ID   AL1A1_RAT               Reviewed;         501 AA.
AC   P51647; O09184;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 73.
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=Aldh;
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; TISSUE=Kidney;
RX   MEDLINE=96125208; PubMed=8543180; DOI=10.1016/0378-1119(96)81752-5;
RA   Bhat P.V., Labrecque J., Boutin J.-M., Lacroix A., Yoshida A.;
RT   "Cloning of a cDNA encoding rat aldehyde dehydrogenase with high
RT   activity for retinal oxidation.";
RL   Gene 166:303-306(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   MEDLINE=97212790; PubMed=9059608;
RA   Kathmann E.C., Lipsky J.J.;
RT   "A preliminary report on the cloning of a constitutively expressed rat
RT   liver cytosolic ALDH cDNA by PCR.";
RL   Adv. Exp. Med. Biol. 414:69-72(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   MEDLINE=97382470; PubMed=9240474; DOI=10.1006/bbrc.1997.6998;
RA   Kathmann E.C., Lipsky J.J.;
RT   "Cloning of a cDNA encoding a constitutively expressed rat liver
RT   cytosolic aldehyde dehydrogenase.";
RL   Biochem. Biophys. Res. Commun. 236:527-531(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Napoli J.L., Penzes P., Wang X., Sperkova Z.;
RT   "Cloning of a rat cDNA encoding retinal dehydrogenase isozyme type I
RT   and its expression in E. coli.";
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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   [6]
RP   PROTEIN SEQUENCE OF 2-19; 80-91; 96-121; 205-225; 237-258 AND 394-438.
RC   STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX   MEDLINE=95134257; PubMed=7832787;
RA   Labrecque J., Dumas F., Lacroix A., Bhat P.V.;
RT   "A novel isoenzyme of aldehyde dehydrogenase specifically involved in
RT   the biosynthesis of 9-cis and all-trans retinoic acid.";
RL   Biochem. J. 305:681-684(1995).
CC   -!- FUNCTION: Is capable of converting 9-cis and all-trans retinal to
CC       corresponding retinoic acid with high efficiency, 9-cis retinal
CC       being 2-fold more active than all-trans retinal.
CC   -!- CATALYTIC ACTIVITY: Retinal + NAD(+) + H(2)O = retinoate + NADH.
CC   -!- ENZYME REGULATION: Inhibited by chloral hydrate.
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in kidney, lung, testis,
CC       intestine, stomach, and trachea, but weakly in the liver.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; L42009; AAA96657.1; -; mRNA.
DR   EMBL; AF001896; AAC53304.1; -; mRNA.
DR   EMBL; AF001898; AAC53306.1; -; mRNA.
DR   EMBL; AF001897; AAC53305.1; -; mRNA.
DR   EMBL; U79118; AAB63423.1; -; mRNA.
DR   EMBL; BC061526; AAH61526.1; -; mRNA.
DR   IPI; IPI00332042; -.
DR   PIR; JC4524; JC4524.
DR   PIR; JC5553; JC5553.
DR   RefSeq; NP_071852.2; -.
DR   UniGene; Rn.6132; -.
DR   HSSP; P51977; 1BXS.
DR   PRIDE; P51647; -.
DR   Ensembl; ENSRNOG00000017619; Rattus norvegicus.
DR   GeneID; 24188; -.
DR   KEGG; rno:24188; -.
DR   RGD; 2087; Aldh1a1.
DR   HOVERGEN; P51647; -.
DR   BRENDA; 1.2.1.36; 248.
DR   NextBio; 602555; -.
DR   ArrayExpress; P51647; -.
DR   GermOnline; ENSRNOG00000017619; Rattus norvegicus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005625; C:soluble fraction; IDA:RGD.
DR   GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; TAS:RGD.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IDA:RGD.
DR   GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR   GO; GO:0001758; F:retinal dehydrogenase activity; IDA:RGD.
DR   GO; GO:0042905; P:9-cis-retinoic acid metabolic process; IDA:RGD.
DR   GO; GO:0060206; P:estrous cycle phase; IEP:RGD.
DR   GO; GO:0001822; P:kidney development; IEP:RGD.
DR   GO; GO:0001889; P:liver development; IEP:RGD.
DR   GO; GO:0007494; P:midgut development; IEP:RGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:RGD.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0032355; P:response to estradiol stimulus; IEP:RGD.
DR   GO; GO:0045471; P:response to ethanol; IDA:RGD.
DR   GO; GO:0014070; P:response to organic cyclic substance; IEP:RGD.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
DR   GO; GO:0032526; P:response to retinoic acid; 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; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; NAD;
KW   Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    501       Retinal dehydrogenase 1.
FT                                /FTId=PRO_0000056419.
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 (Probable).
FT   CONFLICT    100    100       R -> C (in Ref. 1; AAA96657).
FT   CONFLICT    106    106       I -> M (in Ref. 6; AA sequence).
FT   CONFLICT    170    170       N -> E (in Ref. 1; AAA96657).
SQ   SEQUENCE   501 AA;  54459 MW;  A3614C21BCE7E144 CRC64;
     MSSPAQPAVP APLANLKIQH TKIFINNEWH DSVSGKKFPV LNPATEEVIC HVEEGDKADV
     DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLMERDR LLLATIEAIN GGKVFANAYL
     SDLGGSIKAL KYCAGWADKI HGQTIPSDGD IFTFTRREPI GVCGQIIPWN FPLLMFIWKI
     GPALSCGNTV VVKPAEQTPL TALHMASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD
     KVAFTGSTQV GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDIAVEF AHHGVFYHQG
     QCCVAASRIF VEESVYDEFV RKSVERAKKY VLGNPLTQGI NQGPQIDKEQ HDKILDLIES
     GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSIDDVIKR
     ANNTTYGLAA GVFTKDLDRA ITVSSALQAG VVWVNCYMIL SAQCPFGGFK MSGNGRELGE
     HGLYEYTELK TVAMKISQKN S
//