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Reviewed, UniProtKB/Swiss-Prot P51647 (AL1A1_RAT)

Last modified November 4, 2008. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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: Aldh
OrganismRattus norvegicus (Rat)
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(+) + H(2)O = 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 termDirect protein sequencing

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionretinal dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 501500Retinal dehydrogenase 1
PRO_0000056419

Regions

Nucleotide binding246 – 2516NAD By similarity

Sites

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

Amino acid modifications

Modified residue21N-acetylserine Probable

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
P51647-1 [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: 8543180] [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: 9059608] [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: 9240474] [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: 15489334] [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: 7832787] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-19; 80-91; 96-121; 205-225; 237-258 AND 394-438.
Strain: Sprague-Dawley.
Tissue: Kidney.

Cross-references

Sequence databases

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.
UniGeneRn.6132

3D structure databases

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

Genome annotation databases

EnsemblENSRNOG00000017619. Rattus norvegicus. [Contig view]
GeneID24188.
KEGGrno:24188.

Organism-specific databases

RGD2087. Aldh1a1.

Phylogenomic databases

HOVERGENP51647.

Gene expression databases

ArrayExpressP51647.
GermOnlineENSRNOG00000017619. Rattus norvegicus.

Family and domain databases

InterProIPR016160. Ald_DHase_CS.
IPR016162. Ald_DHase_N.
IPR015590. Aldehyde_DHase.
[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

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: November 4, 2008
This is version 68 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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