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Q2XQV4 (ALDH2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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, mitochondrial

EC=1.2.1.3
Alternative name(s):
ALDH class 2
ALDH-E2
Gene names
Name:ALDH2
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length521 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Is capable of converting retinaldehyde to retinoic acid By similarity.

Catalytic activity

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Pathway

Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processethanol catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaldehyde dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2121Mitochondrion By similarity
Chain22 – 521500Aldehyde dehydrogenase, mitochondrial
PRO_0000312492

Regions

Nucleotide binding266 – 2716NAD By similarity

Sites

Active site2891Proton acceptor By similarity
Active site3231Nucleophile By similarity
Site1901Transition state stabilizer By similarity

Amino acid modifications

Modified residue561N6-acetyllysine By similarity
Modified residue771N6-acetyllysine By similarity
Modified residue1631N6-acetyllysine By similarity
Modified residue3721N6-acetyllysine By similarity
Modified residue3791N6-acetyllysine By similarity
Modified residue3871N6-acetyllysine By similarity
Modified residue4301N6-acetyllysine By similarity
Modified residue4321N6-acetyllysine By similarity
Modified residue4451N6-acetyllysine By similarity
Modified residue4551N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2XQV4 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 12913E10ECD560A7

FASTA52156,921
        10         20         30         40         50         60 
MLRPAALAAA RLVLRQGRRL LSAAPTQAVP APNQQPEIFY NQIFINNEWH DAISKKTFPT 

        70         80         90        100        110        120 
VNPSTGDVIC HVAEGDKEDV DRAVEAARAA FQLGSPWRRL DASDRGRLLN RLADLIERDR 

       130        140        150        160        170        180 
TYLAALETLD NGKPYVISYL VDLDMVLKCL RYYAGWADKY HGKTLPIDGD YFSYTRHEPV 

       190        200        210        220        230        240 
GVCGQIIPWN FPLLMQAWKL GPALATGNVV VMKVSEQTPL TALYVANLIK EAGFPPGVVN 

       250        260        270        280        290        300 
IVPGYGPTAG AAIASHEDVD KVAFTGSTEV GHLIQVAAGK SNLKRVTLEL GGKSPNIIMS 

       310        320        330        340        350        360 
DADMDWAVEQ AHFALFFNQG QCCCAGSRTF VQEDIYAEFV ERSVARARSR VVGNPFDSRT 

       370        380        390        400        410        420 
EQGPQIDETQ FKKILGYIKS GKEEGAKLLC GGGAAADRGY FIQPTVFGDV QDGMTIAKEE 

       430        440        450        460        470        480 
IFGPVMQILK FKTIEEVIGR ANNSKYGLAA AVFTKDLDKA NYLSQALQAG TVWVNCYDVF 

       490        500        510        520 
GAQSPFGGYK LSGSGRELGE YGLQAYTEVK TVTVKVPQKN S 

« Hide

References

[1]Ji Y., Bennett B.M.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ266356 mRNA. Translation: ABB70228.1.
RefSeqNP_001038076.1. NM_001044611.2.
UniGeneSsc.11147.

3D structure databases

ProteinModelPortalQ2XQV4.
SMRQ2XQV4. Positions 29-521.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ2XQV4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000010839; ENSSSCP00000010556; ENSSSCG00000009889.
GeneID733685.
KEGGssc:733685.

Organism-specific databases

CTD217.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeENSGT00550000074289.
HOGENOMHOG000271505.
HOVERGENHBG000097.
KOK00128.
OMAYINTGKQ.
OrthoDBEOG7PS1F7.
TreeFamTF300455.

Enzyme and pathway databases

UniPathwayUPA00780; UER00768.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. 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.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALDH2_PIG
AccessionPrimary (citable) accession number: Q2XQV4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 20, 2005
Last modified: June 11, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways