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Protein

Aldehyde dehydrogenase, dimeric NADP-preferring

Gene

Aldh3a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei210 – 2101By similarity
Active sitei244 – 2441By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi188 – 1936NAD or NADPBy similarity

GO - Molecular functioni

GO - Biological processi

  • aging Source: RGD
  • cellular aldehyde metabolic process Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • positive regulation of cell proliferation Source: RGD
  • response to cAMP Source: RGD
  • response to drug Source: RGD
  • response to glucocorticoid Source: RGD
  • response to hypoxia Source: RGD
  • response to nutrient Source: RGD
  • response to organic cyclic compound Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

ReactomeiR-RNO-211945. Phase 1 - Functionalization of compounds.
SABIO-RKP11883.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Aldh3a1
Synonyms:Aldd, Aldh3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi2088. Aldh3a1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: Ensembl
  • extracellular space Source: Ensembl
  • integral component of membrane Source: Ensembl
  • nucleoplasm Source: Ensembl
  • plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 453452Aldehyde dehydrogenase, dimeric NADP-preferringPRO_0000056472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei178 – 1781N6-acetyllysineBy similarity
Modified residuei194 – 1941N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP11883.
PRIDEiP11883.

Expressioni

Inductioni

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

Gene expression databases

GenevisibleiP11883. RN.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

IntActiP11883. 1 interaction.
STRINGi10116.ENSRNOP00000003182.

Structurei

Secondary structure

1
453
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1613Combined sources
Helixi19 – 213Combined sources
Helixi23 – 5230Combined sources
Helixi56 – 627Combined sources
Helixi64 – 8219Combined sources
Turni92 – 954Combined sources
Beta strandi96 – 1049Combined sources
Beta strandi106 – 1116Combined sources
Beta strandi114 – 1163Combined sources
Helixi119 – 13012Combined sources
Beta strandi134 – 1385Combined sources
Helixi144 – 15714Combined sources
Turni160 – 1623Combined sources
Beta strandi163 – 1653Combined sources
Helixi170 – 1767Combined sources
Beta strandi182 – 1887Combined sources
Helixi190 – 20112Combined sources
Turni202 – 2043Combined sources
Beta strandi207 – 2104Combined sources
Beta strandi216 – 2194Combined sources
Beta strandi221 – 2233Combined sources
Helixi225 – 23713Combined sources
Turni238 – 2414Combined sources
Beta strandi249 – 2524Combined sources
Helixi254 – 2563Combined sources
Helixi257 – 27216Combined sources
Helixi276 – 2783Combined sources
Helixi288 – 2969Combined sources
Turni297 – 3004Combined sources
Beta strandi303 – 3053Combined sources
Turni311 – 3144Combined sources
Beta strandi319 – 3213Combined sources
Helixi329 – 3313Combined sources
Beta strandi337 – 3404Combined sources
Beta strandi342 – 3443Combined sources
Helixi348 – 3569Combined sources
Beta strandi362 – 3676Combined sources
Helixi371 – 3788Combined sources
Beta strandi384 – 3929Combined sources
Helixi393 – 3964Combined sources
Helixi406 – 4083Combined sources
Helixi416 – 4216Combined sources
Beta strandi423 – 4308Combined sources
Helixi440 – 4423Combined sources
Beta strandi443 – 4453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AD3X-ray2.60A/B3-453[»]
ProteinModelPortaliP11883.
SMRiP11883. Positions 3-448.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11883.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiKOG2456. Eukaryota.
COG1012. LUCA.
GeneTreeiENSGT00390000002825.
HOGENOMiHOG000271515.
HOVERGENiHBG050483.
InParanoidiP11883.
KOiK00129.
OMAiNDSTEID.
OrthoDBiEOG73RBB3.
PhylomeDBiP11883.
TreeFamiTF314264.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR012394. Aldehyde_DH_NAD(P).
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF036492. ALDH. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11883-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSISDTVKR AREAFNSGKT RSLQFRIQQL EALQRMINEN LKSISGALAS
60 70 80 90 100
DLGKNEWTSY YEEVAHVLEE LDTTIKELPD WAEDEPVAKT RQTQQDDLYI
110 120 130 140 150
HSEPLGVVLV IGAWNYPFNL TIQPMVGAVA AGNAVILKPS EVSGHMADLL
160 170 180 190 200
ATLIPQYMDQ NLYLVVKGGV PETTELLKER FDHIMYTGST AVGKIVMAAA
210 220 230 240 250
AKHLTPVTLE LGGKSPCYVD KDCDLDVACR RIAWGKFMNS GQTCVAPDYI
260 270 280 290 300
LCDPSIQNQI VEKLKKSLKD FYGEDAKQSR DYGRIINDRH FQRVKGLIDN
310 320 330 340 350
QKVAHGGTWD QSSRYIAPTI LVDVDPQSPV MQEEIFGPVM PIVCVRSLEE
360 370 380 390 400
AIQFINQREK PLALYVFSNN EKVIKKMIAE TSSGGVTAND VIVHITVPTL
410 420 430 440 450
PFGGVGNSGM GAYHGKKSFE TFSHRRSCLV KSLLNEEAHK ARYPPSPAKM

PRH
Length:453
Mass (Da):50,339
Last modified:January 23, 2007 - v3
Checksum:i15C501BAB4F9845A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03637 mRNA. Translation: AAA40713.1.
BC070924 mRNA. Translation: AAH70924.1.
PIRiA30149.
RefSeqiNP_114178.1. NM_031972.1.
UniGeneiRn.105627.

Genome annotation databases

EnsembliENSRNOT00000003182; ENSRNOP00000003182; ENSRNOG00000002331.
GeneIDi25375.
KEGGirno:25375.
UCSCiRGD:2088. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03637 mRNA. Translation: AAA40713.1.
BC070924 mRNA. Translation: AAH70924.1.
PIRiA30149.
RefSeqiNP_114178.1. NM_031972.1.
UniGeneiRn.105627.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AD3X-ray2.60A/B3-453[»]
ProteinModelPortaliP11883.
SMRiP11883. Positions 3-448.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP11883. 1 interaction.
STRINGi10116.ENSRNOP00000003182.

Proteomic databases

PaxDbiP11883.
PRIDEiP11883.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000003182; ENSRNOP00000003182; ENSRNOG00000002331.
GeneIDi25375.
KEGGirno:25375.
UCSCiRGD:2088. rat.

Organism-specific databases

CTDi218.
RGDi2088. Aldh3a1.

Phylogenomic databases

eggNOGiKOG2456. Eukaryota.
COG1012. LUCA.
GeneTreeiENSGT00390000002825.
HOGENOMiHOG000271515.
HOVERGENiHBG050483.
InParanoidiP11883.
KOiK00129.
OMAiNDSTEID.
OrthoDBiEOG73RBB3.
PhylomeDBiP11883.
TreeFamiTF314264.

Enzyme and pathway databases

ReactomeiR-RNO-211945. Phase 1 - Functionalization of compounds.
SABIO-RKP11883.

Miscellaneous databases

EvolutionaryTraceiP11883.
PROiP11883.

Gene expression databases

GenevisibleiP11883. RN.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR012394. Aldehyde_DH_NAD(P).
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF036492. ALDH. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Entry informationi

Entry nameiAL3A1_RAT
AccessioniPrimary (citable) accession number: P11883
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.