Reviewed, UniProtKB/Swiss-Prot Q62148 (AL1A2_MOUSE)

Names and origin

Protein names

Recommended name:
    Retinal dehydrogenase 2
      Short name=RALDH 2
      Short name=RalDH2
    EC=1.2.1.36
Alternative name(s):
    Aldehyde dehydrogenase family 1 member A2
    Retinaldehyde-specific dehydrogenase type 2
      Short name=RALDH(II)

Gene names

Name:	Aldh1a2
Synonyms:	Aldh1a7, Raldh2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	518 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently By similarity.
Catalytic activity	Retinal + NAD(+) + H(2)O = retinoate + NADH.
Pathway	Cofactor metabolism; retinol metabolism.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	anterior/posterior pattern formation Inferred from mutant phenotype. Source: MGI camera-type eye development Inferred from mutant phenotype. Source: MGI determination of bilateral symmetry Inferred from mutant phenotype. Source: MGI embryonic forelimb morphogenesis Inferred from mutant phenotype. Source: MGI forebrain development Inferred from mutant phenotype. Source: MGI heart morphogenesis Inferred from mutant phenotype. Source: MGI hindbrain development Inferred from mutant phenotype. Source: MGI morphogenesis of embryonic epithelium Inferred from mutant phenotype. Source: MGI neural crest cell development Inferred from mutant phenotype. Source: MGI neuron differentiation Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pancreas development Inferred from mutant phenotype. Source: MGI positive regulation of cell proliferation Inferred from mutant phenotype. Source: MGI proximal/distal pattern formation Inferred from mutant phenotype. Source: MGI retinoic acid metabolic process Ref.1 Inferred from direct assay. Source: MGI retinoic acid receptor signaling pathway Inferred from mutant phenotype. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-chloroallyl aldehyde dehydrogenase activity Inferred from direct assay. Source: MGI retinal dehydrogenase activity Ref.1 Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 518	518	Retinal dehydrogenase 2		PRO_0000056423
Regions
	Nucleotide binding	263 – 268	6	NAD By similarity
Sites
	Active site	286	1	Proton acceptor By similarity
	Active site	320	1	Nucleophile By similarity
	Site	187	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	119	1	Phosphothreonine
	Modified residue	122	1	Phosphothreonine

Sequences

	Sequence		Length	Mass (Da)
	Q62148-1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: 2BC35B5C90046ABC	FASTA	518	56,626
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular identification of a major retinoic-acid-synthesizing enzyme, a retinaldehyde-specific dehydrogenase." Zhao D., McCaffery P., Ivins K.J., Neve R.L., Hogan P., Chin W.W., Draeger U.C. Eur. J. Biochem. 240:15-22(1996) [PubMed: 8797830] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C3H/He.
[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/6J. Tissue: Kidney.
[3]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-518. Strain: C57BL/6J.
[4]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-119 AND THR-122, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X99273 mRNA. Translation: CAA67666.1. Different initiation. BC075704 mRNA. Translation: AAH75704.1. AK078553 mRNA. Translation: BAC37332.1. Different initiation.
PIR	S74224.
RefSeq	NP_033048.1.
UniGene	Mm.42016
3D structure databases
HSSP	HSSP built from PDB template 1BI9 based on UniProtKB Q63639.
ModBase	Search...
PTM databases
PhosphoSite	Q62148.
2-D gel databases
REPRODUCTION-2DPAGE	Q62148.
Genome annotation databases
Ensembl	ENSMUSG00000013584. Mus musculus. [Contig view]
GeneID	19378.
KEGG	mmu:19378.
NMPDR	fig|10090.3.peg.20462.
Organism-specific databases
MGI	MGI:107928. Aldh1a2.
Phylogenomic databases
HOGENOM	Q62148.
HOVERGEN	Q62148.
Gene expression databases
ArrayExpress	Q62148.
CleanEx	MM_ALDH1A2. MM_ALDH1A7.
GermOnline	ENSMUSG00000013584. Mus musculus.
Family and domain databases
InterPro	IPR016160. Ald_DHase_CS. IPR016162. Ald_DHase_N. IPR015590. Aldehyde_DHase. [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	296481.
SOURCE	Search...

Entry information

Entry name

AL1A2_MOUSE

Accession

Primary (citable) accession number: Q62148
Secondary accession number(s): Q6DI79

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 7, 2006
Last modified:	November 25, 2008
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)