[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2831537 [NCBI, ExPASy, EBI, Israel, Japan] Jones D.E., Brennan M.D., Hempel J., Lindahl R.; "Cloning and complete nucleotide sequence of a full-length cDNA encoding a catalytically functional tumor-associated aldehyde dehydrogenase."; Proc. Natl. Acad. Sci. U.S.A. 85:1782-1786(1988).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lung; 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).
[3]	PARTIAL PROTEIN SEQUENCE. DOI=10.1021/bi00429a034; PubMed=2713359 [NCBI, ExPASy, EBI, Israel, Japan] Hempel J., Harper K., Lindahl R.; "Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria."; Biochemistry 28:1160-1167(1989).
[4]	GENE STRUCTURE. PubMed=8509394 [NCBI, ExPASy, EBI, Israel, Japan] Asman D.C., Takimoto K., Pitot H.C., Dunn T.J., Lindahl R.; "Organization and characterization of the rat class 3 aldehyde dehydrogenase gene."; J. Biol. Chem. 268:12530-12536(1993).
[5]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). DOI=10.1002/prot.340080404; PubMed=2091023 [NCBI, ExPASy, EBI, Israel, Japan] Rose J.P., Hempel J., Kuo I., Lindahl R., Wang B.-C.; "Preliminary crystallographic analysis of class 3 rat liver aldehyde dehydrogenase."; Proteins 8:305-308(1990).
[6]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). DOI=10.1038/nsb0497-317; PubMed=9095201 [NCBI, ExPASy, EBI, Israel, Japan] Liu Z.-J., Sun Y.J., Rose J.P., Chung Y.-J., Hsiao C.D., Chang W.-R., Kuo I., Perozich J., Lindahl R., Hempel J., Wang B.-C.; "The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold."; Nat. Struct. Biol. 4:317-326(1997).

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: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
INDUCTION: This protein can be induced by a number of chemical carcinogens during rat hepatocarcinogenesis.
SIMILARITY: Belongs to the aldehyde dehydrogenase family.

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

J03637; AAA40713.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC070924; AAH70924.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A30149; A30149.

NP_114178.1; -.

3D structure databases

PDB

1AD3; X-ray; 2.60 A; A/B=3-453.

[ExPASy / RCSB / EBI]

PDBsum

1AD3; -.

ModBase

P11883.

Protein-protein interaction databases

IntAct

P11883; -.

Organism-specific databases

RGD

2088; Aldh3a1.

Gene expression databases

ArrayExpress

P11883; -.

GermOnline

ENSRNOG00000002331; Rattus norvegicus.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0008106;	Molecular function: alcohol dehydrogenase (NADP+) activity (inferred from sequence or structural similarity from UniProtKB).
GO:0004029;	Molecular function: aldehyde dehydrogenase (NAD) activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006081;	Biological process: cellular aldehyde metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from sequence or structural similarity 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.

BLOCKS

P11883.

Genome annotation databases

Ensembl

ENSRNOG00000002331; Rattus norvegicus. [Contig view]

GeneID

25375; -.

KEGG

rno:25375; -.

NMPDR

fig|10116.3.peg.5198; -.

Phylogenomic databases

HOVERGEN

P11883; -.

Other

P11883; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 453`	`452`	`Aldehyde dehydrogenase, dimeric NADP-preferring.`	`PRO_0000056472`
`NP_BIND`	`188 193`	`6`	`NAD (By similarity).`
`ACT_SITE`	`210 210`		`By similarity.`
`ACT_SITE`	`244 244`		`By similarity.`
`HELIX`	`4 16`	`13`
`HELIX`	`19 21`	`3`
`HELIX`	`23 52`	`30`
`HELIX`	`56 62`	`7`
`HELIX`	`64 82`	`19`
`TURN`	`92 95`	`4`
`STRAND`	`96 104`	`9`
`STRAND`	`106 111`	`6`
`STRAND`	`114 116`	`3`
`HELIX`	`119 130`	`12`
`STRAND`	`134 138`	`5`
`HELIX`	`144 157`	`14`
`TURN`	`160 162`	`3`
`STRAND`	`163 165`	`3`
`HELIX`	`170 176`	`7`
`STRAND`	`182 188`	`7`
`HELIX`	`190 201`	`12`
`TURN`	`202 204`	`3`
`STRAND`	`207 210`	`4`
`STRAND`	`216 219`	`4`
`STRAND`	`221 223`	`3`
`HELIX`	`225 237`	`13`
`TURN`	`238 241`	`4`
`STRAND`	`249 252`	`4`
`HELIX`	`254 256`	`3`
`HELIX`	`257 272`	`16`
`HELIX`	`276 278`	`3`
`HELIX`	`288 296`	`9`
`TURN`	`297 300`	`4`
`STRAND`	`303 305`	`3`
`TURN`	`311 314`	`4`
`STRAND`	`319 321`	`3`
`HELIX`	`329 331`	`3`
`STRAND`	`337 340`	`4`
`STRAND`	`342 344`	`3`
`HELIX`	`348 356`	`9`
`STRAND`	`362 367`	`6`
`HELIX`	`371 378`	`8`
`STRAND`	`384 392`	`9`
`HELIX`	`393 396`	`4`
`HELIX`	`406 408`	`3`
`HELIX`	`416 421`	`6`
`STRAND`	`423 430`	`8`
`HELIX`	`440 442`	`3`
`STRAND`	`443 445`	`3`

Sequence information

Length: 453 AA [This is the length of the unprocessed precursor]

Molecular weight: 50339 Da [This is the MW of the unprocessed precursor]

CRC64: 15C501BAB4F9845A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSISDTVKR AREAFNSGKT RSLQFRIQQL EALQRMINEN LKSISGALAS DLGKNEWTSY 

        70         80         90        100        110        120 
YEEVAHVLEE LDTTIKELPD WAEDEPVAKT RQTQQDDLYI HSEPLGVVLV IGAWNYPFNL 

       130        140        150        160        170        180 
TIQPMVGAVA AGNAVILKPS EVSGHMADLL ATLIPQYMDQ NLYLVVKGGV PETTELLKER 

       190        200        210        220        230        240 
FDHIMYTGST AVGKIVMAAA AKHLTPVTLE LGGKSPCYVD KDCDLDVACR RIAWGKFMNS 

       250        260        270        280        290        300 
GQTCVAPDYI LCDPSIQNQI VEKLKKSLKD FYGEDAKQSR DYGRIINDRH FQRVKGLIDN 

       310        320        330        340        350        360 
QKVAHGGTWD QSSRYIAPTI LVDVDPQSPV MQEEIFGPVM PIVCVRSLEE AIQFINQREK 

       370        380        390        400        410        420 
PLALYVFSNN EKVIKKMIAE TSSGGVTAND VIVHITVPTL PFGGVGNSGM GAYHGKKSFE 

       430        440        450 
TFSHRRSCLV KSLLNEEAHK ARYPPSPAKM PRH

P11883 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools