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Protein

Retinal dehydrogenase 1

Gene

ALDH1A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Can convert/oxidize retinaldehyde to retinoic acid. Binds free retinal and cellular retinol-binding protein-bound retinal (By similarity). May have a broader specificity and oxidize other aldehydes in vivo (PubMed:19296407, PubMed:26373694, PubMed:25450233).By similarity3 Publications

Catalytic activityi

Retinal + NAD+ + H2O = retinoate + NADH.By similarity

Activity regulationi

Inhibited by citral, disulfiram, and cyanamide. Activated by diethylstilbestrol (PubMed:19296407). Inhibited by duocarmycin analogs (PubMed:26373694).2 Publications

Kineticsi

  1. KM=59.4 µM for NAD (at pH 8.0)1 Publication
  2. KM=238.2 µM for acetaldehyde (at pH 8.0)1 Publication
  3. KM=142.2 µM for benzaldehyde (at pH 8.0)1 Publication
  4. KM=4.8 µM for 4-hydroxynonenal (at pH 8.0)1 Publication
  5. KM=121.4 µM for propionaldehyde (at pH 8.0)1 Publication
  6. KM=15 µM for propionaldehyde (at pH 7.5)1 Publication
  7. KM=3.5 µM for malonaldehyde (at pH 8.0)1 Publication
  8. KM=177.1 µM for trans-2-heptenal (at pH 8.0)1 Publication
  1. Vmax=149.7 nmol/min/mg enzyme with NAD (at pH 8.0)1 Publication
  2. Vmax=631.4 nmol/min/mg enzyme with acetaldehyde (at pH 8.0)1 Publication
  3. Vmax=750.3 nmol/min/mg enzyme with benzaldehyde (at pH 8.0)1 Publication
  4. Vmax=135 nmol/min/mg enzyme with 4-hydroxynonenal (at pH 8.0)1 Publication
  5. Vmax=445.3 nmol/min/mg enzyme with propionaldehyde (at pH 8.0)1 Publication
  6. Vmax=381.6 nmol/min/mg enzyme with malonaldehyde (at pH 8.0)1 Publication
  7. Vmax=155.8 nmol/min/mg enzyme with trans-2-heptenal (at pH 8.0)1 Publication

Pathwayi: retinol metabolism

This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway retinol metabolism and in Cofactor metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei170Transition state stabilizerBy similarity1
Active sitei269Proton acceptorPROSITE-ProRule annotation1 Publication1
Active sitei303NucleophilePROSITE-ProRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi167 – 170NADCombined sources4
Nucleotide bindingi193 – 196NADCombined sources4
Nucleotide bindingi226 – 227NADCombined sources2
Nucleotide bindingi246 – 247NADCombined sources2
Nucleotide bindingi269 – 271NADCombined sources3
Nucleotide bindingi349 – 353NADCombined sources5
Nucleotide bindingi400 – 402NADCombined sources3

GO - Molecular functioni

  • aldehyde dehydrogenase (NAD) activity Source: UniProtKB
  • androgen binding Source: ProtInc
  • benzaldehyde dehydrogenase (NAD+) activity Source: GO_Central
  • GTPase activator activity Source: UniProtKB
  • NAD binding Source: CAFA
  • retinal dehydrogenase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandNAD, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS09183-MONOMER
ReactomeiR-HSA-5365859 RA biosynthesis pathway
R-HSA-70350 Fructose catabolism
R-HSA-71384 Ethanol oxidation
SABIO-RKiP00352
SIGNORiP00352
UniPathwayi
UPA00912

Names & Taxonomyi

Protein namesi
Recommended name:
Retinal dehydrogenase 1Curated (EC:1.2.1.-3 Publications, EC:1.2.1.36By similarity)
Short name:
RALDH 1Curated
Short name:
RalDH1Curated
Alternative name(s):
ALDH-E1
ALHDII
Aldehyde dehydrogenase family 1 member A1Imported
Aldehyde dehydrogenase, cytosolic1 Publication
Gene namesi
Name:ALDH1A1Imported
Synonyms:ALDC, ALDH1Imported, PUMB1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

EuPathDBiHostDB:ENSG00000165092.12
HGNCiHGNC:402 ALDH1A1
MIMi100640 gene
neXtProtiNX_P00352

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi302C → A or S: Does not prevent inhibition by duocarmycin analogs. 1 Publication1
Mutagenesisi458G → N: No significant effect on aldehyde dehydrogenase activity. Prevents the inhibition by ALDH1A1-specific inhibitors. 1 Publication1

Organism-specific databases

DisGeNETi216
OpenTargetsiENSG00000165092
PharmGKBiPA24692

Chemistry databases

ChEMBLiCHEMBL3577
DrugBankiDB09462 Glycerin
DB00157 NADH
DB00755 Tretinoin
DB00162 Vitamin A

Polymorphism and mutation databases

BioMutaiALDH1A1
DMDMi118495

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000564152 – 501Retinal dehydrogenase 1Add BLAST500

