ID ALDH2_PIG Reviewed; 521 AA. AC Q2XQV4; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=Aldehyde dehydrogenase, mitochondrial; DE EC=1.2.1.3; DE AltName: Full=ALDH class 2; DE AltName: Full=ALDH-E2; DE Flags: Precursor; GN Name=ALDH2; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Ji Y., Bennett B.M.; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Required for clearance of cellular formaldehyde, a cytotoxic CC and carcinogenic metabolite that induces DNA damage. CC {ECO:0000250|UniProtKB:P05091}. 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 -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: CC step 2/2. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. 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; DQ266356; ABB70228.1; -; mRNA. DR RefSeq; NP_001038076.1; NM_001044611.2. DR AlphaFoldDB; Q2XQV4; -. DR SMR; Q2XQV4; -. DR STRING; 9823.ENSSSCP00000010556; -. DR PaxDb; 9823-ENSSSCP00000010556; -. DR PeptideAtlas; Q2XQV4; -. DR Ensembl; ENSSSCT00000055390.2; ENSSSCP00000053451.1; ENSSSCG00000009889.5. DR Ensembl; ENSSSCT00025069501.1; ENSSSCP00025029933.1; ENSSSCG00025050497.1. DR Ensembl; ENSSSCT00035044779.1; ENSSSCP00035017930.1; ENSSSCG00035033776.1. DR Ensembl; ENSSSCT00040009144.1; ENSSSCP00040003586.1; ENSSSCG00040006895.1. DR Ensembl; ENSSSCT00045006276.1; ENSSSCP00045004257.1; ENSSSCG00045003770.1. DR Ensembl; ENSSSCT00055023290.1; ENSSSCP00055018413.1; ENSSSCG00055011877.1. DR Ensembl; ENSSSCT00060076086.1; ENSSSCP00060032896.1; ENSSSCG00060055813.1. DR Ensembl; ENSSSCT00065034412.1; ENSSSCP00065014281.1; ENSSSCG00065025693.1. DR Ensembl; ENSSSCT00070014826.1; ENSSSCP00070012258.1; ENSSSCG00070007644.1. DR GeneID; 733685; -. DR KEGG; ssc:733685; -. DR CTD; 217; -. DR VGNC; VGNC:106442; ALDH2. DR eggNOG; KOG2450; Eukaryota. DR GeneTree; ENSGT00940000156240; -. DR HOGENOM; CLU_005391_0_1_1; -. DR InParanoid; Q2XQV4; -. DR OMA; HGIGYYP; -. DR OrthoDB; 2291791at2759; -. DR TreeFam; TF300455; -. DR Reactome; R-SSC-380612; Metabolism of serotonin. DR Reactome; R-SSC-445355; Smooth Muscle Contraction. DR Reactome; R-SSC-71384; Ethanol oxidation. DR UniPathway; UPA00780; UER00768. DR Proteomes; UP000008227; Chromosome 14. DR Proteomes; UP000314985; Chromosome 14. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR Bgee; ENSSSCG00000009889; Expressed in liver and 47 other cell types or tissues. DR ExpressionAtlas; Q2XQV4; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0106435; F:carboxylesterase activity; ISS:UniProtKB. DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC. DR GO; GO:0018547; F:nitroglycerin reductase activity; ISS:UniProtKB. DR GO; GO:0008957; F:phenylacetaldehyde dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0046185; P:aldehyde catabolic process; ISS:UniProtKB. DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:1903179; P:regulation of dopamine biosynthetic process; ISS:UniProtKB. DR GO; GO:1905627; P:regulation of serotonin biosynthetic process; ISS:UniProtKB. DR CDD; cd07141; ALDH_F1AB_F2_RALDH1; 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 PANTHER; PTHR11699:SF233; ALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. DR Genevisible; Q2XQV4; SS. PE 2: Evidence at transcript level; KW Acetylation; Mitochondrion; NAD; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1..21 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 22..521 FT /note="Aldehyde dehydrogenase, mitochondrial" FT /id="PRO_0000312492" FT ACT_SITE 289 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, FT ECO:0000255|PROSITE-ProRule:PRU10008" FT ACT_SITE 323 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, FT ECO:0000255|PROSITE-ProRule:PRU10008" FT BINDING 266..271 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT SITE 190 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P20000" FT MOD_RES 56 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 77 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 163 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 372 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 379 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 387 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 430 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 432 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 445 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" FT MOD_RES 455 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P47738" SQ SEQUENCE 521 AA; 56921 MW; 12913E10ECD560A7 CRC64; MLRPAALAAA RLVLRQGRRL LSAAPTQAVP APNQQPEIFY NQIFINNEWH DAISKKTFPT VNPSTGDVIC HVAEGDKEDV DRAVEAARAA FQLGSPWRRL DASDRGRLLN RLADLIERDR TYLAALETLD NGKPYVISYL VDLDMVLKCL RYYAGWADKY HGKTLPIDGD YFSYTRHEPV GVCGQIIPWN FPLLMQAWKL GPALATGNVV VMKVSEQTPL TALYVANLIK EAGFPPGVVN IVPGYGPTAG AAIASHEDVD KVAFTGSTEV GHLIQVAAGK SNLKRVTLEL GGKSPNIIMS DADMDWAVEQ AHFALFFNQG QCCCAGSRTF VQEDIYAEFV ERSVARARSR VVGNPFDSRT EQGPQIDETQ FKKILGYIKS GKEEGAKLLC GGGAAADRGY FIQPTVFGDV QDGMTIAKEE IFGPVMQILK FKTIEEVIGR ANNSKYGLAA AVFTKDLDKA NYLSQALQAG TVWVNCYDVF GAQSPFGGYK LSGSGRELGE YGLQAYTEVK TVTVKVPQKN S //