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P11883 (AL3A1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde dehydrogenase, dimeric NADP-preferring
EC=1.2.1.5
Alternative name(s):
Aldehyde dehydrogenase family 3 member A1
HTC-ALDH
Tumor-associated aldehyde dehydrogenase
Gene names
Name:Aldh3a1
Synonyms:Aldd, Aldh3
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes.

Catalytic activity

An aldehyde + NAD(P)+ + H2O = a carboxylate + NAD(P)H.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Induction

This protein can be induced by a number of chemical carcinogens during rat hepatocarcinogenesis.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 453452Aldehyde dehydrogenase, dimeric NADP-preferring
PRO_0000056472

Regions

Nucleotide binding188 – 1936NAD or NADP By similarity

Sites

Active site2101 By similarity
Active site2441 By similarity

Amino acid modifications

Modified residue1781N6-acetyllysine By similarity
Modified residue1941N6-acetyllysine By similarity
Modified residue2691N6-acetyllysine By similarity

Secondary structure

1 ................................................................................... 453
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11883 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 15C501BAB4F9845A

FASTA45350,339
        10         20         30         40         50         60 
MSSISDTVKR AREAFNSGKT RSLQFRIQQL EALQRMINEN LKSISGALAS DLGKNEWTSY 

        70         80         90        100        110        120 
YEEVAHVLEE LDTTIKELPD WAEDEPVAKT RQTQQDDLYI HSEPLGVVLV IGAWNYPFNL 

       130        140        150        160        170        180 
TIQPMVGAVA AGNAVILKPS EVSGHMADLL ATLIPQYMDQ NLYLVVKGGV PETTELLKER 

       190        200        210        220        230        240 
FDHIMYTGST AVGKIVMAAA AKHLTPVTLE LGGKSPCYVD KDCDLDVACR RIAWGKFMNS 

       250        260        270        280        290        300 
GQTCVAPDYI LCDPSIQNQI VEKLKKSLKD FYGEDAKQSR DYGRIINDRH FQRVKGLIDN 

       310        320        330        340        350        360 
QKVAHGGTWD QSSRYIAPTI LVDVDPQSPV MQEEIFGPVM PIVCVRSLEE AIQFINQREK 

       370        380        390        400        410        420 
PLALYVFSNN EKVIKKMIAE TSSGGVTAND VIVHITVPTL PFGGVGNSGM GAYHGKKSFE 

       430        440        450 
TFSHRRSCLV KSLLNEEAHK ARYPPSPAKM PRH

« Hide

References

« Hide 'large scale' references
[1]"Cloning and complete nucleotide sequence of a full-length cDNA encoding a catalytically functional tumor-associated aldehyde dehydrogenase."
Jones D.E., Brennan M.D., Hempel J., Lindahl R.
Proc. Natl. Acad. Sci. U.S.A. 85:1782-1786(1988) [PubMed: 2831537] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: Lung.
[3]"Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria."
Hempel J., Harper K., Lindahl R.
Biochemistry 28:1160-1167(1989) [PubMed: 2713359] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[4]"Organization and characterization of the rat class 3 aldehyde dehydrogenase gene."
Asman D.C., Takimoto K., Pitot H.C., Dunn T.J., Lindahl R.
J. Biol. Chem. 268:12530-12536(1993) [PubMed: 8509394] [Abstract]
Cited for: GENE STRUCTURE.
[5]"Preliminary crystallographic analysis of class 3 rat liver aldehyde dehydrogenase."
Rose J.P., Hempel J., Kuo I., Lindahl R., Wang B.-C.
Proteins 8:305-308(1990) [PubMed: 2091023] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[6]"The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold."
Liu Z.-J., Sun Y.J., Rose J.P., Chung Y.-J., Hsiao C.D., Chang W.-R., Kuo I., Perozich J., Lindahl R., Hempel J., Wang B.-C.
Nat. Struct. Biol. 4:317-326(1997) [PubMed: 9095201] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J03637 mRNA. Translation: AAA40713.1.
BC070924 mRNA. Translation: AAH70924.1.
IPIIPI00231064.
PIRA30149.
RefSeqNP_114178.1. NM_031972.1.
UniGeneRn.105627.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AD3X-ray2.60A/B3-453[»]
ProteinModelPortalP11883.
SMRP11883. Positions 3-448.
ModBaseSearch...

Protein-protein interaction databases

IntActP11883. 1 interaction.
STRINGP11883.

Proteomic databases

PRIDEP11883.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000003182; ENSRNOP00000003182; ENSRNOG00000002331.
GeneID25375.
KEGGrno:25375.
NMPDRfig|10116.3.peg.5198.
UCSCBC070924. rat.

Organism-specific databases

CTD218.
RGD2088. Aldh3a1.

Phylogenomic databases

eggNOGroNOG08165.
GeneTreeENSGT00390000002825.
HOVERGENHBG050483.
InParanoidP11883.
OMALQFRIQQ.
OrthoDBEOG49CQ7Q.
PhylomeDBP11883.

Gene expression databases

ArrayExpressP11883.
GenevestigatorP11883.
GermOnlineENSRNOG00000002331. Rattus norvegicus.

Family and domain databases

InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR012394. Aldehyde_DH_NAD(P).
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
KOK00129.
PANTHERPTHR11699:SF15. ALDH. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF036492. ALDH. 1 hit.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio606401.

Entry information

Entry nameAL3A1_RAT
AccessionPrimary (citable) accession number: P11883
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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