[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Salivary gland; DOI=10.1006/geno.1994.1624; PubMed=7698756 [NCBI, ExPASy, EBI, Israel, Japan] Hsu L.C., Chang W.-C., Hiraoka L., Hsieh C.-L.; "Molecular cloning, genomic organization, and chromosomal localization of an additional human aldehyde dehydrogenase gene, ALDH6."; Genomics 24:333-341(1994).
[2]	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).

Comments

FUNCTION: Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Seems to be the key enzyme in the formation of an RA gradient along the dorso-ventral axis during the early eye development and also in the development of the olfactory system (By similarity).
CATALYTIC ACTIVITY: An aldehyde + NAD(P)⁺ + H₂O = an acid + NAD(P)H.
PATHWAY: Cofactor metabolism; retinol metabolism .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
TISSUE SPECIFICITY: Expressed at low levels in many tissues and at higher levels in salivary gland, stomach, and kidney.
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

U07919; AAA79036.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069274; AAH69274.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A55684; A55684.

NP_000684.2; -.

3D structure databases

HSSP

Q63639; 1BI9. [HSSP ENTRY / PDB]

ModBase

P47895.

Organism-specific databases

HIX0026851; -.

HGNC:409; ALDH1A3.

600463; gene. [NCBI / EBI]

PharmGKB

PA24694; -.

GeneCards

P47895.

Gene expression databases

ArrayExpress

P47895; -.

CleanEx

HS_ALDH1A3; -.

GermOnline

ENSG00000184254; Homo sapiens.

Ontologies

GO:0004028;	Molecular function: 3-chloroallyl aldehyde dehydrogenase activity (traceable author statement from ProtInc).
GO:0006066;	Biological process: cellular alcohol metabolic process (traceable author statement from ProtInc).
GO:0006629;	Biological process: lipid metabolic process (traceable author statement from ProtInc).
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

P47895.

Proteomic databases

PeptideAtlas

P47895; -.

Genome annotation databases

Ensembl

ENSG00000184254; Homo sapiens. [Contig view]

GeneID

220; -.

KEGG

hsa:220; -.

NMPDR

fig|9606.3.peg.11311; -.

Phylogenomic databases

HOGENOM

P47895; -.

HOVERGEN

P47895; -.

Other

DrugBank

DB00157; NADH.
DB00162; Vitamin A.

SOURCE

ALDH1A3; Homo sapiens.

ProtoNet

P47895.

UniRef

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

Keywords

Cytoplasm; NAD; Oxidoreductase; Polymorphism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 512`	`512`	`Aldehyde dehydrogenase family 1 member A3.`	`PRO_0000056478`
`NP_BIND`	`257 262`	`6`	`NAD (By similarity).`
`ACT_SITE`	`280 280`		`Proton acceptor (By similarity).`
`ACT_SITE`	`314 314`		`Nucleophile (By similarity).`
`SITE`	`181 181`	`1`	`Transition state stabilizer (By similarity).`
`VARIANT`	`386 386`	`1`	`M -> V (in dbSNP:rs3803430 [NCBI]).`	`VAR_019706`
`CONFLICT`	`15 15`		`R -> G (in Ref. 1; AAA79036).`

Sequence information

Length: 512 AA [This is the length of the unprocessed precursor]

Molecular weight: 56108 Da [This is the MW of the unprocessed precursor]

CRC64: 1BFCF4F56F0FE89A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATANGAVEN GQPDRKPPAL PRPIRNLEVK FTKIFINNEW HESKSGKKFA TCNPSTREQI 

        70         80         90        100        110        120 
CEVEEGDKPD VDKAVEAAQV AFQRGSPWRR LDALSRGRLL HQLADLVERD RATLAALETM 

       130        140        150        160        170        180 
DTGKPFLHAF FIDLEGCIRT LRYFAGWADK IQGKTIPTDD NVVCFTRHEP IGVCGAITPW 

       190        200        210        220        230        240 
NFPLLMLVWK LAPALCCGNT MVLKPAEQTP LTALYLGSLI KEAGFPPGVV NIVPGFGPTV 

       250        260        270        280        290        300 
GAAISSHPQI NKIAFTGSTE VGKLVKEAAS RSNLKRVTLE LGGKNPCIVC ADADLDLAVE 

       310        320        330        340        350        360 
CAHQGVFFNQ GQCCTAASRV FVEEQVYSEF VRRSVEYAKK RPVGDPFDVK TEQGPQIDQK 

       370        380        390        400        410        420 
QFDKILELIE SGKKEGAKLE CGGSAMEDKG LFIKPTVFSE VTDNMRIAKE EIFGPVQPIL 

       430        440        450        460        470        480 
KFKSIEEVIK RANSTDYGLT AAVFTKNLDK ALKLASALES GTVWINCYNA LYAQAPFGGF 

       490        500        510 
KMSGNGRELG EYALAEYTEV KTVTIKLGDK NP

P47895 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