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 03-APR-2013, entry version 103.
DE RecName: Full=Retinal dehydrogenase 1;
DE Short=RALDH 1;
DE Short=RalDH1;
DE EC=1.2.1.36;
DE AltName: Full=ALDH-E1;
DE AltName: Full=ALHDII;
DE AltName: Full=Aldehyde dehydrogenase family 1 member A1;
DE AltName: Full=Aldehyde dehydrogenase, cytosolic;
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 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 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 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 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; NM_022407.3.
DR UniGene; Rn.6132; -.
DR ProteinModelPortal; P51647; -.
DR SMR; P51647; 9-501.
DR PhosphoSite; P51647; -.
DR PaxDb; P51647; -.
DR PRIDE; P51647; -.
DR Ensembl; ENSRNOT00000024000; ENSRNOP00000024000; ENSRNOG00000017619.
DR GeneID; 24188; -.
DR KEGG; rno:24188; -.
DR UCSC; RGD:2087; rat.
DR CTD; 216; -.
DR RGD; 2087; Aldh1a1.
DR eggNOG; COG1012; -.
DR GeneTree; ENSGT00550000074289; -.
DR HOGENOM; HOG000271505; -.
DR HOVERGEN; HBG000097; -.
DR KO; K07249; -.
DR OrthoDB; EOG4Z8XW6; -.
DR BRENDA; 1.2.1.36; 5301.
DR SABIO-RK; P51647; -.
DR UniPathway; UPA00912; -.
DR BindingDB; P51647; -.
DR ChEMBL; CHEMBL2931; -.
DR NextBio; 602555; -.
DR Genevestigator; P51647; -.
DR GermOnline; ENSRNOG00000017619; Rattus norvegicus.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; TAS: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:0042904; P:9-cis-retinoic acid biosynthetic process; IEA:Compara.
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:0002072; P:optic cup morphogenesis involved in camera-type eye development; IEA:Compara.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Compara.
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:0006979; P:response to oxidative stress; IMP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; IMP:RGD.
DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW NAD; Oxidoreductase; Reference proteome.
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 BINDING 456 456 NAD (By similarity).
FT SITE 170 170 Transition state stabilizer (By
FT similarity).
FT MOD_RES 2 2 N-acetylserine (Probable).
FT MOD_RES 91 91 N6-acetyllysine (By similarity).
FT MOD_RES 128 128 N6-acetyllysine (By similarity).
FT MOD_RES 252 252 N6-acetyllysine (By similarity).
FT MOD_RES 353 353 N6-acetyllysine (By similarity).
FT MOD_RES 367 367 N6-acetyllysine (By similarity).
FT MOD_RES 410 410 N6-acetyllysine (By similarity).
FT MOD_RES 419 419 N6-acetyllysine (By similarity).
FT MOD_RES 435 435 N6-acetyllysine (By similarity).
FT MOD_RES 495 495 N6-acetyllysine (By similarity).
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
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