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Reviewed, UniProtKB/Swiss-Prot Q9CZS1 (AL1B1_MOUSE)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Aldehyde dehydrogenase X, mitochondrial
    EC=1.2.1.3
Alternative name(s):
    Aldehyde dehydrogenase family 1 member B1
Gene names
Name: Aldh1b1
Synonyms: Aldhx
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

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 By similarity.

Catalytic activity

An aldehyde + NAD+ + H2O = an acid + 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.

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Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaldehyde dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1919Mitochondrion Potential
Chain20 – 519500Aldehyde dehydrogenase X, mitochondrial
PRO_0000271411

Regions

Nucleotide binding264 – 2696NAD By similarity

Sites

Active site2871Proton acceptor By similarity
Active site3211Nucleophile By similarity
Site1881Transition state stabilizer By similarity

Experimental info

Sequence conflict1461K → R in BAE30339. Ref.1
Sequence conflict2611A → T in BAE30339. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q9CZS1-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 69222D7409BFEEF3

FASTA51957,553
        10         20         30         40         50         60 
MLTARLLLPR LLCLQGRTTS YSTAAALPNP IPNPEICYNK LFINNEWHDA VSKKTFPTVN 

        70         80         90        100        110        120 
PTTGEVIGHV AEGDRADVDL AVKAAREAFR LGSPWRRMDA SERGRLLNRL ADLVERDRVY 

       130        140        150        160        170        180 
LASLETLDNG KPFQESYVLD LDEVIKVYRY FAGWADKWHG KTIPMDGEHF CFTRHEPVGV 

       190        200        210        220        230        240 
CGQIIPWNFP LVMQGWKLAP ALATGNTVVM KVAEQTPLSA LYLASLIKEA GFPPGVVNII 

       250        260        270        280        290        300 
TGYGPTAGAA IAQHMDVDKV AFTGSTEVGH LIQKAAGESN LKRVTLELGG KSPSIVLADA 

       310        320        330        340        350        360 
DMEHAVDQCH EALFFNMGQC CCAGSRTFVE ESIYREFLER TVEKAKQRKV GNPFELDTQQ 

       370        380        390        400        410        420 
GPQVDKEQFE RILGYIRLGQ KEGAKLLCGG ERLGERGFFI KPTVFGDVQD GMRIAKEEIF 

       430        440        450        460        470        480 
GPVQPLFKFK KIEEVIQRAN NTRYGLAAAV FTRDLDKAIY FTQALQAGTV WVNTYNIVTC 

       490        500        510 
HTPFGGFKES GNGRELGEDG LRAYTEVKTV TIKVPEKNS

« Hide

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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].
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Embryo and Thymus.
[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].
Strain: C57BL/6 and FVB/N.
Tissue: Brain and Colon.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AK012213 mRNA. Translation: BAB28101.1.
AK088396 mRNA. Translation: BAC40326.1.
AK150992 mRNA. Translation: BAE30016.1.
AK151349 mRNA. Translation: BAE30325.1.
AK151364 mRNA. Translation: BAE30339.1.
AK153416 mRNA. Translation: BAE31976.1.
BC020001 mRNA. Translation: AAH20001.1.
BC086768 mRNA. Translation: AAH86768.1.
IPIIPI00113073.
RefSeqNP_082546.1.
UniGeneMm.331583

3D structure databases

HSSPHSSP built from PDB template 1O04 based on UniProtKB P05091.
SMRQ9CZS1. Positions 26-519.
ModBaseSearch...

PTM databases

PhosphoSiteQ9CZS1.

Proteomic databases

PRIDEQ9CZS1.

Genome annotation databases

EnsemblENSMUSG00000035561. Mus musculus. [Contig view]
GeneID72535.
KEGGmmu:72535.
NMPDRfig|10090.3.peg.9526.

Organism-specific databases

MGIMGI:1919785. Aldh1b1.

Phylogenomic databases

HOVERGENQ9CZS1.
OMAQ9CZS1. EALFFNM.

Enzyme and pathway databases

BRENDA1.2.1.3. 244.

Gene expression databases

ArrayExpressQ9CZS1.
BgeeQ9CZS1.
CleanExMM_ALDH1B1.

Family and domain databases

InterProIPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio336439.
SOURCESearch...

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Entry information

Entry nameAL1B1_MOUSE
AccessionPrimary (citable) accession number: Q9CZS1
Secondary accession number(s): Q3UAH5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents