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P24549 (AL1A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinal dehydrogenase 1

Short name=RALDH 1
Short name=RalDH1
EC=1.2.1.36
Alternative name(s):
ALDH-E1
ALHDII
Aldehyde dehydrogenase family 1 member A1
Aldehyde dehydrogenase, cytosolic
Gene names
Name:Aldh1a1
Synonyms:Ahd-2, Ahd2, Aldh1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 structure

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.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence caution

The sequence AAH44729.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process9-cis-retinoic acid biosynthetic process

Inferred from direct assay PubMed 11876656. Source: MGI

embryonic eye morphogenesis

Inferred from genetic interaction PubMed 16207763PubMed 16611695. Source: MGI

estrous cycle phase

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

midgut development

Inferred from electronic annotation. Source: Ensembl

optic cup morphogenesis involved in camera-type eye development

Inferred from genetic interaction PubMed 16611695. Source: MGI

positive regulation of apoptotic process

Inferred from genetic interaction PubMed 16207763PubMed 16611695. Source: MGI

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from direct assay PubMed 18971422. Source: MGI

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

retinoic acid metabolic process

Inferred from direct assay PubMed 10191271. Source: MGI

retinol metabolic process

Inferred from mutant phenotype PubMed 12851412. Source: MGI

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_function3-chloroallyl aldehyde dehydrogenase activity

Inferred from direct assay PubMed 12610736. Source: MGI

benzaldehyde dehydrogenase (NAD+) activity

Inferred from electronic annotation. Source: Ensembl

retinal dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 501500Retinal dehydrogenase 1
PRO_0000056417

Regions

Nucleotide binding246 – 2516NAD By similarity
Region300 – 3056Antabuse binding

Sites

Active site2691Proton acceptor By similarity
Active site3031Nucleophile By similarity
Binding site4561NAD By similarity
Site1701Transition state stabilizer By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue911N6-acetyllysine By similarity
Modified residue1281N6-acetyllysine By similarity
Modified residue2521N6-acetyllysine By similarity
Modified residue3531N6-acetyllysine By similarity
Modified residue3671N6-acetyllysine By similarity
Modified residue4101N6-acetyllysine By similarity
Modified residue4191N6-acetyllysine By similarity
Modified residue4351N6-acetyllysine By similarity
Modified residue4951N6-acetyllysine By similarity

Experimental info

Sequence conflict81A → R in AAA37202. Ref.1
Sequence conflict81A → R in AAA37203. Ref.1
Sequence conflict451T → S in AAB32754. Ref.2
Sequence conflict511H → Q in AAB32754. Ref.2
Sequence conflict871R → C in AAA37202. Ref.1
Sequence conflict1401I → Y AA sequence Ref.4
Sequence conflict4581M → I in AAA37202. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P24549 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 0E428151B799BD1D

FASTA50154,468
        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 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a cytosolic aldehyde dehydrogenase-encoding cDNA from mouse liver."
Rongnoparut P., Weaver S.
Gene 101:261-265(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: BALB/c and C57BL/6.
Tissue: Liver.
[2]"DNA sequence analysis of the cytosolic acetaldehyde dehydrogenase gene (Ahd-2) in mouse strains with variable ethanol preferences."
Bond S.L., Singh S.M.
Biochem. Med. Metab. Biol. 52:155-159(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/ReJ, BALB/c and C57BL/6J.
Tissue: Liver.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon and Liver.
[4]"Aldehyde dehydrogenase is a positional marker in the retina."
McCaffery P., Tempst P., Lara G., Drager U.C.
Development 112:693-702(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-52; 140-156; 211-230; 309-320; 330-349; 400-410; 421-435 AND 477-490.
Tissue: Embryonic retina.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74570 mRNA. Translation: AAA37202.1.
M74571 Genomic DNA. Translation: AAA37203.1.
S75713 mRNA. Translation: AAB32754.2.
S77047 Genomic DNA. No translation available.
BC044729 mRNA. Translation: AAH44729.1. Different initiation.
BC054386 mRNA. Translation: AAH54386.1.
PIRJQ1004.
RefSeqNP_038495.2. NM_013467.3.
UniGeneMm.250866.

3D structure databases

ProteinModelPortalP24549.
SMRP24549. Positions 9-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP24549. 4 interactions.
MINTMINT-1859401.

PTM databases

PhosphoSiteP24549.

2D gel databases

REPRODUCTION-2DPAGEIPI00626662.
P24549.
SWISS-2DPAGEP24549.

Proteomic databases

PaxDbP24549.
PRIDEP24549.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000087638; ENSMUSP00000084918; ENSMUSG00000053279.
GeneID11668.
KEGGmmu:11668.
UCSCuc008gym.1. mouse.

Organism-specific databases

CTD216.
MGIMGI:1353450. Aldh1a1.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeENSGT00550000074289.
HOGENOMHOG000271505.
HOVERGENHBG000097.
InParanoidP24549.
KOK07249.
OMAYMGSLIK.
OrthoDBEOG7PS1F7.
PhylomeDBP24549.
TreeFamTF300455.

Enzyme and pathway databases

BRENDA1.2.1.36. 3474.
SABIO-RKP24549.
UniPathwayUPA00912.

Gene expression databases

BgeeP24549.
CleanExMM_ALDH1A1.
GenevestigatorP24549.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279287.
PROP24549.
SOURCESearch...

Entry information

Entry nameAL1A1_MOUSE
AccessionPrimary (citable) accession number: P24549
Secondary accession number(s): Q7TQJ0, Q811J0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 138 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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