ID AL1A1_CHICK Reviewed; 509 AA. AC P27463; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 04-NOV-2008, entry version 62. 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 Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; OC Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Embryonic retina; RX MEDLINE=92217647; PubMed=1559558; DOI=10.1016/S0014-4835(05)80219-2; RA Godbout R.; RT "High levels of aldehyde dehydrogenase transcripts in the RT undifferentiated chick retina."; RL Exp. Eye Res. 54:297-305(1992). CC -!- FUNCTION: Binds free retinal and cellular retinol-binding protein- CC bound retinal. Can convert/oxidize retinaldehyde to retinoic acid CC (By similarity). CC -!- CATALYTIC ACTIVITY: Retinal + NAD(+) + H(2)O = retinoate + NADH. CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. 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; X58869; CAA41679.1; -; mRNA. DR PIR; S14629; S14629. DR RefSeq; NP_989908.1; -. DR UniGene; Gga.4119; -. DR HSSP; P51977; 1BXS. DR Ensembl; ENSGALG00000015147; Gallus gallus. DR GeneID; 395264; -. DR KEGG; gga:395264; -. DR HOVERGEN; P27463; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0001758; F:retinal dehydrogenase activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR016160; Ald_DHase_CS. DR InterPro; IPR016162; Ald_DHase_N. DR InterPro; IPR015590; Aldehyde_DHase. 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 1 509 Retinal dehydrogenase 1. FT /FTId=PRO_0000056421. FT NP_BIND 254 259 NAD (By similarity). FT ACT_SITE 277 277 Proton acceptor (By similarity). FT ACT_SITE 311 311 Nucleophile (By similarity). FT SITE 178 178 Transition state stabilizer (By FT similarity). SQ SEQUENCE 509 AA; 55809 MW; 7771181FA2F05DA9 CRC64; MKKQGSPSNP APVLPALPEP LKDLKIKYTK IFINNEWHDS VSGKKFEVFN PANEEKICEV AEGDKADIDK AVKAARKAFE LGSPWRTMDA SERGRLLNKL ADLVERDRLT LATMEAIDGG KLFSTAYLMD LGACIKTIRY CAGWADKIHG RTVPMDGNFF TFTRHEPVGV CGQIIPWNFP LVMFIWKIAP ALCCGNTVVV KPAEQTPLSA LYMGSLIKEA GFPPGVVNIV PGFGPTAGAA ISHHMDIDKV SFTGSTEVGK LIKEAAGKTN LKRVTLELGG KSPNIIFADA DLDEAAEFAH IGLFYHQGQC CIAGSRIFVE EPIYDEFVRR SIERAKKYTL GDPLLPGVQQ GPQIDKEQFQ KILDLIESGK KEGAKLECGG GPWGNKGYFI QPTVFSNVTD DMRIAKEEIF GPVQQIMKFK TIDEVIKRAN NTTYGLAAAV FTKDIDKALT FASALQAGTV WVNCYSAFSA QCPFGGFKMS GNGRELGEYG LQEYTEVKTV TIKIPQKNS //