[1]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. STRAIN=B6/D2; DOI=10.1016/S0925-4773(00)00352-X; PubMed=10906479 [NCBI, ExPASy, EBI, Israel, Japan] Li H., Wagner E., McCaffery P., Smith D., Andreadis A., Drager U.C.; "A retinoic acid synthesizing enzyme in ventral retina and telencephalon of the embryonic mouse."; Mech. Dev. 95:283-289(2000).
[2]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY. STRAIN=C57BL/6 X 129/SvJ; TISSUE=Kidney; DOI=10.1016/S0925-4773(00)00434-2; PubMed=11025231 [NCBI, ExPASy, EBI, Israel, Japan] Mic F.A., Molotkov A., Fan X., Cuenca A.E., Duester G.; "RALDH3, a retinaldehyde dehydrogenase that generates retinoic acid, is expressed in the ventral retina, otic vesicle and olfactory pit during mouse development."; Mech. Dev. 97:227-230(2000).
[3]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. STRAIN=C57BL/6J; TISSUE=Retina; DOI=10.1016/S0925-4773(00)00450-0; PubMed=11044606 [NCBI, ExPASy, EBI, Israel, Japan] Suzuki R., Shintani T., Sakuta H., Kato A., Ohkawara T., Osumi N., Noda M.; "Identification of RALDH-3, a novel retinaldehyde dehydrogenase, expressed in the ventral region of the retina."; Mech. Dev. 98:37-50(2000).
[4]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1074/jbc.M007376200; PubMed=11013254 [NCBI, ExPASy, EBI, Israel, Japan] Grun F., Hirose Y., Kawauchi S., Ogura T., Umesono K.; "Aldehyde dehydrogenase 6, a cytosolic retinaldehyde dehydrogenase prominently expressed in sensory neuroepithelia during development."; J. Biol. Chem. 275:41210-41218(2000).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Mammary tumor; 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.
CATALYTIC ACTIVITY: An aldehyde + NAD(P)⁺ + H₂O = an acid + NAD(P)H.
PATHWAY: Cofactor metabolism; retinol metabolism .
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Ventral retina.
DEVELOPMENTAL STAGE: In mouse embryos, RALDH3 expression is first noticed in the ventral optic eminence at E8.75, then in the optic vesicle/cup, otic vesicle and olfactory placode/pit from E9.5 to E11.5.
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

AF253409; AAF67736.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF280404; AAF86980.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF246711; AAG38488.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF152359; AAG33935.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC058277; AAH58277.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_444310.3; -.

UniGene

Mm.140988

3D structure databases

HSSP

P51977; 1BXS. [HSSP ENTRY / PDB]

ModBase

Q9JHW9.

Organism-specific databases

MGI

MGI:1861722; Aldh1a3.

Gene expression databases

ArrayExpress

Q9JHW9; -.

CleanEx

MM_ALDH1A3; -.

GermOnline

ENSMUSG00000015134; Mus musculus.

Ontologies

GO:0004028;	Molecular function: 3-chloroallyl aldehyde dehydrogenase activity (traceable author statement from MGI).
GO:0048048;	Biological process: embryonic eye morphogenesis (inferred from genetic interaction from MGI).
GO:0021768;	Biological process: nucleus accumbens development (inferred from mutant phenotype from MGI).
GO:0060166;	Biological process: olfactory pit development (inferred from mutant phenotype 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

Q9JHW9.

Genome annotation databases

Ensembl

ENSMUSG00000015134; Mus musculus. [Contig view]

GeneID

56847; -.

KEGG

mmu:56847; -.

NMPDR

fig|10090.3.peg.16667; -.

Phylogenomic databases

HOGENOM

Q9JHW9; -.

HOVERGEN

Q9JHW9; -.

Other

SOURCE

Aldh1a3; Mus musculus.

ProtoNet

Q9JHW9.

UniRef

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

Keywords

Cytoplasm; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 512`	`512`	`Aldehyde dehydrogenase family 1 member A3.`	`PRO_0000056479`
`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).`
`CONFLICT`	`91 91`		`L -> V (in Ref. 1; AAF67736).`
`CONFLICT`	`208 208`		`Q -> R (in Ref. 4; AAG33935).`
`CONFLICT`	`223 223`		`V -> E (in Ref. 1; AAF67736).`
`CONFLICT`	`341 341`		`R -> S (in Ref. 4; AAG33935).`
`CONFLICT`	`407 407`		`I -> R (in Ref. 1; AAF67736).`

Sequence information

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

Molecular weight: 56157 Da [This is the MW of the unprocessed precursor]

CRC64: 5BBC6DEE41E58CFE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATTNGAVEN GQPDGKPPAL PRPIRNLEVK FTKIFINNDW HESKSGRKFA TYNPSTLEKI 

        70         80         90        100        110        120 
CEVEEGDKPD VDKAVEAAQA AFQRGSPWRR LDALSRGQLL HQLADLVERD RAILATLETM 

       130        140        150        160        170        180 
DTGKPFLHAF FVDLEGCIKT FRYFAGWADK IQGRTIPTDD NVVCFTRHEP IGVCGAITPW 

       190        200        210        220        230        240 
NFPLLMLAWK LAPALCCGNT VVLKPAEQTP LTALYLASLI KEVGFPPGVV NIVPGFGPTV 

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

       310        320        330        340        350        360 
CAHQGVFFNQ GQCCTAASRV FVEEQVYGEF VRRSVEFAKK RPVGDPFDAK TEQGPQIDQK 

       370        380        390        400        410        420 
QFDKILELIE SGKKEGAKLE CGGSAMEDRG LFIKPTVFSD VTDNMRIAKE EIFGPVQPIL 

       430        440        450        460        470        480 
KFKNLEEVIK RANSTDYGLT AAVFTKNLDK ALKLAAALES GTVWINCYNA FYAQAPFGGF 

       490        500        510 
KMSGNGRELG EYALAEYTEV KTVTIKLEEK NP

Q9JHW9 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