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Reviewed, UniProtKB/Swiss-Prot Q9I8W8 (AL1A2_TAEGU)

Last modified June 16, 2009. Version 38. 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 2
      Short name=RALDH 2
      Short name=RalDH2
    EC=1.2.1.36
Alternative name(s):
    Aldehyde dehydrogenase family 1 member A2
    Retinaldehyde-specific dehydrogenase type 2
      Short name=RALDH(II)
    zRalDH
Gene names
Name: ALDH1A2
Synonyms: RALDH2
OrganismTaeniopygia guttata (Zebra finch) (Poephila guttata)
Taxonomic identifier59729 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaePasseriformesPasseroideaEstrildidaeEstrildinaeTaeniopygia

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently By similarity. It is responsible for the ability of brain sites to synthesize retinoic acid. Its activity in the high vocal center (HVC) is required for the song of juvenile zebra finches to become stereotyped.

Catalytic activity

Retinal + NAD+ + H2O = retinoate + NADH.

Pathway

Cofactor metabolism; retinol metabolism.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in the high vocal center (HVC) which integrates auditory and motor activities and constitutes a nodal nucleus on the song system. Ref.1

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 – 517517Retinal dehydrogenase 2
PRO_0000225600

Regions

Nucleotide binding263 – 2686NAD By similarity

Sites

Active site2861Proton acceptor By similarity
Active site3201Nucleophile By similarity
Site1871Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9I8W8-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: D842A2A1BF4DA109

FASTA51756,596
        10         20         30         40         50         60 
MTSSKIEMPG EVKADPAALM ASLHLLPSPT LNLEIKYTKI FINNEWQNSE SGRIFPVYNP 

        70         80         90        100        110        120 
ATGEQICDIQ EADKVDTDKA VRAARLAFSL GSVWRRMDAS ERGHLLDKLA DLVERDRAIL 

       130        140        150        160        170        180 
ATMESLNSGK PFLQAFYVDL QGVIKTLRYY AGWADKIHGM TIPVDGDYFT FTRHEPIGVC 

       190        200        210        220        230        240 
GQIIPWNFPL LMFAWKIAPA LCCGNTVVIK PAEQTPLSAL YMGALIKEAG FPPGVVNILP 

       250        260        270        280        290        300 
GFGPIVGAAI ASHVGIDKIA FTGSTEVGKL IQEAAGRSNL KRVTLELGGK SPNIIFADAD 

       310        320        330        340        350        360 
LDYAVEQAHQ GVFFNQGQCC TAGSRIYVEE SIYEEFVRKS VKRAKRKIVG SPFDPTTEQG 

       370        380        390        400        410        420 
PQIDKKQYNK ILELIQSGIT EGAKLECGGK GLGRKGFFIE PTVFSNVTDD MRIAKEEIFG 

       430        440        450        460        470        480 
PVQEILRFKT MDEVIERANN SDFGLVAAVF TNDINKALTV SSAMQAGTVW INCYNALNAQ 

       490        500        510 
SPFGGSKSGN GREMGECGLR EYSEVKTVTI KIPQENS 

« Hide

References

[1]"Site-specific retinoic acid production in the brain of adult songbirds."
Denisenko-Nehrbass N.I., Jarvis E., Scharff C., Nottebohm F., Mello C.V.
Neuron 27:359-370(2000) [PubMed: 10985355] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.

Cross-references

Sequence databases

AF162770 mRNA. Translation: AAF80471.1.
RefSeqNP_001070153.1.
UniGeneTgu.6744

3D structure databases

HSSPHSSP built from PDB template 1BI9 based on UniProtKB Q63639.
ModBaseSearch...

Genome annotation databases

EnsemblENSTGUG00000006178. Taeniopygia guttata. [Contig view]
GeneID751771.
KEGGtgu:751771.

Phylogenomic databases

HOVERGENQ9I8W8.

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 nameAL1A2_TAEGU
AccessionPrimary (citable) accession number: Q9I8W8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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