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Protein

Alpha-aminoadipic semialdehyde dehydrogenase

Gene

Aldh7a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

(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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei195 – 1951Transition state stabilizerBy similarity
Active sitei296 – 2961Proton acceptorPROSITE-ProRule annotation
Active sitei330 – 3301NucleophilePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi274 – 2796NADBy similarity

GO - Molecular functioni

  1. aldehyde dehydrogenase (NAD) activity Source: GO_Central
  2. betaine-aldehyde dehydrogenase activity Source: UniProtKB-EC
  3. L-aminoadipate-semialdehyde dehydrogenase activity Source: MGI

GO - Biological processi

  1. glycine betaine biosynthetic process from choline Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_239844. Lysine catabolism.
UniPathwayiUPA00529; UER00386.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-aminoadipic semialdehyde dehydrogenase (EC:1.2.1.31)
Short name:
Alpha-AASA dehydrogenase
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 namesi
Name:Aldh7a1
Synonyms:Ald7a1
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:108186. Aldh7a1.

Subcellular locationi

Mitochondrion 1 Publication. Nucleus 1 Publication. Cytoplasmcytosol 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: MGI
  4. mitochondrion Source: MGI
  5. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626MitochondrionSequence AnalysisAdd
BLAST
Chaini27 – 539513Alpha-aminoadipic semialdehyde dehydrogenasePRO_0000056491Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei86 – 861N6-acetyllysine; alternate1 Publication
Modified residuei86 – 861N6-succinyllysine; alternate1 Publication
Modified residuei94 – 941N6-acetyllysine; alternate1 Publication
Modified residuei94 – 941N6-succinyllysine; alternate1 Publication
Modified residuei97 – 971N6-acetyllysine; alternate1 Publication
Modified residuei97 – 971N6-succinyllysine; alternate1 Publication
Modified residuei462 – 4621N6-acetyllysine1 Publication
Modified residuei500 – 5001N6-acetyllysine1 Publication
Modified residuei537 – 5371N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9DBF1.
PaxDbiQ9DBF1.
PRIDEiQ9DBF1.

2D gel databases

REPRODUCTION-2DPAGEQ9DBF1.

PTM databases

PhosphoSiteiQ9DBF1.

Expressioni

Tissue specificityi

Present in liver, kidney, brain and pancreas, and at lower levels in jejunum, duodenum, stomach and testes (at protein level).1 Publication

Gene expression databases

BgeeiQ9DBF1.
CleanExiMM_ALDH7A1.
ExpressionAtlasiQ9DBF1. baseline and differential.
GenevestigatoriQ9DBF1.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ9DBF1. 4 interactions.
MINTiMINT-1859388.
STRINGi10090.ENSMUSP00000112334.

Structurei

3D structure databases

ProteinModelPortaliQ9DBF1.
SMRiQ9DBF1. Positions 30-527.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00780000121975.
HOGENOMiHOG000271511.
HOVERGENiHBG050485.
InParanoidiQ9DBF1.
KOiK14085.
OMAiNAIIVFE.
OrthoDBiEOG78D7JV.
PhylomeDBiQ9DBF1.
TreeFamiTF300388.

