Reviewed, UniProtKB/Swiss-Prot O94788 (AL1A2_HUMAN)

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:	RALDH2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	518 AA.
Sequence status	Complete.
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+ + H2O = 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
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	negative regulation of cell proliferation Inferred from direct assay. Source: UniProtKB neural tube development Inferred from mutant phenotype. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to cytokine stimulus Inferred from direct assay. Source: UniProtKB
Cellular component	nucleus Inferred from direct assay. Source: HPA
Molecular function	3-chloroallyl aldehyde dehydrogenase activity Inferred from sequence or structural similarity. Source: UniProtKB retinal binding Inferred from sequence or structural similarity. Source: UniProtKB retinal dehydrogenase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O94788-1)

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.

Isoform 2 (identifier: O94788-2)

The sequence of this isoform differs from the canonical sequence as follows:
     229-266: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 518	518	Retinal dehydrogenase 2		PRO_0000056422
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	122	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	229 – 266	38	Missing in isoform 2.		VSP_017363
	Natural variant	50	1	E → G: dbSNP rs34266719. Ref.3		VAR_025439
	Natural variant	110	1	A → V: dbSNP rs35365164. Ref.3		VAR_025440
	Natural variant	348	1	V → I: dbSNP rs4646626. Ref.3 Ref.1 Ref.2 Ref.5		VAR_025441
	Natural variant	436	1	E → K: dbSNP rs34744827. Ref.3		VAR_025442

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 3. Checksum: AAEE7A886951373F	FASTA	518	56,724
	10 20 30 40 50 60 MTSSKIEMPG EVKADPAALM ASLHLLPSPT PNLEIKYTKI FINNEWQNSE SGRVFPVYNP 70 80 90 100 110 120 ATGEQVCEVQ EADKADIDKA VQAARLAFSL GSVWRRMDAS ERGRLLDKLA DLVERDRAVL 130 140 150 160 170 180 ATMESLNGGK PFLQAFYVDL QGVIKTFRYY AGWADKIHGM TIPVDGDYFT FTRHEPIGVC 190 200 210 220 230 240 GQIIPWNFPL LMFAWKIAPA LCCGNTVVIK PAEQTPLSAL YMGALIKEAG FPPGVINILP 250 260 270 280 290 300 GYGPTAGAAI ASHIGIDKIA FTGSTEVGKL IQEAAGRSNL KRVTLELGGK SPNIIFADAD 310 320 330 340 350 360 LDYAVEQAHQ GVFFNQGQCC TAGSRIFVEE SIYEEFVRRS VERAKRRVVG SPFDPTTEQG 370 380 390 400 410 420 PQIDKKQYNK ILELIQSGVA EGAKLECGGK GLGRKGFFIE PTVFSNVTDD MRIAKEEIFG 430 440 450 460 470 480 PVQEILRFKT MDEVIERANN SDFGLVAAVF TNDINKALTV SSAMQAGTVW INCYNALNAQ 490 500 510 SPFGGFKMSG NGREMGEFGL REYSEVKTVT VKIPQKNS
	Isoform 2. Checksum: 5AC931BE5ED26AA4	FASTA	480	53,060
	10 20 30 40 50 60 MTSSKIEMPG EVKADPAALM ASLHLLPSPT PNLEIKYTKI FINNEWQNSE SGRVFPVYNP 70 80 90 100 110 120 ATGEQVCEVQ EADKADIDKA VQAARLAFSL GSVWRRMDAS ERGRLLDKLA DLVERDRAVL 130 140 150 160 170 180 ATMESLNGGK PFLQAFYVDL QGVIKTFRYY AGWADKIHGM TIPVDGDYFT FTRHEPIGVC 190 200 210 220 230 240 GQIIPWNFPL LMFAWKIAPA LCCGNTVVIK PAEQTPLSAL YMGALIKEVG KLIQEAAGRS 250 260 270 280 290 300 NLKRVTLELG GKSPNIIFAD ADLDYAVEQA HQGVFFNQGQ CCTAGSRIFV EESIYEEFVR 310 320 330 340 350 360 RSVERAKRRV VGSPFDPTTE QGPQIDKKQY NKILELIQSG VAEGAKLECG GKGLGRKGFF 370 380 390 400 410 420 IEPTVFSNVT DDMRIAKEEI FGPVQEILRF KTMDEVIERA NNSDFGLVAA VFTNDINKAL 430 440 450 460 470 480 TVSSAMQAGT VWINCYNALN AQSPFGGFKM SGNGREMGEF GLREYSEVKT VTVKIPQKNS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"TAL1 and LIM-only proteins synergistically induce retinaldehyde dehydrogenase 2 expression in T-cell acute lymphoblastic leukemia by acting as cofactors for GATA3." Ono Y., Fukuhara N., Yoshie O. Mol. Cell. Biol. 18:6939-6950(1998) [PubMed: 9819382] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-348.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-348. Tissue: Uterus.
[3]	NIEHS SNPs program Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-50; VAL-110; ILE-348 AND LYS-436.
[4]	"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] (ISOFORM 2). Tissue: Testis.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 302-518 (ISOFORMS 1/2), VARIANT ILE-348. Tissue: Testis.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB015226 mRNA. Translation: BAA34785.1. AB015227 mRNA. Translation: BAA34786.1. Different initiation. AB015228 mRNA. Translation: BAA34787.1. Different initiation. AK128709 mRNA. Translation: BAG54714.1. DQ322171 Genomic DNA. Translation: ABC40749.1. BC030589 mRNA. Translation: AAH30589.1. AL110299 mRNA. Translation: CAB53740.2.
IPI	IPI00169288. IPI00216805.
PIR	T14799.
RefSeq	NP_003879.2. NP_733797.1. NP_733798.1.
UniGene	Hs.643455
3D structure databases
SMR	O94788. Positions 20-518.
ModBase	Search...
Protein-protein interaction databases
IntAct	O94788. 1 interaction.
STRING	O94788.
PTM databases
PhosphoSite	O94788.
Proteomic databases
PRIDE	O94788.
Genome annotation databases
Ensembl	ENST00000249750; ENSP00000249750; ENSG00000128918; Homo sapiens. [Genome view]
GeneID	8854.
KEGG	hsa:8854.
NMPDR	fig|9606.3.peg.10760.
UCSC	uc002aew.1. human. uc002aey.1. human.
Organism-specific databases
CTD	8854.
GeneCards	GC15M056032.
H-InvDB	HIX0012280.
HGNC	HGNC:15472. ALDH1A2.
HPA	HPA010022.
MIM	603687. gene.
PharmGKB	PA24693.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12598.
HOGENOM	HBG752218.
HOVERGEN	O94788.
InParanoid	O94788.
OMA	HVGIDKI.
PhylomeDB	O94788.
Enzyme and pathway databases
BRENDA	1.2.1.36. 247.
Gene expression databases
ArrayExpress	O94788.
Bgee	O94788.
CleanEx	HS_ALDH1A2.
Genevestigator	O94788.
GermOnline	ENSG00000128918. Homo sapiens.
Family and domain databases
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. [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
DrugBank	DB00157. NADH. DB00755. Tretinoin. DB00162. Vitamin A.
NextBio	33241.
SOURCE	Search...

Entry information

Entry name

AL1A2_HUMAN

Accession

Primary (citable) accession number: O94788
Secondary accession number(s): B3KY52 , Q2PJS6, Q8NHQ4, Q9UBR8, Q9UFY0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	March 7, 2006
Last modified:	January 19, 2010
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.