AL3A2_HUMAN
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 03-AUG-2022, entry version 204.
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},
GN FALDH {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:9133646, PubMed:22633490, PubMed:25047030, PubMed:18035827,
CC PubMed:9662422, PubMed:18182499). 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 + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
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 + H2O + NAD(+) = a fatty acid + 2 H(+) +
CC NADH; 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 + H2O + NAD(+) = (E)-hexadec-2-enoate + 2
CC H(+) + NADH; Xref=Rhea:RHEA:36135, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17585, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:72745;
CC Evidence={ECO:0000269|PubMed:22633490};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hexadecanoate + NADH = H2O + hexadecanal + NAD(+);
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 + H2O + NAD(+) = docosanedioate + 2 H(+) +
CC NADH; 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 + H2O + NAD(+) = 2,6,10,14-
CC tetramethylpentadecanoate + 2 H(+) + NADH; 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=H2O + NAD(+) + octadecanal = 2 H(+) + NADH + octadecanoate;
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 + 2 H(+) + NADH = dodecanal + H2O + NAD(+);
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 + H2O + NAD(+) = decanoate + 2 H(+) + NADH;
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=H2O + NAD(+) + tetradecanal = 2 H(+) + NADH + tetradecanoate;
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=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate;
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=H2O + heptanal + NAD(+) = 2 H(+) + heptanoate + NADH;
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 + H2O + NAD(+) = (2E,6E)-farnesoate + 2 H(+)
CC + NADH; 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}.
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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_000382.2. [P51648-1]
DR RefSeq; NP_001026976.1; NM_001031806.1. [P51648-2]
DR RefSeq; XP_011522034.1; XM_011523732.1.
DR RefSeq; XP_011522035.1; XM_011523733.1.
DR RefSeq; XP_016879845.1; XM_017024356.1.
DR RefSeq; XP_016879846.1; XM_017024357.1.
DR PDB; 4QGK; X-ray; 2.10 A; A/B=1-460.
DR PDBsum; 4QGK; -.
DR AlphaFoldDB; P51648; -.
DR SMR; P51648; -.
DR BioGRID; 106726; 270.
DR IntAct; P51648; 113.
DR MINT; P51648; -.
DR STRING; 9606.ENSP00000345774; -.
DR ChEMBL; CHEMBL4295779; -.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB12612; Ozanimod.
DR SwissLipids; SLP:000000198; -.
DR iPTMnet; P51648; -.
DR PhosphoSitePlus; P51648; -.
DR SwissPalm; P51648; -.
DR BioMuta; ALDH3A2; -.
DR DMDM; 1706379; -.
DR EPD; P51648; -.
DR jPOST; P51648; -.
DR MassIVE; P51648; -.
DR MaxQB; P51648; -.
DR PaxDb; P51648; -.
DR PeptideAtlas; P51648; -.
DR PRIDE; P51648; -.
DR ProteomicsDB; 56356; -. [P51648-1]
DR ProteomicsDB; 56357; -. [P51648-2]
DR Antibodypedia; 2232; 473 antibodies from 32 providers.
DR DNASU; 224; -.
DR Ensembl; ENST00000176643.11; ENSP00000176643.6; ENSG00000072210.19. [P51648-1]
DR Ensembl; ENST00000339618.8; ENSP00000345774.4; ENSG00000072210.19. [P51648-2]
DR Ensembl; ENST00000579855.5; ENSP00000463637.1; ENSG00000072210.19. [P51648-1]
DR Ensembl; ENST00000581518.6; ENSP00000461916.2; ENSG00000072210.19. [P51648-1]
DR Ensembl; ENST00000672357.1; ENSP00000500092.1; ENSG00000072210.19. [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 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 neXtProt; NX_P51648; -.
DR OpenTargets; ENSG00000072210; -.
DR Orphanet; 816; Sjoegren-Larsson syndrome.
DR PharmGKB; PA24698; -.
DR VEuPathDB; HostDB:ENSG00000072210; -.
DR eggNOG; KOG2456; Eukaryota.
DR GeneTree; ENSGT00940000157944; -.
DR HOGENOM; CLU_005391_3_0_1; -.
DR InParanoid; P51648; -.
DR OMA; GKWTNCG; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; P51648; -.
DR TreeFam; TF314264; -.
DR BioCyc; MetaCyc:HS01061-MON; -.
DR BRENDA; 1.2.1.48; 2681.
DR PathwayCommons; P51648; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis. [P51648-1]
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 SABIO-RK; P51648; -.
DR SignaLink; P51648; -.
DR BioGRID-ORCS; 224; 8 hits in 1077 CRISPR screens.
DR ChiTaRS; ALDH3A2; human.
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 205 other tissues.
DR ExpressionAtlas; P51648; baseline and differential.
DR Genevisible; P51648; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0046577; F:long-chain-alcohol oxidase activity; IDA:UniProtKB.
DR GO; GO:0050061; F:long-chain-aldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0052814; F:medium-chain-aldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0006081; P:cellular 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:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
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 Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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; PTHR43570; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
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; Reference proteome; Transmembrane;
KW 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..59
FT /evidence="ECO:0007829|PDB:4QGK"
FT HELIX 61..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..199
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 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..454
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
