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 25-OCT-2017, entry version 142. DE RecName: Full=Fatty aldehyde dehydrogenase; DE EC=1.2.1.3 {ECO:0000269|PubMed:25286108}; DE AltName: Full=Aldehyde dehydrogenase 3; DE AltName: Full=Aldehyde dehydrogenase family 3 member A2; GN Name=Aldh3a2; Synonyms=Ahd-3, Ahd3, Aldh3, Aldh4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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; RC 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the 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 RT project: 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, RC Pancreas, 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 RT 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 RT via two C-terminal tryptophan residues and lipid modification."; RL Biochem. J. 465:79-87(2015). CC -!- FUNCTION: Catalyzes the oxidation of long-chain aliphatic CC aldehydes to fatty acids (PubMed:25286108). Responsible for CC conversion of the sphingosine 1-phosphate (S1P) degradation CC product hexadecenal to hexadecenoic acid (By similarity). CC {ECO:0000250|UniProtKB:P51648, ECO:0000269|PubMed:25286108}. CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = a carboxylate + CC NADH. {ECO:0000269|PubMed:25286108}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:P30839}; Single-pass membrane protein CC {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P30839}. CC Membrane {ECO:0000269|PubMed:25286108}; Single-pass membrane CC protein {ECO:0000255}. 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; CAI24063.1; -; Genomic_DNA. DR EMBL; BC003797; AAH03797.1; -; mRNA. DR CCDS; CCDS24809.1; -. DR RefSeq; NP_031463.2; NM_007437.5. DR UniGene; Mm.398221; -. DR ProteinModelPortal; P47740; -. DR SMR; P47740; -. DR IntAct; P47740; 4. DR MINT; MINT-4087555; -. DR STRING; 10090.ENSMUSP00000073764; -. DR SwissLipids; SLP:000001741; -. DR iPTMnet; P47740; -. DR PhosphoSitePlus; P47740; -. DR SwissPalm; P47740; -. DR EPD; P47740; -. DR MaxQB; P47740; -. DR PaxDb; P47740; -. DR PRIDE; P47740; -. DR Ensembl; ENSMUST00000074127; ENSMUSP00000073764; ENSMUSG00000010025. DR GeneID; 11671; -. DR KEGG; mmu:11671; -. DR UCSC; uc007jhf.2; mouse. DR CTD; 224; -. DR MGI; MGI:1353452; Aldh3a2. DR eggNOG; KOG2456; Eukaryota. DR eggNOG; COG1012; LUCA. DR GeneTree; ENSGT00390000002825; -. DR HOGENOM; HOG000271515; -. DR HOVERGEN; HBG050483; -. DR InParanoid; P47740; -. DR KO; K00128; -. DR TreeFam; TF314264; -. DR BRENDA; 1.2.1.3; 3474. DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis. DR Reactome; R-MMU-389599; Alpha-oxidation of phytanate. DR ChiTaRS; Aldh3a2; mouse. DR PRO; PR:P47740; -. DR Proteomes; UP000000589; Chromosome 11. DR Bgee; ENSMUSG00000010025; -. DR CleanEx; MM_ALDH3A2; -. DR ExpressionAtlas; P47740; baseline and differential. DR Genevisible; P47740; MM. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0016021; C:integral component of membrane; IDA:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005777; C:peroxisome; ISO:MGI. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IDA:MGI. DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro. DR GO; GO:0046577; F:long-chain-alcohol oxidase activity; ISO:MGI. DR GO; GO:0050061; F:long-chain-aldehyde dehydrogenase activity; ISO:MGI. DR GO; GO:0052814; F:medium-chain-aldehyde dehydrogenase activity; ISO:MGI. DR GO; GO:0006081; P:cellular aldehyde metabolic process; ISO:MGI. DR GO; GO:0007417; P:central nervous system development; ISO:MGI. DR GO; GO:0008544; P:epidermis development; ISO:MGI. DR GO; GO:0055114; P:oxidation-reduction process; ISO:MGI. DR GO; GO:0007422; P:peripheral nervous system development; ISO:MGI. DR GO; GO:0033306; P:phytol metabolic process; ISO:MGI. DR GO; GO:0006714; P:sesquiterpenoid metabolic process; ISO:MGI. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. 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 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 Complete proteome; Endoplasmic reticulum; Membrane; NAD; KW Oxidoreductase; Phosphoprotein; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 484 Fatty aldehyde dehydrogenase. FT /FTId=PRO_0000056475. FT TOPO_DOM 1 463 Cytoplasmic. FT TRANSMEM 464 480 Helical. {ECO:0000255}. FT NP_BIND 185 190 NAD. {ECO:0000255}. FT MOTIF 481 484 Prevents secretion from ER. FT {ECO:0000250}. FT ACT_SITE 207 207 {ECO:0000255|PROSITE-ProRule:PRU10007}. FT ACT_SITE 241 241 {ECO:0000255|PROSITE-ProRule:PRU10008}. FT MOD_RES 293 293 Phosphoserine. FT {ECO:0000250|UniProtKB:P51648}. FT CONFLICT 19 19 P -> L (in Ref. 1; AAB06232). FT {ECO:0000305}. FT CONFLICT 229 229 I -> V (in Ref. 1; AAB06232). FT {ECO:0000305}. FT CONFLICT 418 418 T -> A (in Ref. 1; AAB06232). FT {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 //