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei91N6-acetyllysineCombined sources1
Modified residuei128N6-acetyllysineCombined sources1
Modified residuei252N6-acetyllysineCombined sources1
Modified residuei337PhosphothreonineCombined sources1
Modified residuei353N6-acetyllysineCombined sources1
Modified residuei367N6-acetyllysineCombined sources1
Modified residuei410N6-acetyllysineCombined sources1
Modified residuei413PhosphoserineCombined sources1
Modified residuei419N6-acetyllysineCombined sources1
Modified residuei435N6-acetyllysineCombined sources1
Modified residuei495N6-acetyllysineCombined sources1

Post-translational modificationi

The N-terminus is blocked most probably by acetylation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP00352
PaxDbiP00352
PeptideAtlasiP00352
PRIDEiP00352
ProteomicsDBi51235

2D gel databases

DOSAC-COBS-2DPAGEiP00352
REPRODUCTION-2DPAGEiIPI00218914
P00352
SWISS-2DPAGEiP00352
UCD-2DPAGEiP00352

PTM databases

iPTMnetiP00352
PhosphoSitePlusiP00352
SwissPalmiP00352

Expressioni

Gene expression databases

BgeeiENSG00000165092 Expressed in 224 organ(s), highest expression level in nasal cavity epithelium
CleanExiHS_ALDH1A1
ExpressionAtlasiP00352 baseline and differential
GenevisibleiP00352 HS

Organism-specific databases

HPAiCAB020690
HPA002123

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi106718, 6 interactors
IntActiP00352, 7 interactors
STRINGi9606.ENSP00000297785

Chemistry databases

BindingDBiP00352

Structurei

Secondary structure

1501
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP00352
SMRiP00352
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiKOG2450 Eukaryota
COG1012 LUCA
GeneTreeiENSGT00760000118999
HOGENOMiHOG000271505
HOVERGENiHBG000097
InParanoidiP00352
KOiK07249
OMAiKTIWIAL
OrthoDBiEOG091G05E8
PhylomeDBiP00352
TreeFamiTF300455

Family and domain databases

Gene3Di3.40.309.10, 1 hit
3.40.605.10, 1 hit
InterProiView protein in InterPro
IPR016161 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
PfamiView protein in Pfam
PF00171 Aldedh, 1 hit
SUPFAMiSSF53720 SSF53720, 1 hit
PROSITEiView protein in PROSITE
PS00070 ALDEHYDE_DEHYDR_CYS, 1 hit
PS00687 ALDEHYDE_DEHYDR_GLU, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P00352-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC
60 70 80 90 100
QVEEGDKEDV DKAVKAARQA FQIGSPWRTM DASERGRLLY KLADLIERDR
110 120 130 140 150
LLLATMESMN GGKLYSNAYL NDLAGCIKTL RYCAGWADKI QGRTIPIDGN
160 170 180 190 200
FFTYTRHEPI GVCGQIIPWN FPLVMLIWKI GPALSCGNTV VVKPAEQTPL
210 220 230 240 250
TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID KVAFTGSTEV
260 270 280 290 300
GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG
310 320 330 340 350
QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ
360 370 380 390 400
YDKILDLIES GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE
410 420 430 440 450
IFGPVQQIMK FKSLDDVIKR ANNTFYGLSA GVFTKDIDKA ITISSALQAG
460 470 480 490 500
TVWVNCYGVV SAQCPFGGFK MSGNGRELGE YGFHEYTEVK TVTVKISQKN

S
Length:501
Mass (Da):54,862
Last modified:January 23, 2007 - v2
Checksum:iB26464DC7168348E
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5SYQ9Q5SYQ9_HUMAN
Retinal dehydrogenase 1
ALDH1A1
230Annotation score:
Q5SYQ7Q5SYQ7_HUMAN
Retinal dehydrogenase 1
ALDH1A1
203Annotation score:
Q5SYQ8Q5SYQ8_HUMAN
Retinal dehydrogenase 1
ALDH1A1
238Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti162V → I in AAA35518 (PubMed:4015823).Curated1
Sequence conflicti162V → I in AAA51695 (PubMed:2987944).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_048901121N → S1 PublicationCorresponds to variant dbSNP:rs1049981Ensembl.1
Natural variantiVAR_048902125G → R. Corresponds to variant dbSNP:rs11554423Ensembl.1
Natural variantiVAR_017778177I → F1 PublicationCorresponds to variant dbSNP:rs8187929Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31994
, M31982, M31983, M31984, M31985, M31986, M31987, M31988, M31989, M31990, M31991, M31992 Genomic DNA Translation: AAA51692.1
AF003341 mRNA Translation: AAC51652.1
AY390731 mRNA Translation: AAR92229.1
BT006921 mRNA Translation: AAP35567.1
AY338497 Genomic DNA Translation: AAP88039.1
AL591031 Genomic DNA No translation available.
CH471089 Genomic DNA Translation: EAW62543.1
BC001505 mRNA Translation: AAH01505.1
S61235 Genomic DNA Translation: AAD13925.1
M26761 mRNA Translation: AAA35518.1
K03000 mRNA Translation: AAA51695.1
CCDSiCCDS6644.1
PIRiA33371 DEHUE1
RefSeqiNP_000680.2, NM_000689.4
UniGeneiHs.76392

