ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P00352


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name AL1A1_HUMAN
Primary accession number P00352
Secondary accession number O00768
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 98)
Name and origin of the protein
Protein name Retinal dehydrogenase 1
Synonyms RALDH 1
RalDH1
EC 1.2.1.36
Aldehyde dehydrogenase family 1 member A1
Aldehyde dehydrogenase, cytosolic
ALHDII
ALDH-E1
Gene name
Name: ALDH1A1
Synonyms: ALDC, ALDH1, PUMB1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0888-7543(89)90127-4; PubMed=2591967 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu L.C., Chang W.-C., Yoshida A.;
"Genomic structure of the human cytosolic aldehyde dehydrogenase gene.";
Genomics 5:857-865(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8214422 [NCBI, ExPASy, EBI, Israel, Japan]
Zheng C.F., Wang T.T., Weiner H.;
"Cloning and expression of the full-length cDNAS encoding human liver class 1 and class 2 aldehyde dehydrogenase.";
Alcohol. Clin. Exp. Res. 17:828-831(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lens;
Ramana K.V., Xiao T., Ansari N.H.;
"Cloning and expression of aldehyde dehydrogenase 1 (ALDH1A1) from human lens cDNA library.";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-177.
Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
PubMed=8493914 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida A., Hsu L.C., Yanagawa Y.;
"Biological role of human cytosolic aldehyde dehydrogenase 1: hormonal response, retinal oxidation and implication in testicular feminization.";
Adv. Exp. Med. Biol. 328:37-44(1993).
[8]
PROTEIN SEQUENCE OF 2-501, AND ACETYLATION AT SER-2.
TISSUE=Liver;
PubMed=6723659 [NCBI, ExPASy, EBI, Israel, Japan]
Hempel J., von Bahr-Lindstroem H., Joernvall H.;
"Aldehyde dehydrogenase from human liver. Primary structure of the cytoplasmic isoenzyme.";
Eur. J. Biochem. 141:21-35(1984).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
DOI=10.1016/0741-8329(85)90024-2; PubMed=4015823 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida A., Ikawa M., Hsu L.C., Tani K.;
"Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases.";
Alcohol 2:103-106(1985).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
TISSUE=Liver;
PubMed=2987944 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu L.C., Tani K., Fujiyoshi T., Kurachi K., Yoshida A.;
"Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2.";
Proc. Natl. Acad. Sci. U.S.A. 82:3771-3775(1985).
[11]
PROTEIN SEQUENCE OF 266-273, ACTIVE SITES GLU-269 AND CYS-303, AND NAD-BINDING SITE CYS-456.
DOI=10.1021/bi00392a015; PubMed=3676276 [NCBI, ExPASy, EBI, Israel, Japan]
Abriola D.P., Fields R., Stein S., Mackerell A.D. Jr., Pietruszko R.;
"Active site of human liver aldehyde dehydrogenase.";
Biochemistry 26:5679-5684(1987).
[12]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Erythrocyte;
PubMed=2776714 [NCBI, ExPASy, EBI, Israel, Japan]
Agarwal D.P., Cohn P., Goedde H.W., Hempel J.;
"Aldehyde dehydrogenase from human erythrocytes: structural relationship to the liver cytosolic isozyme.";
Enzyme 42:47-52(1989).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M31994; AAA51692.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M31982; AAA51692.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M31983; AAA51692.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M31984; AAA51692.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M31985; AAA51692.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M31986; AAA51692.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M31987; AAA51692.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M31988; AAA51692.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M31989; AAA51692.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M31990; AAA51692.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M31991; AAA51692.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M31992; AAA51692.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF003341; AAC51652.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY390731; AAR92229.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006921; AAP35567.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY338497; AAP88039.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001505; AAH01505.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S61235; AAD13925.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M26761; AAA35518.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K03000; AAA51695.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A33371; DEHUE1.
RefSeq NP_000680.2; -.
UniGene Hs.76392
3D structure databases
HSSP P51977; 1BXS. [HSSP ENTRY / PDB]
SMR P00352; 22-501.
ModBase P00352.
PTM databases
PhosphoSite P00352; -.
Enzyme and pathway databases
Reactome REACT_2063; Metabolism of xenobiotics.
Polymorphism databases
NIEHS-SNPs ALDH1A1.
2D gel databases
SWISS-2DPAGE P00352; -.
Cornea-2DPAGE P00352; -.
DOSAC-COBS-2DPAGE P00352; -.
REPRODUCTION-2DPAGE IPI00218914; -.
P00352; -.
Organism-specific databases
H-InvDB HIX0008099; -.
HGNC HGNC:402; ALDH1A1.
GenAtlas ALDH1A1.
HPA HPA002123; -.
MIM 100640; gene. [NCBI / EBI]
PharmGKB PA24692; -.
GeneCards P00352.
Gene expression databases
ArrayExpress P00352; -.
CleanEx HS_ALDH1A1; -.
GermOnline ENSG00000165092; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0004029; Molecular function: aldehyde dehydrogenase (NAD) activity (traceable author statement from ProtInc).
GO:0005497; Molecular function: androgen binding (traceable author statement from ProtInc).
GO:0005099; Molecular function: Ras GTPase activator activity (traceable author statement from UniProtKB).
GO:0006081; Biological process: cellular aldehyde metabolic process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
BLOCKS P00352.
Proteomic databases
PeptideAtlas P00352; -.
Genome annotation databases
Ensembl ENSG00000165092; Homo sapiens. [Contig view]
GeneID 216; -.
KEGG hsa:216; -.
Phylogenomic databases
HOGENOM P00352; -.
HOVERGEN P00352; -.
Other
DrugBank DB00157; NADH.
DB00755; Tretinoin.
DB00162; Vitamin A.
SOURCE ALDH1A1; Homo sapiens.
ProtoNet P00352.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   501  500     Retinal dehydrogenase 1. PRO_0000056415
NP_BIND   246   251  6     NAD (By similarity). 
ACT_SITE   269   269        Proton acceptor. 
ACT_SITE   303   303        Nucleophile. 
BINDING   456   456        NAD. 
SITE   170   170  1     Transition state stabilizer (By similarity). 
MOD_RES   2     2        N-acetylserine. 
VARIANT   177   177  1     I -> F (in dbSNP:rs8187929 [NCBI]). VAR_017778 [3D]
CONFLICT   121   121        N -> S (in Ref. 2; AAC51652). 
CONFLICT   162   162        V -> I (in Ref. 9 and 10). 
Sequence information
Length: 501 AA [This is the length of the unprocessed precursor] Molecular weight: 54862 Da [This is the MW of the unprocessed precursor] CRC64: B26464DC7168348E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKEDV 

        70         80         90        100        110        120 
DKAVKAARQA FQIGSPWRTM DASERGRLLY KLADLIERDR LLLATMESMN GGKLYSNAYL 

       130        140        150        160        170        180 
NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKI 

       190        200        210        220        230        240 
GPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID 

       250        260        270        280        290        300 
KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG 

       310        320        330        340        350        360 
QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ YDKILDLIES 

       370        380        390        400        410        420 
GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR 

       430        440        450        460        470        480 
ANNTFYGLSA GVFTKDIDKA ITISSALQAG TVWVNCYGVV SAQCPFGGFK MSGNGRELGE 

       490        500 
YGFHEYTEVK TVTVKISQKN S 

P00352 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!