ID AL3A2_MOUSE Reviewed; 484 AA. AC P47740; Q99L64; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 24-JUL-2024, entry version 180. DE RecName: Full=Aldehyde dehydrogenase family 3 member A2; DE EC=1.2.1.3 {ECO:0000269|PubMed:25286108}; DE EC=1.2.1.94 {ECO:0000250|UniProtKB:P51648}; DE AltName: Full=Aldehyde dehydrogenase 3; DE AltName: Full=Fatty aldehyde dehydrogenase; GN Name=Aldh3a2; Synonyms=Ahd-3, Ahd3, Aldh3, Aldh4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Liver; RX PubMed=8634152; DOI=10.1089/dna.1996.15.235; RA Vasiliou V., Kozak C.A., Lindahl R., Nebert D.W.; RT "Mouse microsomal class 3 aldehyde dehydrogenase: AHD3 cDNA sequence, RT inducibility by dioxin and clofibrate, and genetic mapping."; RL DNA Cell Biol. 15:235-245(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, Spinal cord, Stomach, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=25286108; DOI=10.1042/bj20140624; RA Kitamura T., Takagi S., Naganuma T., Kihara A.; RT "Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets via RT two C-terminal tryptophan residues and lipid modification."; RL Biochem. J. 465:79-87(2015). 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:25286108). Responsible for conversion of the sphingosine 1- CC phosphate (S1P) degradation product hexadecenal to hexadecenoic acid CC (PubMed:25286108). {ECO:0000269|PubMed:25286108}. 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; CC Evidence={ECO:0000269|PubMed:25286108}; 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:25286108}; 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:25286108}; 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:25286108}; 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:0000250|UniProtKB:P51648}; 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:0000250|UniProtKB:P51648}; 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:0000250|UniProtKB:P51648}; 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:0000250|UniProtKB:P51648}; 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:0000250|UniProtKB:P51648}; 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:0000250|UniProtKB:P51648}; 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:0000250|UniProtKB:P51648}; 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:0000250|UniProtKB:P51648}; 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:0000250|UniProtKB:P51648}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P51648}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:25286108}. Microsome CC membrane {ECO:0000250|UniProtKB:P51648}; Single-pass membrane protein CC {ECO:0000250|UniProtKB:P51648}. Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:P51648}; Single-pass membrane protein CC {ECO:0000250|UniProtKB:P51648}; Cytoplasmic side CC {ECO:0000250|UniProtKB:P30839}. 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; U14390; AAB06232.1; -; mRNA. DR EMBL; AK079639; BAC37712.1; -; mRNA. DR EMBL; AK140932; BAE24523.1; -; mRNA. DR EMBL; AK159246; BAE34928.1; -; mRNA. DR EMBL; AK163040; BAE37166.1; -; mRNA. DR EMBL; AK169157; BAE40936.1; -; mRNA. DR EMBL; AK170195; BAE41628.1; -; mRNA. DR EMBL; AL672172; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC003797; AAH03797.1; -; mRNA. DR CCDS; CCDS24809.1; -. DR RefSeq; NP_031463.2; NM_007437.5. DR AlphaFoldDB; P47740; -. DR SMR; P47740; -. DR BioGRID; 198066; 6. DR STRING; 10090.ENSMUSP00000073764; -. DR SwissLipids; SLP:000001741; -. DR iPTMnet; P47740; -. DR PhosphoSitePlus; P47740; -. DR SwissPalm; P47740; -. DR jPOST; P47740; -. DR PaxDb; 