Aldehyde dehydrogenase, dimeric NADP-preferring

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Reviewed, UniProtKB/Swiss-Prot P30838 (AL3A1_HUMAN)

Last modified June 16, 2009. Version 96. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Aldehyde dehydrogenase, dimeric NADP-preferring
    EC=1.2.1.5
Alternative name(s):
    Aldehyde dehydrogenase family 3 member A1
      Short name=Aldehyde dehydrogenase 3
    ALDHIII

Gene names

Name:	ALDH3A1
Synonyms:	ALDH3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes.
Catalytic activity	An aldehyde + NAD(P)⁺ + H₂O = an acid + NAD(P)H.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Tissue specificity	High levels in stomach, esophagus and lung; low level in the liver and kidney.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.
biophysicochemical properties	Kinetic parameters: Has a high Km for acetaldehyde.

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular aldehyde metabolic process Ref.2 Inferred from direct assay. Source: UniProtKB oxidation reduction Ref.2 Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum Inferred from direct assay. Source: LIFEdb
Molecular function	alcohol dehydrogenase (NADP+) activity Ref.2 Inferred from direct assay. Source: UniProtKB aldehyde dehydrogenase (NAD) activity Ref.2 Inferred from direct assay. Source: UniProtKB aldehyde dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 453

453

Aldehyde dehydrogenase, dimeric NADP-preferring

PRO_0000056470

Regions

Nucleotide binding

188 – 193

NAD By similarity

Sites

Active site

210

By similarity

Active site

244

By similarity

Natural variations

Natural variant

134

A → S: dbSNP rs887241. Ref.2 Ref.3 Ref.5

VAR_018981

Natural variant

309

G → E: dbSNP rs3744692.

VAR_018982

Natural variant

329

P → A in allele ALDH3A1*2. dbSNP rs2228100. Ref.9

VAR_011303

Experimental info

Sequence conflict

R → P in AAB46377. Ref.2

Sequence conflict

R → P in AAB26658. Ref.3

Sequence conflict

I → F in AAA51696. Ref.1

Sequence conflict

170

V → L AA sequence Ref.7

Sequence conflict

436

D → E AA sequence Ref.7

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Sequences

Sequence

Length

Mass (Da)

Tools

P30838-1 [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: 8F3DAEE33775A47A
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FASTA

453

50,379

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and complete nucleotide sequence of a cDNA encoding the full-length open reading frame of the human aldehyde dehydrogenase type III gene." Schuuring E.M.D., Verhoeven E., Eckey R., Vos H.L., Michalides R.J.A. Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Stomach.
[2]	"Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary structure, and expression in Escherichia coli." Hsu L.C., Chang W.-C., Shibuya A., Yoshida A. J. Biol. Chem. 267:3030-3037(1992) [PubMed: 1737758] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-134. Tissue: Stomach.
[3]	"Human stomach aldehyde dehydrogenase, ALDH3." Hsu L.C., Yoshida A. Adv. Exp. Med. Biol. 328:141-152(1993) [PubMed: 8493892] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-134. Tissue: Stomach.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." 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. Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-134.
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
[7]	"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." Yin S.-J., Vagelopoulos N., Wang S.-L., Joernvall H. FEBS Lett. 283:85-88(1991) [PubMed: 2037078] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE OF 62-453. Tissue: Stomach.
[8]	"Biochemical, immunological, and molecular characterization of a 'high Km' aldehyde dehydrogenase." Eckey R., Timmann R., Hempel J., Agarwal D.P., Goedde H.W. Adv. Exp. Med. Biol. 284:43-52(1991) [PubMed: 1905102] [Abstract] Cited for: CHARACTERIZATION.
[9]	"Mutations associated with Sjogren-Larsson syndrome." Tsukamoto N., Chang C., Yoshida A. Ann. Hum. Genet. 61:235-242(1997) [PubMed: 9250352] [Abstract] Cited for: VARIANT ALA-329.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M74542 mRNA. Translation: AAA51696.1. M77477 mRNA. Translation: AAB46377.1. S61044 mRNA. Translation: AAB26658.1. BT007102 mRNA. Translation: AAP35766.1. AC005722 Genomic DNA. No translation available. BC004370 mRNA. Translation: AAH04370.1. BC008892 mRNA. Translation: AAH08892.1. BC021194 mRNA. Translation: AAH21194.1.
IPI	IPI00296183.
PIR	A42584.
RefSeq	NP_001128639.1.
UniGene	Hs.531682
3D structure databases
HSSP	HSSP built from PDB template 1AD3 based on UniProtKB P11883.
SMR	P30838. Positions 4-448.
ModBase	Search...
PTM databases
PhosphoSite	P30838.
2-D gel databases
Cornea-2DPAGE	P30838.
Proteomic databases
PRIDE	P30838.
Genome annotation databases
Ensembl	ENSG00000108602. Homo sapiens. [Contig view]
GeneID	218.
Organism-specific databases
GeneCards	GC17M019581.
H-InvDB	HIX0013622.
HGNC	HGNC:405. ALDH3A1.
MIM	100660. gene.
PharmGKB	PA24697.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P30838.
Enzyme and pathway databases
BRENDA	1.2.1.5. 247.
Gene expression databases
ArrayExpress	P30838.
Bgee	P30838.
CleanEx	HS_ALDH3A1.
GermOnline	ENSG00000108602. Homo sapiens.
Family and domain databases
InterPro	IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. IPR012394. Aldehyde_DH_NAD(P). [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit. PTHR11699:SF15. ALDH. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
PIRSF	PIRSF036492. ALDH. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00157. NADH.
NextBio	882.
SOURCE	Search...

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Entry information

Entry name

AL3A1_HUMAN

Accession

Primary (citable) accession number: P30838
Secondary accession number(s): Q9BT37

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	June 7, 2004
Last modified:	June 16, 2009
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents