ID AL1A3_RAT Reviewed; 512 AA. AC Q8K4D8; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 48. DE RecName: Full=Aldehyde dehydrogenase family 1 member A3; DE EC=1.2.1.5; DE AltName: Full=Aldehyde dehydrogenase 6; DE AltName: Full=Retinaldehyde dehydrogenase 3; DE Short=RALDH-3; GN Name=Aldh1a3; Synonyms=Aldh6, Raldh3; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; RX MEDLINE=22277966; PubMed=12390888; DOI=10.1095/biolreprod.102.007021; RA Rexer B.N., Ong D.E.; RT "A novel short-chain alcohol dehydrogenase from rats with retinol RT dehydrogenase activity, cyclically expressed in uterine epithelium."; RL Biol. Reprod. 67:1555-1564(2002). CC -!- FUNCTION: Recognizes as substrates free retinal and cellular CC retinol-binding protein-bound retinal. Seems to be the key enzyme CC in the formation of an RA gradient along the dorso-ventral axis CC during the early eye development and also in the development of CC the olfactory system (By similarity). CC -!- CATALYTIC ACTIVITY: An aldehyde + NAD(P)(+) + H(2)O = an acid + CC NAD(P)H. CC -!- PATHWAY: Cofactor metabolism; retinol metabolism. 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; AF434845; AAN03711.1; -; mRNA. DR IPI; IPI00203138; -. DR RefSeq; NP_695212.1; -. DR UniGene; Rn.8297; -. DR HSSP; P51977; 1BXS. DR Ensembl; ENSRNOG00000013028; Rattus norvegicus. DR GeneID; 266603; -. DR KEGG; rno:266603; -. DR RGD; 628662; Aldh1a3. DR HOVERGEN; Q8K4D8; -. DR BRENDA; 1.2.1.36; 248. DR BRENDA; 1.2.1.5; 248. DR NextBio; 624416; -. DR ArrayExpress; Q8K4D8; -. DR GermOnline; ENSRNOG00000013028; Rattus norvegicus. DR GO; GO:0005829; C:cytosol; NAS:RGD. DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IDA:RGD. DR GO; GO:0001822; P:kidney development; IEP:RGD. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0021983; P:pituitary gland development; IEP:RGD. DR GO; GO:0042493; P:response to drug; IEP:RGD. 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; FALSE_NEG. PE 2: Evidence at transcript level; KW Acetylation; Cytoplasm; NAD; Oxidoreductase. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 512 Aldehyde dehydrogenase family 1 member FT A3. FT /FTId=PRO_0000056480. FT NP_BIND 257 262 NAD (By similarity). FT ACT_SITE 280 280 Proton acceptor (By similarity). FT ACT_SITE 314 314 Nucleophile (By similarity). FT SITE 181 181 Transition state stabilizer (By FT similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). SQ SEQUENCE 512 AA; 56171 MW; 2A818D7472F67A5E CRC64; MATANGAVEN GQPDGKPPAL PRPIRNLEVK FTKIFINNDW HEPKSGRKFA TYNPSTLEKI CEVEEGDKPD VDKAVEAAQA AFQRGSPWRR LDALSRGQLL HQLADLIERD RAILATLETM DTGKPFLHAF FVDLEGCIKT FRYFAGWADK IQGRTIPTDD NVMCFTRHEP IGVCGAITPW NFPLLMLAWK LAPALCCGNT VVLKPAEQTP LTALYLASLI KEVGFPPGVV NIVPGFGPTV GAAISSHPQI NKIAFTGSTE VGKLVKEAAS RSNLKRVTLE LGGRNPCIVC ADADLDLAVE CAHQGVFFNQ GQCCTAASRV FVEEQVYGEF VRRSVEFAKK RPVGDPFDAK TEQGPQIDQK QFDKILELIE SGKKEGAKLE CGGSAMEDRG LFIKPTVFSD VTDNMRIAKE EIFGPVQPIL KFKNLEEVIK RANSTDYGLT AAVFTKNLDK ALKLASALES GTVWVNCYNA FYAQAPFGGF KMSGNGRELG EYALAEYTEV KTVTIKLDEK NP //