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Q9DBF1 (AL7A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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

Mitochondrion. Nucleus. Cytoplasm › cytosol Ref.3.

Tissue specificity

Present in liver, kidney, brain and pancreas, and at lower levels in jejunum, duodenum, stomach and testes (at protein level). Ref.3

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence caution

The sequence AAH12407.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay. Source: MGI

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-aminoadipate-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: EC

betaine-aldehyde dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9DBF1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9DBF1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Mitochondrion Potential
Chain27 – 539513Alpha-aminoadipic semialdehyde dehydrogenase
PRO_0000056491

Regions

Nucleotide binding274 – 2796NAD By similarity

Sites

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

Natural variations

Alternative sequence1 – 2828Missing in isoform 2.
VSP_038989

Experimental info

Sequence conflict1641I → M in BAE26715. Ref.1
Sequence conflict4671I → V in BAE35641. Ref.1
Sequence conflict4911E → G in BAE35641. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 20, 2010. Version 4.
Checksum: 7591EE5652F2577E

FASTA53958,861
        10         20         30         40         50         60 
MWRVPRRLCV QSVKTSKLSG PWSRPAAHMS TLLIHHPQYA WLQDLGLRED NEGVYNGSWG 

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

       130        140        150        160        170        180 
FREKIQLLGR LVSLEMGKIL VEGIGEVQEY VDVCDYAAGL SRMIGGPTLP SERPGHALIE 

       190        200        210        220        230        240 
MWNPLGLVGI ITAFNFPVAV FGWNNAIALI TGNVCLWKGA PTTSLVSVAV TKIIAQVLED 

       250        260        270        280        290        300 
NLLPGAICSL VCGGADIGTT MARDERVNLL SFTGSTQVGK EVALMVQERF GKSLLELGGN 

       310        320        330        340        350        360 
NAIIAFEDAD LSLVVPSVLF AAVGTAGQRC TTVRRLFLHE SIHNEVVDRL RSAYSQIRVG 

       370        380        390        400        410        420 
NPWDPNILYG PLHTKQAVSM FVRAVEEAKK QGGTVVYGGK VMDHPGNYVE PTIVTGLAHD 

       430        440        450        460        470        480 
APIVHQETFA PILYVFKFQD EEEVFEWNNE VKQGLSSSIF TKDLGRIFRW LGPKGSDCGI 

       490        500        510        520        530 
VNVNIPTSGA EIGGAFGGEK HTGGGRESGS DAWKQYMRRS TCTINYSTSL PLAQGIKFQ

« Hide

Isoform 2 [UniParc].

Checksum: 37952CEC7C5F3A85
Show »

FASTA51155,645

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Liver.
[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] (ISOFORM 1).
Tissue: Salivary gland.
[3]"Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress."
Brocker C., Lassen N., Estey T., Pappa A., Cantore M., Orlova V.V., Chavakis T., Kavanagh K.L., Oppermann U., Vasiliou V.
J. Biol. Chem. 285:18452-18463(2010) [PubMed: 20207735] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK004991 mRNA. Translation: BAB23726.1.
AK145873 mRNA. Translation: BAE26715.1.
AK160117 mRNA. Translation: BAE35641.1.
AK169195 mRNA. Translation: BAE40971.1.
BC012407 mRNA. Translation: AAH12407.1. Different initiation.
IPIIPI00230084.
IPI00890092.
RefSeqNP_001120810.1. NM_001127338.1.
NP_613066.2. NM_138600.4.
UniGeneMm.30250.

3D structure databases

ProteinModelPortalQ9DBF1.
SMRQ9DBF1. Positions 30-527.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9DBF1.

PTM databases

PhosphoSiteQ9DBF1.

2D gel databases

REPRODUCTION-2DPAGEQ9DBF1.

Proteomic databases

PRIDEQ9DBF1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000066208; ENSMUSP00000065089; ENSMUSG00000053644.
ENSMUST00000116635; ENSMUSP00000112334; ENSMUSG00000053644.
ENSMUST00000174518; ENSMUSP00000133372; ENSMUSG00000053644.
GeneID110695.
KEGGmmu:110695.
NMPDRfig|10090.3.peg.4006.
UCSCuc008eyn.2. mouse.
uc008eyo.2. mouse.

Organism-specific databases

CTD501.
MGIMGI:108186. Aldh7a1.

Phylogenomic databases

GeneTreeENSGT00560000077032.
HOVERGENHBG050485.
InParanoidQ9DBF1.
OMACDYATGL.
OrthoDBEOG4W3SMQ.

Gene expression databases

ArrayExpressQ9DBF1.
BgeeQ9DBF1.
CleanExMM_ALDH7A1.
GenevestigatorQ9DBF1.
GermOnlineENSMUSG00000053644. Mus musculus.

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.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
KOK14085.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. False negative.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio364487.
SOURCESearch...

Entry information

Entry nameAL7A1_MOUSE
AccessionPrimary (citable) accession number: Q9DBF1
Secondary accession number(s): Q3TFC7, Q3TVH7, Q3UKT6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: April 20, 2010
Last modified: January 25, 2012
This is version 94 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents