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Reviewed, UniProtKB/Swiss-Prot Q63639 (AL1A2_RAT)

Last modified January 19, 2010. Version 84. 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

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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)
Gene names
Name: Aldh1a2
Synonyms: Raldh2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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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.

Catalytic activity

Retinal + NAD+ + H2O = retinoate + NADH.

Pathway

Cofactor metabolism; retinol metabolism.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Tissue specificity

Found in testis and less abundantly in lung, brain, heart, liver and kidney.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 518518Retinal dehydrogenase 2
PRO_0000056424

Regions

Nucleotide binding263 – 2686NAD By similarity

Sites

Active site2861Proton acceptor
Active site3201Nucleophile
Site1871Transition state stabilizer

Amino acid modifications

Modified residue1191Phosphothreonine By similarity
Modified residue1221Phosphothreonine By similarity

Secondary structure

1 .................................................................................. 518
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q63639-1 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 2BDDAABB0D2D066C

FASTA51856,640
        10         20         30         40         50         60 
MTSSEIAMPG EVKADPAALM ASLQLLPSPT PNLEIKYTKI FINNEWQNSE SGRVFPVCNP 

        70         80         90        100        110        120 
ATGEQVCEVQ EADKVDIDKA VQAARLAFSL GSVWRRMDAS ERGRLLDKLA DLVERDRATL 

       130        140        150        160        170        180 
ATMESLNGGK PFLQAFYIDL QGVIKTLRYY AGWADKIHGM TIPVDGDYFT FTRHEPIGVC 

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

       250        260        270        280        290        300 
GYGPTAGAAI ASHIGIDKIA FTGSTEVGKL IQEAAGRSNL KRVTLELGGK SPNIIFADAD 

       310        320        330        340        350        360 
LDYAVEQAHQ GVFFNQGQCC TAGSRIFVEE SIYEEFVKRS VERAKRRIVG SPFDPTTEQG 

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

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

       490        500        510 
SPFGGFKMSG NGREMGEFGL REYSEVKTVT VKIPQKNS

« Hide

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References

« Hide 'large scale' references
[1]"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: Testis.
[2]"Cloning of a cDNA encoding an aldehyde dehydrogenase and its expression in Escherichia coli. Recognition of retinal as substrate."
Wang X., Penzes P., Napoli J.L.
J. Biol. Chem. 271:16288-16293(1996) [PubMed: 8663198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-518.
Tissue: Testis.
[3]"The structure of retinal dehydrogenase type II at 2.7 A resolution: implications for retinal specificity."
Lamb A.L., Newcomer M.E.
Biochemistry 38:6003-6011(1999) [PubMed: 10320326] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 20-518.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC098910 mRNA. Translation: AAH98910.1.
U60063 mRNA. Translation: AAC52637.1. Different initiation.
IPIIPI00211419.
RefSeqNP_446348.2.
UniGeneRn.10514

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BI9X-ray2.70A/B/C/D20-518[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ63639.

Genome annotation databases

EnsemblENSRNOT00000021757; ENSRNOP00000021757; ENSRNOG00000016042; Rattus norvegicus. [Genome view]
GeneID116676.
KEGGrno:116676.
NMPDRfig|10116.3.peg.28888.
UCSCBC098910. rat.

Organism-specific databases

CTD116676.
RGD620250. Aldh1a2.

Phylogenomic databases

eggNOGmaNOG14172.
HOVERGENQ63639.
InParanoidQ63639.
OMAHVGIDKI.
OrthoDBEOG9WWV4D.
PhylomeDBQ63639.

Enzyme and pathway databases

BRENDA1.2.1.36. 248.

Gene expression databases

ArrayExpressQ63639.
GenevestigatorQ63639.
GermOnlineENSRNOG00000016042. Rattus norvegicus.

Family and domain databases

InterProIPR016161. Ald_DH/histidinol_DH.
IPR016160. 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

NextBio619506.

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Entry information

Entry nameAL1A2_RAT
AccessionPrimary (citable) accession number: Q63639
Secondary accession number(s): Q4FZY8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 7, 2006
Last modified: January 19, 2010
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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