ID ALDH2_MACPR Reviewed; 240 AA. AC Q29491; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 49. DE RecName: Full=Aldehyde dehydrogenase, cytosolic 2; DE EC=1.2.1.3; DE AltName: Full=ALDH class 1; DE AltName: Full=Non-lens ALDH1; DE AltName: Full=ALDH1-NL; DE Flags: Fragment; OS Macroscelides proboscideus (Short-eared elephant shrew). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Macroscelidea; Macroscelididae; OC Macroscelides. OX NCBI_TaxID=29082; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=96279083; PubMed=8663049; DOI=10.1074/jbc.271.26.15623; RA Graham C., Hodin J., Wistow G.; RT "A retinaldehyde dehydrogenase as a structural protein in a mammalian RT eye lens. Gene recruitment of eta-crystallin."; RL J. Biol. Chem. 271:15623-15628(1996). CC -!- FUNCTION: Elephant shrews, in contrast to other mammals, possess CC both a lens- and a non-lens specific class-1 aldehyde CC dehydrogenase. Can convert/oxidize retinaldehyde to retinoic acid. CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = an acid + NADH. CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from CC ethanol: step 2/2. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Non-lens specific, predominant form expressed CC in the liver. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U40486; AAC48589.1; -; mRNA. DR HSSP; P51977; 1BXS. DR SMR; Q29491; 1-240. DR HOVERGEN; Q29491; -. DR BRENDA; 1.2.1.3; 317919. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR015590; Aldehyde_DH. DR Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1. DR PANTHER; PTHR11699; Aldehyde_dehyd; 1. DR Pfam; PF00171; Aldedh; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 2: Evidence at transcript level; KW Cytoplasm; NAD; Oxidoreductase. FT CHAIN <1 240 Aldehyde dehydrogenase, cytosolic 2. FT /FTId=PRO_0000056429. FT ACT_SITE 8 8 Potential. FT ACT_SITE 42 42 Potential. FT NON_TER 1 1 SQ SEQUENCE 240 AA; 26515 MW; 9E34DC9B4D5153A9 CRC64; NLKRVTLELG GKSPCIVFAD ADLDNAVEFA HRGLFFHQGQ CCVAASRLFV EESIYDEFVR RSVERAKKYV LGNPLTPGVS QGPQIDKEQY DKIIDLIESG KKEGAKLECG GGPWGNKGYF IQPTVFSNVT DEMRIAKEEI FGPVQQIMKF KSLDEVIKRA NNTFYGLAAG VFTKDLDKAV TVSAALQAGT VWVNCYMANS VQCPFGGFKM SGNGRELGEY GLHEYTEVKT VTMKISKKNS //