ID   AL1A1_MACFA             Reviewed;         501 AA.
AC   Q8HYE4;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 40.
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   Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney proximal tubule;
RX   PubMed=12576512; DOI=10.1194/jlr.M200359-JLR200;
RA   Brodeur H., Gagnon I., Mader S., Bhat P.V.;
RT   "Cloning of monkey RALDH1 and characterization of retinoid metabolism
RT   in monkey kidney proximal tubule cells.";
RL   J. Lipid Res. 44:303-313(2003).
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; AF542418; AAN85861.1; -; mRNA.
DR   HSSP; P51977; 1BXS.
DR   HOVERGEN; Q8HYE4; -.
DR   BRENDA; 1.2.1.36; 3438.
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   Acetylation; Cytoplasm; NAD; Oxidoreductase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    501       Retinal dehydrogenase 1.
FT                                /FTId=PRO_0000056416.
FT   NP_BIND     246    251       NAD (By similarity).
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).
SQ   SEQUENCE   501 AA;  54736 MW;  E3864A9190BBD6B2 CRC64;
     MSSSGTSDLP VLPTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKADV
     DKAVKAARQA FQIGSPWRTM DASERGRLLY KLADLIERDR LLLATMESMN GGKLYSNAYL
     NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKI
     GPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID
     KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG
     QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGA TQGPQIDKEQ YDKILDLIES
     GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR
     ANNTFYGLSA GVFTNDIDKA VTISSALQAG TVWVNCYGVV TAQCPFGGFK MSGNGRELGE
     YGFHEYTEVK TVTVKISQKN S
//