Genome annotation databases

EnsembliENST00000297785; ENSP00000297785; ENSG00000165092
GeneIDi216
KEGGihsa:216

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31994
, M31982, M31983, M31984, M31985, M31986, M31987, M31988, M31989, M31990, M31991, M31992 Genomic DNA Translation: AAA51692.1
AF003341 mRNA Translation: AAC51652.1
AY390731 mRNA Translation: AAR92229.1
BT006921 mRNA Translation: AAP35567.1
AY338497 Genomic DNA Translation: AAP88039.1
AL591031 Genomic DNA No translation available.
CH471089 Genomic DNA Translation: EAW62543.1
BC001505 mRNA Translation: AAH01505.1
S61235 Genomic DNA Translation: AAD13925.1
M26761 mRNA Translation: AAA35518.1
K03000 mRNA Translation: AAA51695.1
CCDSiCCDS6644.1
PIRiA33371 DEHUE1
RefSeqiNP_000680.2, NM_000689.4
UniGeneiHs.76392

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WB9X-ray2.07A1-501[»]
4WJ9X-ray1.74A1-501[»]
4WP7X-ray1.80A1-501[»]
4WPNX-ray1.95A1-501[»]
4X4LX-ray1.85A1-501[»]
5AC2X-ray1.85A1-501[»]
5L2MX-ray1.70A1-501[»]
5L2NX-ray1.70A1-501[»]
5L2OX-ray2.05A/B/C/D/E/F/G/H1-501[»]
5TEIX-ray2.10A1-501[»]
ProteinModelPortaliP00352
SMRiP00352
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106718, 6 interactors
IntActiP00352, 7 interactors
STRINGi9606.ENSP00000297785

Chemistry databases

BindingDBiP00352
ChEMBLiCHEMBL3577
DrugBankiDB09462 Glycerin
DB00157 NADH
DB00755 Tretinoin
DB00162 Vitamin A

PTM databases

iPTMnetiP00352
PhosphoSitePlusiP00352
SwissPalmiP00352

Polymorphism and mutation databases

BioMutaiALDH1A1
DMDMi118495

2D gel databases

DOSAC-COBS-2DPAGEiP00352
REPRODUCTION-2DPAGEiIPI00218914
P00352
SWISS-2DPAGEiP00352
UCD-2DPAGEiP00352

Proteomic databases

EPDiP00352
PaxDbiP00352
PeptideAtlasiP00352
PRIDEiP00352
ProteomicsDBi51235

Protocols and materials databases

DNASUi216
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000297785; ENSP00000297785; ENSG00000165092
GeneIDi216
KEGGihsa:216

Organism-specific databases

CTDi216
DisGeNETi216
EuPathDBiHostDB:ENSG00000165092.12
GeneCardsiALDH1A1
HGNCiHGNC:402 ALDH1A1
HPAiCAB020690
HPA002123
MIMi100640 gene
neXtProtiNX_P00352
OpenTargetsiENSG00000165092
PharmGKBiPA24692
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2450 Eukaryota
COG1012 LUCA
GeneTreeiENSGT00760000118999
HOGENOMiHOG000271505
HOVERGENiHBG000097
InParanoidiP00352
KOiK07249
OMAiKTIWIAL
OrthoDBiEOG091G05E8
PhylomeDBiP00352
TreeFamiTF300455

Enzyme and pathway databases

UniPathwayi
UPA00912

BioCyciMetaCyc:HS09183-MONOMER
ReactomeiR-HSA-5365859 RA biosynthesis pathway
R-HSA-70350 Fructose catabolism
R-HSA-71384 Ethanol oxidation
SABIO-RKiP00352
SIGNORiP00352

Miscellaneous databases

ChiTaRSiALDH1A1 human
GeneWikiiALDH1A1
GenomeRNAii216
PROiPR:P00352
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000165092 Expressed in 224 organ(s), highest expression level in nasal cavity epithelium
CleanExiHS_ALDH1A1
ExpressionAtlasiP00352 baseline and differential
GenevisibleiP00352 HS

Family and domain databases

Gene3Di3.40.309.10, 1 hit
3.40.605.10, 1 hit
InterProiView protein in InterPro
IPR016161 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
PfamiView protein in Pfam
PF00171 Aldedh, 1 hit
SUPFAMiSSF53720 SSF53720, 1 hit
PROSITEiView protein in PROSITE
PS00070 ALDEHYDE_DEHYDR_CYS, 1 hit
PS00687 ALDEHYDE_DEHYDR_GLU, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiAL1A1_HUMAN
AccessioniPrimary (citable) accession number: P00352
Secondary accession number(s): O00768, Q5SYR1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 193 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
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