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Reviewed, UniProtKB/Swiss-Prot P24549 (AL1A1_MOUSE)

Last modified November 3, 2009. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

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 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
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
P24549-1 [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: 2055490] [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: 7993664] [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: 15489334] [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: 1935685] [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

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.
IPIIPI00626662.
PIRJQ1004.
RefSeqNP_038495.2.
UniGeneMm.435667

3D structure databases

HSSPHSSP built from PDB template 1BXS based on UniProtKB P51977.
ModBaseSearch...

Protein-protein interaction databases

STRINGP24549.

PTM databases

PhosphoSiteP24549.

2-D gel databases

SWISS-2DPAGEP24549.
REPRODUCTION-2DPAGEP24549.

Proteomic databases

PRIDEP24549.

Genome annotation databases

EnsemblENSMUST00000087638; ENSMUSP00000084918; ENSMUSG00000053279; Mus musculus. [Genome view]
GeneID11668.
KEGGmmu:11668.
UCSCuc008gym.1. mouse.

Organism-specific databases

CTD11668.
MGIMGI:1353450. Aldh1a1.

Phylogenomic databases

HOGENOMP24549.
HOVERGENP24549.
OMAVNCYSVV.

Enzyme and pathway databases

BRENDA1.2.1.36. 244.

Gene expression databases

ArrayExpressP24549.
BgeeP24549.
CleanExMM_ALDH1A1.
GenevestigatorP24549.
GermOnlineENSMUSG00000053279. Mus musculus.

Family and domain databases

InterProIPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio279287.
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: November 3, 2009
This is version 101 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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) · Sequences · References · Cross-references · Entry information · Relevant documents