10090-ENSMUSP00000073764; -. DR ProteomicsDB; 282068; -. DR Pumba; P47740; -. DR Antibodypedia; 2232; 504 antibodies from 33 providers. DR DNASU; 11671; -. DR Ensembl; ENSMUST00000074127.14; ENSMUSP00000073764.8; ENSMUSG00000010025.20. DR GeneID; 11671; -. DR KEGG; mmu:11671; -. DR UCSC; uc007jhf.2; mouse. DR AGR; MGI:1353452; -. DR CTD; 224; -. DR MGI; MGI:1353452; Aldh3a2. DR VEuPathDB; HostDB:ENSMUSG00000010025; -. DR eggNOG; KOG2456; Eukaryota. DR GeneTree; ENSGT00940000157944; -. DR HOGENOM; CLU_005391_3_0_1; -. DR InParanoid; P47740; -. DR OMA; EIDWCKQ; -. DR OrthoDB; 606537at2759; -. DR TreeFam; TF314264; -. DR BRENDA; 1.2.1.3; 3474. DR Reactome; R-MMU-389599; Alpha-oxidation of phytanate. DR Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import. DR Reactome; R-MMU-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane. DR Reactome; R-MMU-9696270; RND2 GTPase cycle. DR Reactome; R-MMU-9696273; RND1 GTPase cycle. DR Reactome; R-MMU-9845614; Sphingolipid catabolism. DR BioGRID-ORCS; 11671; 1 hit in 81 CRISPR screens. DR ChiTaRS; Aldh3a2; mouse. DR PRO; PR:P47740; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; P47740; Protein. DR Bgee; ENSMUSG00000010025; Expressed in prostate gland ventral lobe and 255 other cell types or tissues. DR ExpressionAtlas; P47740; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; ISO:MGI. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:MGI. DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC. DR GO; GO:0050061; F:long-chain-aldehyde dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0052814; F:medium-chain-aldehyde dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central. DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW. DR GO; GO:0046292; P:formaldehyde metabolic process; ISO:MGI. DR GO; GO:0046458; P:hexadecanal metabolic process; ISS:UniProtKB. DR GO; GO:0000302; P:response to reactive oxygen species; ISO:MGI. DR CDD; cd07132; ALDH_F3AB; 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. PE 1: Evidence at protein level; KW Endoplasmic reticulum; Fatty acid metabolism; Lipid metabolism; Membrane; KW Microsome; NAD; Oxidoreductase; Phosphoprotein; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1..484 FT /note="Aldehyde dehydrogenase family 3 member A2" FT /id="PRO_0000056475" FT TOPO_DOM 1..463 FT /note="Cytoplasmic" FT TRANSMEM 464..484 FT /note="Helical" FT /evidence="ECO:0000255" FT MOTIF 481..484 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000250" FT ACT_SITE 207 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007" FT ACT_SITE 241 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008" 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:0000250|UniProtKB:P51648" FT CONFLICT 19 FT /note="P -> L (in Ref. 1; AAB06232)" FT /evidence="ECO:0000305" FT CONFLICT 229 FT /note="I -> V (in Ref. 1; AAB06232)" FT /evidence="ECO:0000305" FT CONFLICT 418 FT /note="T -> A (in Ref. 1; AAB06232)" FT /evidence="ECO:0000305" SQ SEQUENCE 484 AA; 53971 MW; DFC67C96C757832A CRC64; MERQVLRLRQ AFRSGRSRPL RFRLQQLEAL RRMVQEREKE ILAAIAADLS KSELNAYSHE VITILGEIDF MLGNLPELAS ARPAKKNLLT MMDEAYVQPE PLGVVLIIGA WNYPFVLTMQ PLVGAIAAGN AAIVKPSELS ENTAKILAEL LPQYLDQDLY AIVNGGIPET TELLKQRFDH ILYTGNTAVG KIVMEAAAKH LTPVTLELGG KSPCYIDRDC DLDVACRRIA WGKYMNCGQT CIAPDYILCE ASLQNQIVQK IKETVKDFYG ENIKASPDYE RIINLRHFKR LQSLLKGQKI AFGGEMDEAT RYLAPTILTD VDPNSKVMQE EIFGPILPIV SVKNVDEAIN FINDREKPLA LYVFSRNNKL IKRVIDETSS GGVTGNDVIM HFTVNSLPFG GVGASGMGAY HGKYSFDTFS HQRPCLLKGL KGESVNKLRY PPNSESKVSW AKFFLLKQFN KGRLGMLLFV CLVAVAAVIV KDQL //