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O94788 (AL1A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process9-cis-retinoic acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

anterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

blood vessel development

Inferred from electronic annotation. Source: Ensembl

cardiac muscle tissue development

Inferred from electronic annotation. Source: Ensembl

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

determination of bilateral symmetry

Inferred from electronic annotation. Source: Ensembl

embryonic camera-type eye development

Inferred from electronic annotation. Source: Ensembl

embryonic digestive tract development

Inferred from electronic annotation. Source: Ensembl

embryonic forelimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

face development

Inferred from electronic annotation. Source: Ensembl

heart morphogenesis

Inferred from electronic annotation. Source: Ensembl

hindbrain development

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

midgut development

Inferred from electronic annotation. Source: Ensembl

morphogenesis of embryonic epithelium

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from direct assay PubMed 16166285. Source: UniProtKB

neural crest cell development

Inferred from electronic annotation. Source: Ensembl

neural tube development

Inferred from mutant phenotype PubMed 16237707. Source: UniProtKB

neuron differentiation

Inferred from electronic annotation. Source: Ensembl

pancreas development

Inferred from electronic annotation. Source: Ensembl

pituitary gland development

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

proximal/distal pattern formation

Inferred from electronic annotation. Source: Ensembl

regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

response to cytokine

Inferred from direct assay PubMed 18495959. Source: UniProtKB

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to vitamin A

Inferred from electronic annotation. Source: Ensembl

retinal metabolic process

Inferred from electronic annotation. Source: Ensembl

retinoic acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

retinoic acid receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

retinol metabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

ureter maturation

Inferred from electronic annotation. Source: Ensembl

vitamin A metabolic process

Non-traceable author statement PubMed 8663198. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 18495959. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_function3-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 4 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.
Isoform 3 (identifier: O94788-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MTSSKIEMPGEVKADPAALMASLHLLPSPTPNLEIKYTK → MKNQCETVWLKSPIKLKL
Note: No experimental confirmation available.
Isoform 4 (identifier: O94788-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 518518Retinal dehydrogenase 2
PRO_0000056422

Regions

Nucleotide binding263 – 2686NAD By similarity

Sites

Active site2861Proton acceptor By similarity
Active site3201Nucleophile By similarity
Site1871Transition state stabilizer By similarity

Natural variations

Alternative sequence1 – 9696Missing in isoform 4.
VSP_047259
Alternative sequence1 – 3939MTSSK…IKYTK → MKNQCETVWLKSPIKLKL in isoform 3.
VSP_044496
Alternative sequence229 – 26638Missing in isoform 2.
VSP_017363
Natural variant501E → G. Ref.3
Corresponds to variant rs34266719 [ dbSNP | Ensembl ].
VAR_025439
Natural variant1101A → V. Ref.3
Corresponds to variant rs35365164 [ dbSNP | Ensembl ].
VAR_025440
Natural variant3481V → I. Ref.1 Ref.2 Ref.3 Ref.6
Corresponds to variant rs4646626 [ dbSNP | Ensembl ].
VAR_025441
Natural variant4361E → K. Ref.3
Corresponds to variant rs34744827 [ dbSNP | Ensembl ].
VAR_025442

Experimental info

Sequence conflict2311F → L in BAG64174. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 7, 2006. Version 3.
Checksum: AAEE7A886951373F

FASTA51856,724
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 5AC931BE5ED26AA4
Show »

FASTA48053,060
Isoform 3 [UniParc].

Checksum: 27E8A8307A680BB7
Show »

FASTA49754,673
Isoform 4 [UniParc].

Checksum: 4927D07BDD3BAC5D
Show »

FASTA42246,137

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), 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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT ILE-348.
Tissue: Testis and 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]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 302-518 (ISOFORMS 1/2), VARIANT ILE-348.
Tissue: Testis.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB015226 mRNA. Translation: BAA34785.1.
AB015227 mRNA. Translation: BAA34786.1.
AB015228 mRNA. Translation: BAA34787.1.
AK128709 mRNA. Translation: BAG54714.1.
AK303057 mRNA. Translation: BAG64174.1.
DQ322171 Genomic DNA. Translation: ABC40749.1.
AC012653 Genomic DNA. No translation available.
AC018904 Genomic DNA. No translation available.
AC025431 Genomic DNA. No translation available.
AC066616 Genomic DNA. No translation available.
AC084781 Genomic DNA. No translation available.
BC030589 mRNA. Translation: AAH30589.1.
AL110299 mRNA. Translation: CAB53740.2.
CCDSCCDS10163.1. [O94788-1]
CCDS10164.1. [O94788-2]
CCDS45266.1. [O94788-4]
CCDS55968.1. [O94788-3]
PIRT14799.
RefSeqNP_001193826.1. NM_001206897.1. [O94788-3]
NP_003879.2. NM_003888.3. [O94788-1]
NP_733797.1. NM_170696.2. [O94788-2]
NP_733798.1. NM_170697.2. [O94788-4]
UniGeneHs.643455.

3D structure databases

ProteinModelPortalO94788.
SMRO94788. Positions 20-518.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114379. 2 interactions.
IntActO94788. 1 interaction.
STRING9606.ENSP00000249750.

Chemistry

DrugBankDB00157. NADH.
DB00755. Tretinoin.
DB00162. Vitamin A.

PTM databases

PhosphoSiteO94788.

Proteomic databases

MaxQBO94788.
PaxDbO94788.
PRIDEO94788.

Protocols and materials databases

DNASU8854.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000249750; ENSP00000249750; ENSG00000128918. [O94788-1]
ENST00000347587; ENSP00000309623; ENSG00000128918. [O94788-2]
ENST00000537372; ENSP00000438296; ENSG00000128918. [O94788-3]
ENST00000559517; ENSP00000453408; ENSG00000128918. [O94788-4]
GeneID8854.
KEGGhsa:8854.
UCSCuc002aew.3. human. [O94788-1]
uc002aey.3. human. [O94788-2]
uc010ugv.2. human. [O94788-3]

Organism-specific databases

CTD8854.
GeneCardsGC15M058245.
H-InvDBHIX0038341.
HGNCHGNC:15472. ALDH1A2.
HPAHPA010022.
MIM603687. gene.
neXtProtNX_O94788.
PharmGKBPA24693.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271505.
HOVERGENHBG000097.
InParanoidO94788.
KOK07249.
OMAWINCFNA.
OrthoDBEOG7PS1F7.
PhylomeDBO94788.
TreeFamTF300455.

Enzyme and pathway databases

BioCycMetaCyc:HS05232-MONOMER.
UniPathwayUPA00912.

Gene expression databases

ArrayExpressO94788.
BgeeO94788.
CleanExHS_ALDH1A2.
GenevestigatorO94788.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALDH1A2. human.
GeneWikiALDH1A2.
GenomeRNAi8854.
NextBio33241.
PROO94788.
SOURCESearch...

Entry information

Entry nameAL1A2_HUMAN
AccessionPrimary (citable) accession number: O94788
Secondary accession number(s): B3KY52 expand/collapse secondary AC list , B4DZR2, F5H2Y9, H0YM00, Q2PJS6, Q8NHQ4, Q9UBR8, Q9UFY0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM