Aldehyde dehydrogenase, dimeric NADP-preferring

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P30838 (AL3A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Aldehyde dehydrogenase, dimeric NADP-preferring
EC=1.2.1.5

Alternative name(s):
ALDHIII
Aldehyde dehydrogenase 3
Aldehyde dehydrogenase family 3 member A1

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

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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 = a carboxylate + 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	NAD NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular aldehyde metabolic process Inferred from direct assay Ref.2. 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 Inferred from direct assay Ref.2. Source: UniProtKB aldehyde dehydrogenase (NAD) activity Inferred from direct assay Ref.2. Source: UniProtKB aldehyde dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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 or NADP By similarity

Sites

Active site

210

By similarity

Active site

244

By similarity

Amino acid modifications

Modified residue

N6-acetyllysine Ref.9

Modified residue

178

N6-acetyllysine Ref.9

Modified residue

194

N6-acetyllysine Ref.9

Modified residue

269

N6-acetyllysine Ref.9

Natural variations

Natural variant

134

S → A. Ref.1 Ref.4 Ref.6
Corresponds to variant rs887241 [ dbSNP | Ensembl ].

VAR_018981

Natural variant

309

G → E.
Corresponds to variant rs3744692 [ dbSNP | Ensembl ].

VAR_018982

Natural variant

329

P → A in allele ALDH3A1*2. Ref.10
Corresponds to variant rs2228100 [ dbSNP | Ensembl ].

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

Sequences

Sequence

Length

Mass (Da)

Tools

P30838 [UniParc].

Last modified November 2, 2010. Version 3.
Checksum: D35C488A022FAACA
Show »

FASTA

453

50,395

        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 AGNSVVLKPS 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

« Hide

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], VARIANT ALA-134. 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]. 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]. 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], VARIANT ALA-134.
[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].
[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], VARIANT ALA-134. 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: 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]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-178; LYS-194 AND LYS-269, MASS SPECTROMETRY.
[10]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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_000682.3. NM_000691.4.
NP_001128639.1. NM_001135167.1.
NP_001128640.1. NM_001135168.1.

UniGene

Hs.531682.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3SZA	X-ray	1.48	A/B	1-453	[»]
3SZB	X-ray	1.51	A/B	1-453	[»]

ProteinModelPortal

P30838.

SMR

P30838. Positions 4-448.

ModBase

Search...

Protein-protein interaction databases

IntAct

P30838. 2 interactions.

STRING

P30838.

PTM databases

PhosphoSite

P30838.

Polymorphism databases

DMDM

311033473.

2D gel databases

Cornea-2DPAGE

P30838.

Proteomic databases

PRIDE

P30838.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000225740; ENSP00000225740; ENSG00000108602.
ENST00000444455; ENSP00000388469; ENSG00000108602.
ENST00000457500; ENSP00000411821; ENSG00000108602.

GeneID

218.

KEGG

hsa:218.

Organism-specific databases

CTD

218.

GeneCards

GC17M019641.

H-InvDB

HIX0013622.

HGNC

HGNC:405. ALDH3A1.

MIM

100660. gene.

neXtProt

NX_P30838.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08185.

GeneTree

ENSGT00390000002825.

HOVERGEN

HBG050483.

PhylomeDB

P30838.

Gene expression databases

ArrayExpress

P30838.

Bgee

P30838.

CleanEx

HS_ALDH3A1.

Genevestigator

P30838.

GermOnline

ENSG00000108602. Homo sapiens.

Family and domain databases

InterPro

IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR012394. Aldehyde_DH_NAD(P).
[Graphical view]

Gene3D

G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.

K00129.

PANTHER

PTHR11699:SF15. ALDH. 1 hit.

Pfam

PF00171. Aldedh. 1 hit.
[Graphical view]

PIRSF

PIRSF036492. ALDH. 1 hit.

SUPFAM

SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.

PROSITE

PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00157. NADH.

NextBio

882.

SOURCE

Search...

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:	November 2, 2010
Last modified:	January 25, 2012
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents