[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. STRAIN=BALB/c, and C57BL/6; TISSUE=Liver; DOI=10.1016/0378-1119(91)90421-7; PubMed=2055490 [NCBI, ExPASy, EBI, Israel, Japan] Rongnoparut P., Weaver S.; "Isolation and characterization of a cytosolic aldehyde dehydrogenase-encoding cDNA from mouse liver."; Gene 101:261-265(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. STRAIN=129/ReJ, BALB/c, and C57BL/6J; TISSUE=Liver; DOI=10.1006/bmmb.1994.1048; PubMed=7993664 [NCBI, ExPASy, EBI, Israel, Japan] Bond S.L., Singh S.M.; "DNA sequence analysis of the cytosolic acetaldehyde dehydrogenase gene (Ahd-2) in mouse strains with variable ethanol preferences."; Biochem. Med. Metab. Biol. 52:155-159(1994).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Colon, and Liver; 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).
[4]	PROTEIN SEQUENCE OF 23-52; 140-156; 211-230; 309-320; 330-349; 400-410; 421-435 AND 477-490. TISSUE=Embryonic retina; PubMed=1935685 [NCBI, ExPASy, EBI, Israel, Japan] McCaffery P., Tempst P., Lara G., Drager U.C.; "Aldehyde dehydrogenase is a positional marker in the retina."; Development 112:693-702(1991).

Comments

FUNCTION: In addition to the activity on acetaldehyde and related substrates, is also involved in the oxidation of aldehydes derived from biogenic amines such as epinephrine and norepinephrine, as well as the aldehydes generated via lipid peroxidation. Binds free retinal and cellular retinol-binding protein-bound retinal. Can convert/oxidize retinaldehyde to retinoic acid (By similarity).
CATALYTIC ACTIVITY: Retinal + NAD⁺ + H₂O = retinoate + NADH.
PATHWAY: Cofactor metabolism; retinol metabolism .
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Expressed in the liver, lung, and testis. Apparently not expressed at detectable levels in kidney, stomach, ovary, heart, and brain.
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

M74570; AAA37202.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M74571; AAA37203.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S75713; AAB32754.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S77047; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
BC044729; AAH44729.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC054386; AAH54386.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

JQ1004; JQ1004.

NP_038495.2; -.

3D structure databases

HSSP

P51977; 1BXS. [HSSP ENTRY / PDB]

ModBase

P24549.

Protein-protein interaction databases

IntAct

P24549; -.

PTM databases

PhosphoSite

P24549; -.

2D gel databases

SWISS-2DPAGE

P24549; -.

REPRODUCTION-2DPAGE

P24549; -.

Organism-specific databases

MGI

MGI:1353450; Aldh1a1.

Gene expression databases

ArrayExpress

P24549; -.

CleanEx

MM_ALDH1A1; -.

GermOnline

ENSMUSG00000053279; Mus musculus.

Ontologies

GO:0004028;	Molecular function: 3-chloroallyl aldehyde dehydrogenase activity (inferred from direct assay from MGI).
GO:0048048;	Biological process: embryonic eye morphogenesis (inferred from genetic interaction from MGI).
GO:0002072;	Biological process: optic cup morphogenesis involved in camera-type eye development (inferred from genetic interaction from MGI).
GO:0043065;	Biological process: positive regulation of apoptosis (inferred from genetic interaction from MGI).
GO:0042573;	Biological process: retinoic acid metabolic process (inferred from mutant phenotype from MGI).
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

P24549.

Genome annotation databases

Ensembl

ENSMUSG00000053279; Mus musculus. [Contig view]

GeneID

11668; -.

KEGG

mmu:11668; -.

Phylogenomic databases

HOGENOM

P24549; -.

HOVERGEN

P24549; -.

Other

SOURCE

Aldh1a1; Mus musculus.

ProtoNet

P24549.

UniRef

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

Keywords

Acetylation; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 501`	`500`	`Retinal dehydrogenase 1.`	`PRO_0000056417`
`NP_BIND`	`246 251`	`6`	`NAD (By similarity).`
`REGION`	`300 305`	`6`	`Antabuse binding.`
`ACT_SITE`	`269 269`		`Proton acceptor (By similarity).`
`ACT_SITE`	`303 303`		`Nucleophile (By similarity).`
`SITE`	`170 170`	`1`	`Transition state stabilizer (By similarity).`
`MOD_RES`	`2 2`		`N-acetylserine (By similarity).`
`CONFLICT`	`8 8`		`A -> R (in Ref. 1; AAA37202/AAA37203).`
`CONFLICT`	`45 45`		`T -> S (in Ref. 2; AAB32754).`
`CONFLICT`	`51 51`		`H -> Q (in Ref. 2; AAB32754).`
`CONFLICT`	`87 87`		`R -> C (in Ref. 1; AAA37202).`
`CONFLICT`	`140 140`		`I -> Y (in Ref. 4; AA sequence).`
`CONFLICT`	`458 458`		`M -> I (in Ref. 1; AAA37202).`

Sequence information

Length: 501 AA [This is the length of the unprocessed precursor]

Molecular weight: 54468 Da [This is the MW of the unprocessed precursor]

CRC64: 0E428151B799BD1D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSPAQPAVP APLADLKIQH TKIFINNEWH NSVSGKKFPV LNPATEEVIC HVEEGDKADV 

        70         80         90        100        110        120 
DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLMERDR LLLATMEALN GGKVFANAYL 

       130        140        150        160        170        180 
SDLGGCIKAL KYCAGWADKI HGQTIPSDGD IFTYTRREPI GVCGQIIPWN FPMLMFIWKI 

       190        200        210        220        230        240 
GPALSCGNTV VVKPAEQTPL TALHLASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD 

       250        260        270        280        290        300 
KVAFTGSTQV GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDIAVEF AHHGVFYHQG 

       310        320        330        340        350        360 
QCCVAASRIF VEESVYDEFV KRSVERAKKY VLGNPLTPGI NQGPQIDKEQ HDKILDLIES 

       370        380        390        400        410        420 
GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSVDDVIKR 

       430        440        450        460        470        480 
ANNTTYGLAA GLFTKDLDKA ITVSSALQAG VVWVNCYMML SAQCPFGGFK MSGNGRELGE 

       490        500 
HGLYEYTELK TVAMKISQKN S

P24549 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