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UniProtKB/Swiss-Prot entry Q62148


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

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Entry information
Entry name AL1A2_MOUSE
Primary accession number Q62148
Secondary accession number Q6DI79
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on March 7, 2006 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 75)
Name and origin of the protein
Protein name Retinal dehydrogenase 2
Synonyms RALDH 2
RalDH2
EC 1.2.1.36
Aldehyde dehydrogenase family 1 member A2
Retinaldehyde-specific dehydrogenase type 2
RALDH(II)
Gene name
Name: Aldh1a2
Synonyms: Aldh1a7, Raldh2
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 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/He;
PubMed=8797830 [NCBI, ExPASy, EBI, Israel, Japan]
Zhao D., McCaffery P., Ivins K.J., Neve R.L., Hogan P., Chin W.W., Draeger U.C.;
"Molecular identification of a major retinoic-acid-synthesizing enzyme, a retinaldehyde-specific dehydrogenase.";
Eur. J. Biochem. 240:15-22(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Kidney;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-518.
STRAIN=C57BL/6J;
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-119 AND THR-122, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr0604155; PubMed=17203969 [NCBI, ExPASy, EBI, Israel, Japan]
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry.";
J. Proteome Res. 6:250-262(2007).
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
X99273; CAA67666.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC075704; AAH75704.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK078553; BAC37332.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S74224; S74224.
RefSeq NP_033048.1; -.
UniGene Mm.42016
3D structure databases
HSSP Q63639; 1BI9. [HSSP ENTRY / PDB]
ModBase Q62148.
PTM databases
PhosphoSite Q62148; -.
2D gel databases
REPRODUCTION-2DPAGE Q62148; -.
Organism-specific databases
MGI MGI:107928; Aldh1a2.
Gene expression databases
ArrayExpress Q62148; -.
CleanEx MM_ALDH1A2; -.
MM_ALDH1A7; -.
GermOnline ENSMUSG00000013584; Mus musculus.
Ontologies
GO
GO:0004028; Molecular function: 3-chloroallyl aldehyde dehydrogenase activity (inferred from direct assay from MGI).
GO:0001758; Molecular function: retinal dehydrogenase activity (inferred from direct assay from MGI).
GO:0009952; Biological process: anterior/posterior pattern formation (inferred from mutant phenotype from MGI).
GO:0043010; Biological process: camera-type eye development (inferred from mutant phenotype from MGI).
GO:0009855; Biological process: determination of bilateral symmetry (inferred from mutant phenotype from MGI).
GO:0035115; Biological process: embryonic forelimb morphogenesis (inferred from mutant phenotype from MGI).
GO:0030900; Biological process: forebrain development (inferred from mutant phenotype from MGI).
GO:0003007; Biological process: heart morphogenesis (inferred from mutant phenotype from MGI).
GO:0030902; Biological process: hindbrain development (inferred from mutant phenotype from MGI).
GO:0016331; Biological process: morphogenesis of embryonic epithelium (inferred from mutant phenotype from MGI).
GO:0014032; Biological process: neural crest cell development (inferred from mutant phenotype from MGI).
GO:0030182; Biological process: neuron differentiation (inferred from mutant phenotype from MGI).
GO:0031016; Biological process: pancreas development (inferred from mutant phenotype from MGI).
GO:0008284; Biological process: positive regulation of cell proliferation (inferred from mutant phenotype from MGI).
GO:0009954; Biological process: proximal/distal pattern formation (inferred from mutant phenotype from MGI).
GO:0042573; Biological process: retinoic acid metabolic process (inferred from direct assay from MGI).
GO:0048384; Biological process: retinoic acid receptor signaling pathway (inferred from mutant phenotype from MGI).
QuickGo view.
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 Q62148.
Genome annotation databases
Ensembl ENSMUSG00000013584; Mus musculus. [Contig view]
GeneID 19378; -.
KEGG mmu:19378; -.
NMPDR fig|10090.3.peg.20462; -.
Phylogenomic databases
HOGENOM Q62148; -.
HOVERGEN Q62148; -.
Other
SOURCE Aldh1a2; Mus musculus.
ProtoNet Q62148.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; NAD; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   518  518     Retinal dehydrogenase 2. PRO_0000056423
NP_BIND   263   268  6     NAD (By similarity). 
ACT_SITE   286   286        Proton acceptor (By similarity). 
ACT_SITE   320   320        Nucleophile (By similarity). 
SITE   187   187  1     Transition state stabilizer (By similarity). 
MOD_RES   119   119        Phosphothreonine. 
MOD_RES   122   122        Phosphothreonine. 
Sequence information
Length: 518 AA [This is the length of the unprocessed precursor] Molecular weight: 56626 Da [This is the MW of the unprocessed precursor] CRC64: 2BC35B5C90046ABC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTSSEIAMPG EVKADPAALM ASLQLLPSPT PNLEIKYTKI FINNEWQNSE SGRVFPVCNP 

        70         80         90        100        110        120 
ATGEQVCEVQ EADKVDIDKA VQAARLAFSL GSVWRRMDAS ERGRLLDKLA DLVERDRATL 

       130        140        150        160        170        180 
ATMESLNGGK PFLQAFYIDL QGVIKTLRYY AGWADKIHGM TIPVDGDYFT FTRHEPIGVC 

       190        200        210        220        230        240 
GQIIPWNFPL LMFTWKIAPA LCCGNTVVIK PAEQTPLSAL YMGALIKEAG FPPGVVNILP 

       250        260        270        280        290        300 
GYGPTAGAAI ASHIGIDKIA FTGSTEVGKL IQEAAGRSNL KRVTLELGGK SPNIIFADAD 

       310        320        330        340        350        360 
LDYAVEQAHQ GVFFNQGQCC TAGSRIFVEE SIYEEFVKRS VERAKRRIVG SPFDPTTEQG 

       370        380        390        400        410        420 
PQIDKKQYNK VLELIQSGVA EGAKLECGGK GLGRKGFFIE PTVFSNVTDD MRIAKEEIFG 

       430        440        450        460        470        480 
PVQEILRFKT MDEVIERANN SDFGLVAAVF TNDINKALMV SSAMQAGTVW INCYNALNAQ 

       490        500        510 
SPFGGFKMSG NGREMGEFGL REYSEVKTVT VKIPQKNS 

Q62148 in FASTA format

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