IMP:UniProtKB. DR GO; GO:0008544; P:epidermis development; IMP:UniProtKB. DR GO; GO:0046458; P:hexadecanal metabolic process; IDA:UniProtKB. DR GO; GO:0007422; P:peripheral nervous system development; IMP:UniProtKB. DR GO; GO:0033306; P:phytol metabolic process; IMP:UniProtKB. DR GO; GO:0006714; P:sesquiterpenoid metabolic process; IDA:UniProtKB. DR CDD; cd07132; ALDH_F3AB; 1. DR FunFam; 3.40.309.10:FF:000003; Aldehyde dehydrogenase; 1. DR FunFam; 3.40.605.10:FF:000004; Aldehyde dehydrogenase; 1. DR Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1. DR Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS_CYS. DR InterPro; IPR029510; Ald_DH_CS_GLU. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR012394; Aldehyde_DH_NAD(P). DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR43570:SF9; ALDEHYDE DEHYDROGENASE FAMILY 3 MEMBER A2; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF036492; ALDH; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. DR PDBsum; 4QGK; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; KW Disease variant; Endoplasmic reticulum; Fatty acid metabolism; Ichthyosis; KW Intellectual disability; Lipid metabolism; Membrane; Microsome; NAD; KW Oxidoreductase; Phosphoprotein; Proteomics identification; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..485 FT /note="Aldehyde dehydrogenase family 3 member A2" FT /id="PRO_0000056473" FT TOPO_DOM 1..463 FT /note="Cytoplasmic" FT TRANSMEM 464..484 FT /note="Helical" FT /evidence="ECO:0000255" FT ACT_SITE 207 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, FT ECO:0000269|PubMed:25047030" FT ACT_SITE 241 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008, FT ECO:0000269|PubMed:25047030" FT BINDING 185..190 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255" FT MOD_RES 293 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 482..485 FT /note="AEYY -> KYQAVLRRKALLIFLVVHRLRWSSKQR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9027499" FT /id="VSP_001283" FT VARIANT 45 FT /note="I -> F (in SLS; severe loss of activity)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017510" FT VARIANT 64 FT /note="V -> D (in SLS; severe loss of activity; FT dbSNP:rs72547556)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017511" FT VARIANT 106 FT /note="L -> R (in SLS; severe loss of activity; FT dbSNP:rs72547558)" FT /evidence="ECO:0000269|PubMed:10577908, FT ECO:0000269|PubMed:9829906" FT /id="VAR_002249" FT VARIANT 114 FT /note="P -> L (in SLS; severe loss of activity; FT dbSNP:rs72547559)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017512" FT VARIANT 121 FT /note="P -> L (in SLS; severe loss of activity; FT dbSNP:rs72547560)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017513" FT VARIANT 184 FT /note="T -> M (in SLS; severe loss of activity; FT dbSNP:rs72547562)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017514" FT VARIANT 184 FT /note="T -> R (in SLS; severe loss of activity)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017515" FT VARIANT 185 FT /note="G -> A (in SLS; severe loss of activity; FT dbSNP:rs72547563)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017516" FT VARIANT 214 FT /note="C -> Y (in SLS; 4% of activity; dbSNP:rs72547564)" FT /evidence="ECO:0000269|PubMed:8528251" FT /id="VAR_002250" FT VARIANT 226 FT /note="C -> W (in SLS; dbSNP:rs72547565)" FT /evidence="ECO:0000269|PubMed:9829906" FT /id="VAR_002251" FT VARIANT 228 FT /note="R -> C (in SLS; severe loss of activity; FT dbSNP:rs72547566)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017517" FT VARIANT 237 FT /note="C -> Y (in SLS; severe loss of activity; FT dbSNP:rs72547567)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017518" FT VARIANT 245 FT /note="D -> N (in SLS; severe loss of activity; FT dbSNP:rs72547568)" FT /evidence="ECO:0000269|PubMed:10577908, FT ECO:0000269|PubMed:9829906" FT /id="VAR_002252" FT VARIANT 266 FT /note="K -> N (in SLS; mild reduction of activity; the FT underlying nucleotide substitution affects transcript FT stability; dbSNP:rs72547569)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017519" FT VARIANT 279 FT /note="Y -> N (in SLS; severe loss of activity; FT dbSNP:rs72547570)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017520" FT VARIANT 314..315 FT /note="AP -> GAKSTVGA (in SLS; 8% of activity)" FT /evidence="ECO:0000269|PubMed:8528251" FT /id="VAR_002253" FT VARIANT 315 FT /note="P -> S (in SLS; common mutation in Europeans; severe FT loss of enzymatic activity; dbSNP:rs72547571)" FT /evidence="ECO:0000269|PubMed:10577908, FT ECO:0000269|PubMed:9254849, ECO:0000269|PubMed:9829906" FT /id="VAR_002254" FT VARIANT 328 FT /note="M -> I (in SLS; dbSNP:rs72547572)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017521" FT VARIANT 365 FT /note="S -> L (in SLS; severe loss of activity; FT dbSNP:rs72547573)" FT /evidence="ECO:0000269|PubMed:10577908, FT ECO:0000269|PubMed:9829906" FT /id="VAR_002255" FT VARIANT 386 FT /note="N -> S (in SLS; dbSNP:rs72547575)" FT /evidence="ECO:0000269|PubMed:10792573" FT /id="VAR_017522" FT VARIANT 406 FT /note="G -> R (in SLS)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017523" FT VARIANT 411 FT /note="H -> Y (in SLS; severe loss of activity)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017524" FT VARIANT 412 FT /note="G -> R (in SLS; dbSNP:rs778115541)" FT /evidence="ECO:0000269|PubMed:9829906" FT /id="VAR_002256" FT VARIANT 415 FT /note="S -> N (in SLS; severe loss of activity)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017525" FT VARIANT 419 FT /note="F -> S (in SLS; severe loss of activity; FT dbSNP:rs72547576)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017526" FT VARIANT 423 FT /note="R -> H (in SLS; severe loss of activity; FT dbSNP:rs768290318)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017527" FT VARIANT 447 FT /note="K -> E (in SLS; severe loss of activity; FT dbSNP:rs67939114)" FT /evidence="ECO:0000269|PubMed:10577908" FT /id="VAR_017528" FT MUTAGEN 112 FT /note="N->A: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:25047030" FT MUTAGEN 207 FT /note="E->Q: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:25047030" FT MUTAGEN 241 FT /note="C->S: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:25047030" FT MUTAGEN 331 FT /note="E->Q: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:25047030" FT MUTAGEN 410 FT /note="Y->F: Decreased enzyme activity with dodecanal and FT hexadecanal. No effect on enzyme activity with octanal." FT /evidence="ECO:0000269|PubMed:25047030" FT MUTAGEN 445..485 FT /note="Missing: Decreased enzyme activity with dodecanal. FT Strongly decreased enzyme activity with hexadecanal. No FT effect on enzyme activity with octanal." FT /evidence="ECO:0000269|PubMed:25047030" FT HELIX 1..13 FT /evidence="ECO:0007829|PDB:4QGK" FT TURN 14..17 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 20..36 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 38..49 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 53..56 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 57..61 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 62..78 FT /evidence="ECO:0007829|PDB:4QGK" FT TURN 88..92 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 93..101 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 103..108 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 116..127 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 131..135 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 141..154 FT /evidence="ECO:0007829|PDB:4QGK" FT TURN 157..159 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 167..173 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 179..185 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 187..200 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 204..207 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 213..216 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 218..220 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 222..234 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 235..238 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 246..249 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 251..253 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 254..269 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 273..275 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 285..293 FT /evidence="ECO:0007829|PDB:4QGK" FT TURN 294..297 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 300..302 FT /evidence="ECO:0007829|PDB:4QGK" FT TURN 308..311 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 326..328 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 334..341 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 345..353 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 356..358 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 359..364 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 368..377 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 381..389 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 390..393 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 403..405 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 413..418 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 420..427 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 433..438 FT /evidence="ECO:0007829|PDB:4QGK" FT STRAND 440..442 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 445..450 FT /evidence="ECO:0007829|PDB:4QGK" FT HELIX 451..455 FT /evidence="ECO:0007829|PDB:4QGK" SQ SEQUENCE 485 AA; 54848 MW; 209601CB5803C7E3 CRC64; MELEVRRVRQ AFLSGRSRPL RFRLQQLEAL RRMVQEREKD ILTAIAADLC KSEFNVYSQE VITVLGEIDF MLENLPEWVT AKPVKKNVLT MLDEAYIQPQ PLGVVLIIGA WNYPFVLTIQ PLIGAIAAGN AVIIKPSELS ENTAKILAKL LPQYLDQDLY IVINGGVEET TELLKQRFDH IFYTGNTAVG KIVMEAAAKH LTPVTLELGG KSPCYIDKDC DLDIVCRRIT WGKYMNCGQT CIAPDYILCE ASLQNQIVWK IKETVKEFYG ENIKESPDYE RIINLRHFKR ILSLLEGQKI AFGGETDEAT RYIAPTVLTD VDPKTKVMQE EIFGPILPIV PVKNVDEAIN FINEREKPLA LYVFSHNHKL IKRMIDETSS GGVTGNDVIM HFTLNSFPFG GVGSSGMGAY HGKHSFDTFS HQRPCLLKSL KREGANKLRY PPNSQSKVDW GKFFLLKRFN KEKLGLLLLT FLGIVAAVLV KAEYY //