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UniProtKB/Swiss-Prot entry P30838


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

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Entry information
Entry name AL3A1_HUMAN
Primary accession number P30838
Secondary accession number Q9BT37
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on June 7, 2004 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 92)
Name and origin of the protein
Protein name Aldehyde dehydrogenase, dimeric NADP-preferring
Synonyms EC 1.2.1.5
Aldehyde dehydrogenase family 3 member A1
Aldehyde dehydrogenase 3
ALDHIII
Gene name
Name: ALDH3A1
Synonyms: ALDH3
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 [MRNA].
TISSUE=Stomach;
Schuuring E.M.D., Verhoeven E., Eckey R., Vos H.L., Michalides R.J.A.;
"Cloning and complete nucleotide sequence of a cDNA encoding the full-length open reading frame of the human aldehyde dehydrogenase type III gene.";
Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-134.
TISSUE=Stomach;
PubMed=1737758 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu L.C., Chang W.-C., Shibuya A., Yoshida A.;
"Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary structure, and expression in Escherichia coli.";
J. Biol. Chem. 267:3030-3037(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-134.
TISSUE=Stomach;
PubMed=8493892 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu L.C., Yoshida A.;
"Human stomach aldehyde dehydrogenase, ALDH3.";
Adv. Exp. Med. Biol. 328:141-152(1993).
[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 [LARGE SCALE GENOMIC DNA], AND VARIANT SER-134.
DOI=10.1038/nature04689; PubMed=16625196 [NCBI, ExPASy, EBI, Israel, Japan]
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
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]
PARTIAL PROTEIN SEQUENCE OF 62-453.
TISSUE=Stomach;
DOI=10.1016/0014-5793(91)80559-L; PubMed=2037078 [NCBI, ExPASy, EBI, Israel, Japan]
Yin S.-J., Vagelopoulos N., Wang S.-L., Joernvall H.;
"Structural features of stomach aldehyde dehydrogenase distinguish dimeric aldehyde dehydrogenase as a 'variable' enzyme. 'Variable' and 'constant' enzymes within the alcohol and aldehyde dehydrogenase families.";
FEBS Lett. 283:85-88(1991).
[8]
CHARACTERIZATION.
PubMed=1905102 [NCBI, ExPASy, EBI, Israel, Japan]
Eckey R., Timmann R., Hempel J., Agarwal D.P., Goedde H.W.;
"Biochemical, immunological, and molecular characterization of a 'high Km' aldehyde dehydrogenase.";
Adv. Exp. Med. Biol. 284:43-52(1991).
[9]
VARIANT ALA-329.
DOI=10.1017/S0003480097006143; PubMed=9250352 [NCBI, ExPASy, EBI, Israel, Japan]
Tsukamoto N., Chang C., Yoshida A.;
"Mutations associated with Sjogren-Larsson syndrome.";
Ann. Hum. Genet. 61:235-242(1997).
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
M74542; AAA51696.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77477; AAB46377.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S61044; AAB26658.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007102; AAP35766.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005722; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC004370; AAH04370.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008892; AAH08892.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021194; AAH21194.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A42584; A42584.
UniGene Hs.531682
3D structure databases
HSSP P11883; 1AD3. [HSSP ENTRY / PDB]
SMR P30838; 4-448.
ModBase P30838.
PTM databases
PhosphoSite P30838; -.
2D gel databases
Cornea-2DPAGE P30838; -.
Organism-specific databases
GeneCards GC17M019581; -.
H-InvDB HIX0013622; -.
HGNC HGNC:405; ALDH3A1.
GenAtlas ALDH3A1.
MIM 100660; gene. [NCBI / EBI]
PharmGKB PA24697; -.
GeneCards P30838.
Gene expression databases
ArrayExpress P30838; -.
CleanEx HS_ALDH3A1; -.
GermOnline ENSG00000108602; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from sequence or structural similarity from UniProtKB).
GO:0005783; Cellular component: endoplasmic reticulum (inferred from direct assay from LIFEdb).
GO:0008106; Molecular function: alcohol dehydrogenase (NADP+) activity (inferred from direct assay from UniProtKB).
GO:0004029; Molecular function: aldehyde dehydrogenase (NAD) activity (inferred from direct assay from UniProtKB).
GO:0004030; Molecular function: aldehyde dehydrogenase [NAD(P)+] activity (inferred from electronic annotation from InterPro).
GO:0006081; Biological process: cellular aldehyde metabolic process (inferred from direct assay from UniProtKB).
GO:0055114; Biological process: oxidation reduction (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR012394; Ald_DHase_NAD(P).
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
PTHR11699:SF15; ALDH; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF036492; ALDH; 1.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
Proteomics databases
PRIDE P30838; -.
Genome annotation databases
Ensembl ENSG00000108602; Homo sapiens. [Contig view]
KEGG hsa:218; -.
Phylogenomic databases
HOVERGEN P30838; -.
Other
DrugBank DB00157; NADH.
NextBio 882; -.
SOURCE ALDH3A1; Homo sapiens.
ProtoNet P30838.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   453  453     Aldehyde dehydrogenase, dimeric NADP-preferring. PRO_0000056470
NP_BIND   188   193  6     NAD (By similarity). 
ACT_SITE   210   210        By similarity. 
ACT_SITE   244   244        By similarity. 
VARIANT   134   134  1     A -> S (in dbSNP:rs887241 [NCBI]). VAR_018981 
VARIANT   309   309  1     G -> E (in dbSNP:rs3744692 [NCBI]). VAR_018982 
VARIANT   329   329  1     P -> A (in allele ALDH3A1*2; dbSNP:rs2228100 [NCBI]). VAR_011303 
CONFLICT   12    12        R -> P (in Ref. 2; AAB46377 and 3; AAB26658). 
CONFLICT   27    27        I -> F (in Ref. 1; AAA51696). 
CONFLICT   170   170        V -> L (in Ref. 7; AA sequence). 
CONFLICT   436   436        D -> E (in Ref. 7; AA sequence). 
Sequence information
Length: 453 AA [This is the length of the unprocessed precursor] Molecular weight: 50379 Da [This is the MW of the unprocessed precursor] CRC64: 8F3DAEE33775A47A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKISEAVKR ARAAFSSGRT RPLQFRIQQL EALQRLIQEQ EQELVGALAA DLHKNEWNAY 

        70         80         90        100        110        120 
YEEVVYVLEE IEYMIQKLPE WAADEPVEKT PQTQQDELYI HSEPLGVVLV IGTWNYPFNL 

       130        140        150        160        170        180 
TIQPMVGAIA AGNAVVLKPS ELSENMASLL ATIIPQYLDK DLYPVINGGV PETTELLKER 

       190        200        210        220        230        240 
FDHILYTGST GVGKIIMTAA AKHLTPVTLE LGGKSPCYVD KNCDLDVACR RIAWGKFMNS 

       250        260        270        280        290        300 
GQTCVAPDYI LCDPSIQNQI VEKLKKSLKE FYGEDAKKSR DYGRIISARH FQRVMGLIEG 

       310        320        330        340        350        360 
QKVAYGGTGD AATRYIAPTI LTDVDPQSPV MQEEIFGPVL PIVCVRSLEE AIQFINQREK 

       370        380        390        400        410        420 
PLALYMFSSN DKVIKKMIAE TSSGGVAAND VIVHITLHSL PFGGVGNSGM GSYHGKKSFE 

       430        440        450 
TFSHRRSCLV RPLMNDEGLK VRYPPSPAKM TQH 

P30838 in FASTA format

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