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Q64057 (AL7A1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 108. 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:
Alpha-aminoadipic semialdehyde dehydrogenase

Short name=Alpha-AASA dehydrogenase
EC=1.2.1.31
Alternative name(s):
Aldehyde dehydrogenase family 7 member A1
EC=1.2.1.3
Antiquitin-1
Betaine aldehyde dehydrogenase
EC=1.2.1.8
Delta1-piperideine-6-carboxylate dehydrogenase
Short name=P6c dehydrogenase
Gene names
Name:Aldh7a1
Synonyms:Ald7a1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism By similarity.

Catalytic activity

(S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H.

Betaine aldehyde + NAD+ + H2O = betaine + NADH.

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

Pathway

Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1.

Subunit structure

Homotetramer By similarity. UniProtKB P83402

Subcellular location

Nucleus By similarity. Cytoplasmcytosol By similarity. Mitochondrion By similarity.

Tissue specificity

Abundant in kidney, liver, cochlea and outer hair cells but not inner hair cells or vestibular type I hair cells. Very low levels in lung, brain, intestine and pancreas. Ref.3 Ref.4

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Mitochondrion Potential
Chain27 – 539513Alpha-aminoadipic semialdehyde dehydrogenase
PRO_0000056492

Regions

Nucleotide binding274 – 2796NAD By similarity

Sites

Active site2961Proton acceptor By similarity
Active site3301Nucleophile By similarity
Site1951Transition state stabilizer By similarity

Amino acid modifications

Modified residue861N6-acetyllysine; alternate By similarity
Modified residue861N6-succinyllysine; alternate By similarity
Modified residue941N6-acetyllysine; alternate By similarity
Modified residue941N6-succinyllysine; alternate By similarity
Modified residue971N6-acetyllysine; alternate By similarity
Modified residue971N6-succinyllysine; alternate By similarity
Modified residue4621N6-acetyllysine By similarity
Modified residue5001N6-acetyllysine By similarity
Modified residue5371N6-succinyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64057 [UniParc].

Last modified April 20, 2010. Version 2.
Checksum: 90F355B926582E77

FASTA53958,749
        10         20         30         40         50         60 
MLRLARPLCV QTVKASKLSR LWSRPAALMS TLLIHHPQYA WLQDLGLRED NEGVFNGSWG 

        70         80         90        100        110        120 
GRGEVITTYC PANNEPIARV RQASMKDYEE TIGKAKKAWN IWADIPAPKR GEIVRKIGDA 

       130        140        150        160        170        180 
LREKIQLLGR LVSLEMGKIL VEGIGEVQEY VDVCDYAAGL SRMIGGPTLP SERPGHALME 

       190        200        210        220        230        240 
QWNPLGLVGI ITAFNFPVAV FGWNNAIALI TGNVCLWKGA PTTSLVSIAV TKIIAKVLED 

       250        260        270        280        290        300 
NLLPGAICSL TCGGADMGTA MARDERVNLL SFTGSTQVGK QVALMVQERF GKSLLELGGN 

       310        320        330        340        350        360 
NAIIAFEDAD LSLVLPSALF AAVGTAGQRC TTVRRLFLHE SIHDEVVDRL KNAYSQIRVG 

       370        380        390        400        410        420 
NPWDPNILYG PLHTKQAVSM FVQAVEEAKK EGGTVVYGGK VMDHPGNYVE PTIVTGLVHD 

       430        440        450        460        470        480 
APIVHKETFA PILYVFKFKN EEEVFEWNNE VKQGLSSSIF TKDLGRIFRW LGPKGSDCGI 

       490        500        510        520        530 
VNVNIPTSGA EIGGAFGGEK HTGGGRESGS DAWKQYMRRS TCTINYSTAL PLAQGIKFQ 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 53-66 AND 144-154, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
[3]"Homology between a human protein and a protein of the green garden pea."
Lee P., Kuhl W., Gelbart T., Kamimura T., West C., Beutler E.
Genomics 21:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 312-539, TISSUE SPECIFICITY.
Tissue: Intestinal mucosa.
[4]"An ancient conserved gene expressed in the human inner ear: identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1)."
Skvorak A.B., Robertson N.G., Yin Y., Weremowicz S., Her H., Bieber F.R., Beisel K.W., Lynch E.D., Beier D.R., Morton C.C.
Genomics 46:191-199(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03109709 Genomic DNA. No translation available.
S75019 mRNA. Translation: AAB31967.2.
PIRB54676.
RefSeqNP_001258034.1. NM_001271105.1.
UniGeneRn.7330.

3D structure databases

ProteinModelPortalQ64057.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4574870.
STRING10116.ENSRNOP00000020325.

Proteomic databases

PaxDbQ64057.
PRIDEQ64057.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000020325; ENSRNOP00000020325; ENSRNOG00000014645.
GeneID291450.
KEGGrno:291450.
UCSCRGD:1308614. rat.

Organism-specific databases

CTD501.
RGD1308614. Aldh7a1.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeENSGT00720000108597.
HOGENOMHOG000271511.
HOVERGENHBG050485.
InParanoidQ64057.
KOK14085.
OMANAIIVFE.
OrthoDBEOG78D7JV.
PhylomeDBQ64057.
TreeFamTF300388.

Enzyme and pathway databases

UniPathwayUPA00529; UER00386.

Gene expression databases

GenevestigatorQ64057.

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.
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.
PROSITEPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio632620.
PROQ64057.

Entry information

Entry nameAL7A1_RAT
AccessionPrimary (citable) accession number: Q64057
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: April 20, 2010
Last modified: June 11, 2014
This is version 108 of the entry and version 2 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