ID AL1A1_MOUSE Reviewed; 501 AA. AC P24549; Q7TQJ0; Q811J0; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 5. DT 25-NOV-2008, entry version 90. 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; Synonyms=Ahd-2, Ahd2, Aldh1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=BALB/c, and C57BL/6; TISSUE=Liver; RX MEDLINE=91276281; PubMed=2055490; DOI=10.1016/0378-1119(91)90421-7; RA Rongnoparut P., Weaver S.; RT "Isolation and characterization of a cytosolic aldehyde dehydrogenase- RT encoding cDNA from mouse liver."; RL Gene 101:261-265(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=129/ReJ, BALB/c, and C57BL/6J; TISSUE=Liver; RX MEDLINE=95085815; PubMed=7993664; DOI=10.1006/bmmb.1994.1048; RA Bond S.L., Singh S.M.; RT "DNA sequence analysis of the cytosolic acetaldehyde dehydrogenase RT gene (Ahd-2) in mouse strains with variable ethanol preferences."; RL Biochem. Med. Metab. Biol. 52:155-159(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon, and Liver; 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 [4] RP PROTEIN SEQUENCE OF 23-52; 140-156; 211-230; 309-320; 330-349; RP 400-410; 421-435 AND 477-490. RC TISSUE=Embryonic retina; RX PubMed=1935685; RA McCaffery P., Tempst P., Lara G., Drager U.C.; RT "Aldehyde dehydrogenase is a positional marker in the retina."; RL Development 112:693-702(1991). CC -!- FUNCTION: In addition to the activity on acetaldehyde and related CC substrates, is also involved in the oxidation of aldehydes derived CC from biogenic amines such as epinephrine and norepinephrine, as CC well as the aldehydes generated via lipid peroxidation. Binds free CC retinal and cellular retinol-binding protein-bound retinal. Can CC convert/oxidize retinaldehyde to retinoic acid (By similarity). CC -!- CATALYTIC ACTIVITY: Retinal + NAD(+) + H(2)O = retinoate + NADH. CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed in the liver, lung, and testis. CC Apparently not expressed at detectable levels in kidney, stomach, CC ovary, heart, and brain. 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; M74570; AAA37202.1; -; mRNA. DR EMBL; M74571; AAA37203.1; -; Genomic_DNA. DR EMBL; S75713; AAB32754.2; -; mRNA. DR EMBL; S77047; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC044729; AAH44729.1; ALT_INIT; mRNA. DR EMBL; BC054386; AAH54386.1; -; mRNA. DR PIR; JQ1004; JQ1004. DR RefSeq; NP_038495.2; -. DR UniGene; Mm.457973; -. DR HSSP; P51977; 1BXS. DR PhosphoSite; P24549; -. DR SWISS-2DPAGE; P24549; -. DR REPRODUCTION-2DPAGE; P24549; -. DR Ensembl; ENSMUSG00000053279; Mus musculus. DR GeneID; 11668; -. DR KEGG; mmu:11668; -. DR MGI; MGI:1353450; Aldh1a1. DR HOGENOM; P24549; -. DR HOVERGEN; P24549; -. DR NextBio; 279287; -. DR ArrayExpress; P24549; -. DR CleanEx; MM_ALDH1A1; -. DR GermOnline; ENSMUSG00000053279; Mus musculus. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; IDA:MGI. DR GO; GO:0001758; F:retinal dehydrogenase activity; IEA:EC. DR GO; GO:0048048; P:embryonic eye morphogenesis; IGI:MGI. DR GO; GO:0002072; P:optic cup morphogenesis involved in camera-...; IGI:MGI. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0043065; P:positive regulation of apoptosis; IGI:MGI. DR GO; GO:0042573; P:retinoic acid metabolic process; IMP:MGI. DR GO; GO:0042572; P:retinol metabolic process; IMP:MGI. 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 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; NAD; KW Oxidoreductase. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 501 Retinal dehydrogenase 1. FT /FTId=PRO_0000056417. FT NP_BIND 246 251 NAD (By similarity). FT REGION 300 305 Antabuse binding. FT ACT_SITE 269 269 Proton acceptor (By similarity). FT ACT_SITE 303 303 Nucleophile (By similarity). FT SITE 170 170 Transition state stabilizer (By FT similarity). FT MOD_RES 2 2 N-acetylserine (By similarity). FT CONFLICT 8 8 A -> R (in Ref. 1; AAA37202/AAA37203). FT CONFLICT 45 45 T -> S (in Ref. 2; AAB32754). FT CONFLICT 51 51 H -> Q (in Ref. 2; AAB32754). FT CONFLICT 87 87 R -> C (in Ref. 1; AAA37202). FT CONFLICT 140 140 I -> Y (in Ref. 4; AA sequence). FT CONFLICT 458 458 M -> I (in Ref. 1; AAA37202). SQ SEQUENCE 501 AA; 54468 MW; 0E428151B799BD1D CRC64; MSSPAQPAVP APLADLKIQH TKIFINNEWH NSVSGKKFPV LNPATEEVIC HVEEGDKADV DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLMERDR LLLATMEALN GGKVFANAYL SDLGGCIKAL KYCAGWADKI HGQTIPSDGD IFTYTRREPI GVCGQIIPWN FPMLMFIWKI GPALSCGNTV VVKPAEQTPL TALHLASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD KVAFTGSTQV GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDIAVEF AHHGVFYHQG QCCVAASRIF VEESVYDEFV KRSVERAKKY VLGNPLTPGI NQGPQIDKEQ HDKILDLIES GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSVDDVIKR ANNTTYGLAA GLFTKDLDKA ITVSSALQAG VVWVNCYMML SAQCPFGGFK MSGNGRELGE HGLYEYTELK TVAMKISQKN S //