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UniProtKB/Swiss-Prot entry Q9CZS1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AL1B1_MOUSE
Primary accession number Q9CZS1
Secondary accession number Q3UAH5
Integrated into Swiss-Prot on January 9, 2007
Sequence was last modified on June 1, 2001 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 57)
Name and origin of the protein
Protein name Aldehyde dehydrogenase X, mitochondrial [Precursor]
Synonyms EC 1.2.1.3
Aldehyde dehydrogenase family 1 member B1
Gene name
Name: Aldh1b1
Synonyms: Aldhx
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Bone marrow, Embryo, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6, and FVB/N;
TISSUE=Brain, and Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK012213; BAB28101.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK088396; BAC40326.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK150992; BAE30016.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK151349; BAE30325.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK151364; BAE30339.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK153416; BAE31976.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020001; AAH20001.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC086768; AAH86768.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_082546.1; -.
UniGene Mm.331583
3D structure databases
HSSP P05091; 1O04. [HSSP ENTRY / PDB]
SMR Q9CZS1; 26-519.
ModBase Q9CZS1.
PTM databases
PhosphoSite Q9CZS1; -.
Organism-specific databases
MGI MGI:1919785; Aldh1b1.
Gene expression databases
ArrayExpress Q9CZS1; -.
CleanEx MM_ALDH1B1; -.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
BLOCKS Q9CZS1.
Genome annotation databases
Ensembl ENSMUSG00000035561; Mus musculus. [Contig view]
GeneID 72535; -.
KEGG mmu:72535; -.
NMPDR fig|10090.3.peg.9526; -.
Phylogenomic databases
HOVERGEN Q9CZS1; -.
Other
SOURCE Aldh1b1; Mus musculus.
ProtoNet Q9CZS1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Mitochondrion; NAD; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    19  19     Mitochondrion (Potential). 
CHAIN   20   519  500     Aldehyde dehydrogenase X, mitochondrial. PRO_0000271411
NP_BIND   264   269  6     NAD (By similarity). 
ACT_SITE   287   287        Proton acceptor (By similarity). 
ACT_SITE   321   321        Nucleophile (By similarity). 
SITE   188   188  1     Transition state stabilizer (By similarity). 
CONFLICT   146   146        K -> R (in Ref. 1; BAE30339). 
CONFLICT   261   261        A -> T (in Ref. 1; BAE30339). 
Sequence information
Length: 519 AA [This is the length of the unprocessed precursor] Molecular weight: 57553 Da [This is the MW of the unprocessed precursor] CRC64: 69222D7409BFEEF3 [This is a checksum on the sequence]
        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 

Q9CZS1 in FASTA format

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