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Reviewed, UniProtKB/Swiss-Prot Q8MI17 (AL1A1_RABIT)

Last modified June 16, 2009. Version 39. 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
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Can convert/oxidize retinaldehyde to retinoic acid By similarity.

Catalytic activity

Retinal + NAD+ + H2O = retinoate + NADH.

Pathway

Cofactor metabolism; retinol metabolism.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionretinal dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 496496Retinal dehydrogenase 1
PRO_0000056418

Regions

Nucleotide binding241 – 2466NAD By similarity

Sites

Active site2641Proton acceptor By similarity
Active site2981Nucleophile By similarity
Site1651Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8MI17-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 4BD963CF015FD164

FASTA49654,341
        10         20         30         40         50         60 
MADLPTPLTN LKIQYTKIFI NNEWHDSVSG KKFPVLNPAT EEQICLIEEG DKADVDKAVK 

        70         80         90        100        110        120 
AARQAFQIGS PWRTMDASER GRLLYKLADL IERDRLLLAT MESLNAGKLF PNAYLMDLGG 

       130        140        150        160        170        180 
CIKTLRYCAG WADKIQGRTM PMDGDFFCYT RHEPVGVCGQ IIPWNFPLVM LIWKIGPALS 

       190        200        210        220        230        240 
CGNTVIVKPA EQTPLTALHV ASLIKEAGFP PGVVNIVPGY GPTAGAAISS HMDIDKVAFT 

       250        260        270        280        290        300 
GSTEVGKLIK EAAGKSNLKR VTLELGGKSP CIVFADADLD NAVEFAHQGV FYHQGQCCIA 

       310        320        330        340        350        360 
ASRLFVEESI YDEFVRRSVE RAKKYVLGNP LAPEVNQGPQ IDKEQYNKIL DLIESGKKEG 

       370        380        390        400        410        420 
AKLECGGGPW GNKGYFIQPT VFSNVTDEMR IAKEEIFGPV QQIMKFKSLD DVIKRANNTT 

       430        440        450        460        470        480 
YGLSAGIFTK DLDKAVTVSS ALQAGTVWVN CYSVVSAQVP FGGFKMSGNG RELGEYGLQQ 

       490 
YTEVKTVTVK ISQKNS 

« Hide

References

[1]"Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA."
Manzer R., Qamar L., Estey T., Pappa A., Petersen D.R., Vasiliou V.
DNA Cell Biol. 22:329-338(2003) [PubMed: 12941160] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cornea.

Cross-references

Sequence databases

AY038801 mRNA. Translation: AAK72097.1.
UniGeneOcu.1307

3D structure databases

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

Phylogenomic databases

HOVERGENQ8MI17.

Enzyme and pathway databases

BRENDA1.2.1.36. 255.

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...

Entry information

Entry nameAL1A1_RABIT
AccessionPrimary (citable) accession number: Q8MI17
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 39 of the entry and version 1 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