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.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9DBF1-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MWRVPRRLCV QSVKTSKLSG PWSRPAAHMS TLLIHHPQYA WLQDLGLRED
60 70 80 90 100
NEGVYNGSWG GRGEVITTYC PANNEPIARV RQASLKDYEE TIGKAKKAWN
110 120 130 140 150
IWADIPAPKR GEIVRKIGDA FREKIQLLGR LVSLEMGKIL VEGIGEVQEY
160 170 180 190 200
VDVCDYAAGL SRMIGGPTLP SERPGHALIE MWNPLGLVGI ITAFNFPVAV
210 220 230 240 250
FGWNNAIALI TGNVCLWKGA PTTSLVSVAV TKIIAQVLED NLLPGAICSL
260 270 280 290 300
VCGGADIGTT MARDERVNLL SFTGSTQVGK EVALMVQERF GKSLLELGGN
310 320 330 340 350
NAIIAFEDAD LSLVVPSVLF AAVGTAGQRC TTVRRLFLHE SIHNEVVDRL
360 370 380 390 400
RSAYSQIRVG NPWDPNILYG PLHTKQAVSM FVRAVEEAKK QGGTVVYGGK
410 420 430 440 450
VMDHPGNYVE PTIVTGLAHD APIVHQETFA PILYVFKFQD EEEVFEWNNE
460 470 480 490 500
VKQGLSSSIF TKDLGRIFRW LGPKGSDCGI VNVNIPTSGA EIGGAFGGEK
510 520 530
HTGGGRESGS DAWKQYMRRS TCTINYSTSL PLAQGIKFQ
Length:539
Mass (Da):58,861
Last modified:April 20, 2010 - v4
Checksum:i7591EE5652F2577E
GO
Isoform 2 (identifier: Q9DBF1-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:511
Mass (Da):55,645
Checksum:i37952CEC7C5F3A85
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641I → M in BAE26715. (PubMed:16141072)Curated
Sequence conflicti467 – 4671I → V in BAE35641. (PubMed:16141072)Curated
Sequence conflicti491 – 4911E → G in BAE35641. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform 2. 1 PublicationVSP_038989Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29258.2. [Q9DBF1-1]
CCDS50291.1. [Q9DBF1-2]
RefSeqiNP_001120810.1. NM_001127338.1. [Q9DBF1-2]
NP_613066.2. NM_138600.4. [Q9DBF1-1]
UniGeneiMm.30250.

Genome annotation databases

EnsembliENSMUST00000066208; ENSMUSP00000065089; ENSMUSG00000053644. [Q9DBF1-1]
ENSMUST00000174518; ENSMUSP00000133372; ENSMUSG00000053644. [Q9DBF1-2]
GeneIDi110695.
KEGGimmu:110695.
UCSCiuc008eyn.2. mouse. [Q9DBF1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29258.2. [Q9DBF1-1]
CCDS50291.1. [Q9DBF1-2]
RefSeqiNP_001120810.1. NM_001127338.1. [Q9DBF1-2]
NP_613066.2. NM_138600.4. [Q9DBF1-1]
UniGeneiMm.30250.

3D structure databases

ProteinModelPortaliQ9DBF1.
SMRiQ9DBF1. Positions 30-527.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DBF1. 4 interactions.
MINTiMINT-1859388.
STRINGi10090.ENSMUSP00000112334.

PTM databases

PhosphoSiteiQ9DBF1.

2D gel databases

REPRODUCTION-2DPAGEQ9DBF1.

Proteomic databases

MaxQBiQ9DBF1.
PaxDbiQ9DBF1.
PRIDEiQ9DBF1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066208; ENSMUSP00000065089; ENSMUSG00000053644. [Q9DBF1-1]
ENSMUST00000174518; ENSMUSP00000133372; ENSMUSG00000053644. [Q9DBF1-2]
GeneIDi110695.
KEGGimmu:110695.
UCSCiuc008eyn.2. mouse. [Q9DBF1-1]

Organism-specific databases

CTDi501.
MGIiMGI:108186. Aldh7a1.

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00780000121975.
HOGENOMiHOG000271511.
HOVERGENiHBG050485.
InParanoidiQ9DBF1.
KOiK14085.
OMAiNAIIVFE.
OrthoDBiEOG78D7JV.
PhylomeDBiQ9DBF1.
TreeFamiTF300388.

Enzyme and pathway databases

UniPathwayiUPA00529; UER00386.
ReactomeiREACT_239844. Lysine catabolism.

Miscellaneous databases

NextBioi364487.
PROiQ9DBF1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBF1.
CleanExiMM_ALDH7A1.
ExpressionAtlasiQ9DBF1. baseline and differential.
GenevestigatoriQ9DBF1.

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.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-86; LYS-94; LYS-97 AND LYS-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-86; LYS-94; LYS-97; LYS-462 AND LYS-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAL7A1_MOUSE
AccessioniPrimary (citable) accession number: Q9DBF1
Secondary accession number(s): Q3TFC7, Q3TVH7, Q3UKT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: April 20, 2010
Last modified: February 4, 2015
This is version 121 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.