Aldehyde dehydrogenase family 1 member A3

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Reviewed, UniProtKB/Swiss-Prot Q9JHW9 (AL1A3_MOUSE)

Last modified November 3, 2009. Version 69. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Aldehyde dehydrogenase family 1 member A3
    EC=1.2.1.5
Alternative name(s):
    Aldehyde dehydrogenase 6
    Retinaldehyde dehydrogenase 3
      Short name=RALDH-3

Gene names

Name:	Aldh1a3
Synonyms:	Aldh6, Raldh3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	512 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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General annotation (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. Ref.1 Ref.2 Ref.3 Ref.4
Catalytic activity	An aldehyde + NAD(P)⁺ + H₂O = an acid + NAD(P)H.
Pathway	Cofactor metabolism; retinol metabolism.
Subcellular location	Cytoplasm. Ref.4
Tissue specificity	Ventral retina. Ref.1 Ref.2 Ref.3 Ref.4
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. Ref.2
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

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Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation
Gene Ontology (GO)
Biological process	face development Inferred from genetic interaction. Source: MGI nucleus accumbens development Inferred from mutant phenotype. Source: MGI olfactory pit development Inferred from mutant phenotype. Source: MGI optic cup morphogenesis involved in camera-type eye development Inferred from genetic interaction. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of apoptosis Inferred from genetic interaction. Source: MGI retinoic acid biosynthetic process Ref.3 Ref.4 Inferred from direct assay. Source: MGI
Cellular component	cytoplasm Inferred from direct assay. Source: MGI
Molecular function	3-chloroallyl aldehyde dehydrogenase activity Ref.1 Traceable author statement. Source: MGI NAD binding Inferred from direct assay. Source: MGI aldehyde dehydrogenase (NAD) activity Ref.4 Inferred from direct assay. Source: MGI aldehyde dehydrogenase [NAD(P)+] activity Ref.3 Inferred from direct assay. Source: MGI thyroid hormone binding Inferred from physical interaction. Source: MGI
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 512

511

Aldehyde dehydrogenase family 1 member A3

PRO_0000056479

Regions

Nucleotide binding

257 – 262

NAD By similarity

Sites

Active site

280

Proton acceptor By similarity

Active site

314

Nucleophile By similarity

Site

181

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Experimental info

Sequence conflict

L → V in AAF67736. Ref.1

Sequence conflict

208

Q → R in AAG33935. Ref.4

Sequence conflict

223

V → E in AAF67736. Ref.1

Sequence conflict

341

R → S in AAG33935. Ref.4

Sequence conflict

407

I → R in AAF67736. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9JHW9-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 5BBC6DEE41E58CFE
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FASTA

512

56,157

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A retinoic acid synthesizing enzyme in ventral retina and telencephalon of the embryonic mouse." Li H., Wagner E., McCaffery P., Smith D., Andreadis A., Drager U.C. Mech. Dev. 95:283-289(2000) [PubMed: 10906479] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Strain: B6/D2.
[2]	"RALDH3, a retinaldehyde dehydrogenase that generates retinoic acid, is expressed in the ventral retina, otic vesicle and olfactory pit during mouse development." Mic F.A., Molotkov A., Fan X., Cuenca A.E., Duester G. Mech. Dev. 97:227-230(2000) [PubMed: 11025231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY. Strain: C57BL/6 X 129/SvJ. Tissue: Kidney.
[3]	"Identification of RALDH-3, a novel retinaldehyde dehydrogenase, expressed in the ventral region of the retina." Suzuki R., Shintani T., Sakuta H., Kato A., Ohkawara T., Osumi N., Noda M. Mech. Dev. 98:37-50(2000) [PubMed: 11044606] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Strain: C57BL/6J. Tissue: Retina.
[4]	"Aldehyde dehydrogenase 6, a cytosolic retinaldehyde dehydrogenase prominently expressed in sensory neuroepithelia during development." Grun F., Hirose Y., Kawauchi S., Ogura T., Umesono K. J. Biol. Chem. 275:41210-41218(2000) [PubMed: 11013254] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]	"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]. Strain: FVB/N. Tissue: Mammary tumor.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	AF253409 mRNA. Translation: AAF67736.1. AF280404 mRNA. Translation: AAF86980.1. AF246711 mRNA. Translation: AAG38488.1. AF152359 mRNA. Translation: AAG33935.1. BC058277 mRNA. Translation: AAH58277.1.
IPI	IPI00310215.
RefSeq	NP_444310.3.
UniGene	Mm.140988
3D structure databases
HSSP	HSSP built from PDB template 1BXS based on UniProtKB P51977.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9JHW9.
Proteomic databases
PRIDE	Q9JHW9.
Genome annotation databases
Ensembl	ENSMUST00000015278; ENSMUSP00000015278; ENSMUSG00000015134; Mus musculus. [Genome view]
GeneID	56847.
KEGG	mmu:56847.
NMPDR	fig\|10090.3.peg.16667.
UCSC	uc009hhi.1. mouse.
Organism-specific databases
CTD	56847.
MGI	MGI:1861722. Aldh1a3.
Phylogenomic databases
HOGENOM	Q9JHW9.
HOVERGEN	Q9JHW9.
OMA	GLFIKPT.
Enzyme and pathway databases
BRENDA	1.2.1.36. 244. 1.2.1.5. 244.
Gene expression databases
ArrayExpress	Q9JHW9.
Bgee	Q9JHW9.
CleanEx	MM_ALDH1A3.
Genevestigator	Q9JHW9.
GermOnline	ENSMUSG00000015134. Mus musculus.
Family and domain databases
InterPro	IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	313405.
SOURCE	Search...

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Entry information

Entry name

AL1A3_MOUSE

Accession

Primary (citable) accession number: Q9JHW9
Secondary accession number(s): Q9EQP7, Q9JI72

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents