ID AL1A1_RABIT Reviewed; 496 AA. AC Q8MI17; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 39. DE RecName: Full=Retinal dehydrogenase 1; DE Short=RALDH 1; DE Short=RalDH1; DE EC=1.2.1.36; DE AltName: Full=Aldehyde dehydrogenase family 1 member A1; DE AltName: Full=Aldehyde dehydrogenase, cytosolic; DE AltName: Full=ALHDII; DE AltName: Full=ALDH-E1; GN Name=ALDH1A1; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cornea; RX PubMed=12941160; DOI=10.1089/104454903322216671; RA Manzer R., Qamar L., Estey T., Pappa A., Petersen D.R., Vasiliou V.; RT "Molecular cloning and baculovirus expression of the rabbit corneal RT aldehyde dehydrogenase (ALDH1A1) cDNA."; RL DNA Cell Biol. 22:329-338(2003). CC -!- FUNCTION: Can convert/oxidize retinaldehyde to retinoic acid (By CC similarity). CC -!- CATALYTIC ACTIVITY: Retinal + NAD(+) + H(2)O = retinoate + NADH. CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). 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; AY038801; AAK72097.1; -; mRNA. DR UniGene; Ocu.1307; -. DR HSSP; P51977; 1BXS. DR HOVERGEN; Q8MI17; -. DR BRENDA; 1.2.1.36; 255. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0001758; F:retinal dehydrogenase activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH. DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 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 1 496 Retinal dehydrogenase 1. FT /FTId=PRO_0000056418. FT NP_BIND 241 246 NAD (By similarity). FT ACT_SITE 264 264 Proton acceptor (By similarity). FT ACT_SITE 298 298 Nucleophile (By similarity). FT SITE 165 165 Transition state stabilizer (By FT similarity). SQ SEQUENCE 496 AA; 54341 MW; 4BD963CF015FD164 CRC64; MADLPTPLTN LKIQYTKIFI NNEWHDSVSG KKFPVLNPAT EEQICLIEEG DKADVDKAVK AARQAFQIGS PWRTMDASER GRLLYKLADL IERDRLLLAT MESLNAGKLF PNAYLMDLGG CIKTLRYCAG WADKIQGRTM PMDGDFFCYT RHEPVGVCGQ IIPWNFPLVM LIWKIGPALS CGNTVIVKPA EQTPLTALHV ASLIKEAGFP PGVVNIVPGY GPTAGAAISS HMDIDKVAFT GSTEVGKLIK EAAGKSNLKR VTLELGGKSP CIVFADADLD NAVEFAHQGV FYHQGQCCIA ASRLFVEESI YDEFVRRSVE RAKKYVLGNP LAPEVNQGPQ IDKEQYNKIL DLIESGKKEG AKLECGGGPW GNKGYFIQPT VFSNVTDEMR IAKEEIFGPV QQIMKFKSLD DVIKRANNTT YGLSAGIFTK DLDKAVTVSS ALQAGTVWVN CYSVVSAQVP FGGFKMSGNG RELGEYGLQQ YTEVKTVTVK ISQKNS //