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P51647 (AL1A1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:Aldh
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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

Is capable of converting 9-cis and all-trans retinal to corresponding retinoic acid with high efficiency, 9-cis retinal being 2-fold more active than all-trans retinal.

Catalytic activity

Retinal + NAD+ + H2O = retinoate + NADH.

Enzyme regulation

Inhibited by chloral hydrate.

Pathway

Cofactor metabolism; retinol metabolism.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

Strongly expressed in kidney, lung, testis, intestine, stomach, and trachea, but weakly in the liver.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

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 electronic annotation. Source: Ensembl

9-cis-retinoic acid metabolic process

Inferred from direct assay PubMed 17167544. Source: RGD

estrous cycle phase

Inferred from expression pattern PubMed 18202528. Source: RGD

kidney development

Inferred from expression pattern PubMed 15567713. Source: RGD

liver development

Inferred from expression pattern PubMed 14729401. Source: RGD

midgut development

Inferred from expression pattern PubMed 15964596. Source: RGD

optic cup morphogenesis involved in camera-type eye development

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from direct assay PubMed 10998257. Source: RGD

response to drug

Inferred from expression pattern PubMed 10323328. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 18202528. Source: RGD

response to ethanol

Inferred from direct assay PubMed 17673211. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 18807137. Source: RGD

response to oxidative stress

Inferred from mutant phenotype PubMed 15623782. Source: RGD

response to retinoic acid

Inferred from expression pattern PubMed 11169459. Source: RGD

retinoic acid biosynthetic process

Inferred from mutant phenotype PubMed 21138835. Source: RGD

retinol metabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 21138835. Source: RGD

nucleus

Inferred from direct assay PubMed 21138835. Source: RGD

   Molecular_function3-chloroallyl aldehyde dehydrogenase activity

Traceable author statement Ref.1. Source: RGD

aldehyde dehydrogenase (NAD) activity

Inferred from direct assay PubMed 10998257. Source: RGD

benzaldehyde dehydrogenase (NAD+) activity

Inferred from direct assay PubMed 10998257. Source: RGD

identical protein binding

Inferred from direct assay PubMed 10998257. Source: RGD

retinal dehydrogenase activity

Inferred from direct assay PubMed 17167544. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 501500Retinal dehydrogenase 1
PRO_0000056419

Regions

Nucleotide binding246 – 2516NAD By similarity

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 Probable
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 conflict1001R → C in AAA96657. Ref.1
Sequence conflict1061I → M AA sequence Ref.6
Sequence conflict1701N → E in AAA96657. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P51647 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A3614C21BCE7E144

FASTA50154,459
        10         20         30         40         50         60 
MSSPAQPAVP APLANLKIQH TKIFINNEWH DSVSGKKFPV LNPATEEVIC HVEEGDKADV 

        70         80         90        100        110        120 
DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLMERDR LLLATIEAIN GGKVFANAYL 

       130        140        150        160        170        180 
SDLGGSIKAL KYCAGWADKI HGQTIPSDGD IFTFTRREPI GVCGQIIPWN FPLLMFIWKI 

       190        200        210        220        230        240 
GPALSCGNTV VVKPAEQTPL TALHMASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD 

       250        260        270        280        290        300 
KVAFTGSTQV GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDIAVEF AHHGVFYHQG 

       310        320        330        340        350        360 
QCCVAASRIF VEESVYDEFV RKSVERAKKY VLGNPLTQGI NQGPQIDKEQ HDKILDLIES 

       370        380        390        400        410        420 
GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSIDDVIKR 

       430        440        450        460        470        480 
ANNTTYGLAA GVFTKDLDRA ITVSSALQAG VVWVNCYMIL SAQCPFGGFK MSGNGRELGE 

       490        500 
HGLYEYTELK TVAMKISQKN S 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a cDNA encoding rat aldehyde dehydrogenase with high activity for retinal oxidation."
Bhat P.V., Labrecque J., Boutin J.-M., Lacroix A., Yoshida A.
Gene 166:303-306(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Kidney.
[2]"A preliminary report on the cloning of a constitutively expressed rat liver cytosolic ALDH cDNA by PCR."
Kathmann E.C., Lipsky J.J.
Adv. Exp. Med. Biol. 414:69-72(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[3]"Cloning of a cDNA encoding a constitutively expressed rat liver cytosolic aldehyde dehydrogenase."
Kathmann E.C., Lipsky J.J.
Biochem. Biophys. Res. Commun. 236:527-531(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[4]"Cloning of a rat cDNA encoding retinal dehydrogenase isozyme type I and its expression in E. coli."
Napoli J.L., Penzes P., Wang X., Sperkova Z.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pituitary.
[6]"A novel isoenzyme of aldehyde dehydrogenase specifically involved in the biosynthesis of 9-cis and all-trans retinoic acid."
Labrecque J., Dumas F., Lacroix A., Bhat P.V.
Biochem. J. 305:681-684(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-19; 80-91; 96-121; 205-225; 237-258 AND 394-438.
Strain: Sprague-Dawley.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42009 mRNA. Translation: AAA96657.1.
AF001896 mRNA. Translation: AAC53304.1.
AF001898 mRNA. Translation: AAC53306.1.
AF001897 mRNA. Translation: AAC53305.1.
U79118 mRNA. Translation: AAB63423.1.
BC061526 mRNA. Translation: AAH61526.1.
PIRJC4524.
JC5553.
RefSeqNP_071852.2. NM_022407.3.
XP_006231218.1. XM_006231156.1.
XP_006231219.1. XM_006231157.1.
XP_006231220.1. XM_006231158.1.
UniGeneRn.6132.

3D structure databases

ProteinModelPortalP51647.
SMRP51647. Positions 9-501.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP51647.
ChEMBLCHEMBL2931.

PTM databases

PhosphoSiteP51647.

Proteomic databases

PaxDbP51647.
PRIDEP51647.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000024000; ENSRNOP00000024000; ENSRNOG00000017619.
GeneID24188.
KEGGrno:24188.
UCSCRGD:2087. rat.

Organism-specific databases

CTD216.
RGD2087. Aldh1a1.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeENSGT00550000074289.
HOGENOMHOG000271505.
HOVERGENHBG000097.
KOK07249.
OMAEWHDSAS.
OrthoDBEOG7PS1F7.
PhylomeDBP51647.
TreeFamTF300455.

Enzyme and pathway databases

BRENDA1.2.1.36. 5301.
SABIO-RKP51647.
UniPathwayUPA00912.

Gene expression databases

GenevestigatorP51647.

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_CYS.
IPR029510. Ald_DH_CS_GLU.
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

NextBio602555.

Entry information

Entry nameAL1A1_RAT
AccessionPrimary (citable) accession number: P51647
Secondary accession number(s): O09184
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 113 of the entry and version 3 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