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Protein

Retinal dehydrogenase 1

Gene

ALDH1A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Enzyme 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: CACAO
  • androgen binding Source: ProtInc
  • benzaldehyde dehydrogenase (NAD+) activity Source: GO_Central
  • GTPase activator activity Source: UniProtKB
  • retinal dehydrogenase activity Source: Reactome

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS09183-MONOMER.
ZFISH:HS09183-MONOMER.
ReactomeiR-HSA-5365859. RA biosynthesis pathway.
R-HSA-70350. Fructose catabolism.
R-HSA-71384. Ethanol oxidation.
SABIO-RKP00352.
UniPathwayiUPA00912.

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

HGNCiHGNC:402. ALDH1A1.

Subcellular locationi

  • Cytoplasmcytosol By similarity

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

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.
DrugBankiDB00755. 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.

2D gel databases

DOSAC-COBS-2DPAGEP00352.
REPRODUCTION-2DPAGEIPI00218914.
P00352.
SWISS-2DPAGEP00352.
UCD-2DPAGEP00352.

PTM databases

iPTMnetiP00352.
PhosphoSitePlusiP00352.
SwissPalmiP00352.

Expressioni

Gene expression databases

BgeeiENSG00000165092.
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. 6 interactors.
MINTiMINT-4999613.
STRINGi9606.ENSP00000297785.

Chemistry databases

BindingDBiP00352.

Structurei

Secondary structure

1501
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 25Combined sources4
Beta strandi28 – 30Combined sources3
Beta strandi37 – 41Combined sources5
Turni43 – 45Combined sources3
Beta strandi48 – 53Combined sources6
Helixi57 – 71Combined sources15
Helixi76 – 79Combined sources4
Helixi82 – 98Combined sources17
Helixi100 – 111Combined sources12
Helixi115 – 120Combined sources6
Helixi122 – 136Combined sources15
Helixi137 – 139Combined sources3
Beta strandi148 – 159Combined sources12
Beta strandi162 – 166Combined sources5
Beta strandi169 – 171Combined sources3
Helixi172 – 185Combined sources14
Beta strandi189 – 193Combined sources5
Helixi200 – 212Combined sources13
Beta strandi218 – 221Combined sources4
Turni226 – 228Combined sources3
Helixi229 – 235Combined sources7
Beta strandi241 – 246Combined sources6
Helixi248 – 260Combined sources13
Beta strandi265 – 269Combined sources5
Beta strandi275 – 278Combined sources4
Helixi284 – 296Combined sources13
Helixi297 – 300Combined sources4
Beta strandi308 – 312Combined sources5
Helixi313 – 327Combined sources15
Helixi348 – 363Combined sources16
Beta strandi367 – 370Combined sources4
Beta strandi373 – 379Combined sources7
Beta strandi385 – 389Combined sources5
Helixi395 – 398Combined sources4
Beta strandi403 – 412Combined sources10
Helixi414 – 422Combined sources9
Beta strandi428 – 433Combined sources6
Helixi437 – 446Combined sources10
Beta strandi450 – 455Combined sources6
Helixi470 – 472Combined sources3
Beta strandi473 – 475Combined sources3
Helixi479 – 483Combined sources5
Helixi484 – 486Combined sources3
Beta strandi487 – 495Combined sources9

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[»]
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.
OMAiEWHSSVS.
OrthoDBiEOG091G05E8.
PhylomeDBiP00352.
TreeFamiTF300455.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. 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]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

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

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 → S.1 PublicationCorresponds to variant rs1049981dbSNPEnsembl.1
Natural variantiVAR_048902125G → R.Corresponds to variant rs11554423dbSNPEnsembl.1
Natural variantiVAR_017778177I → F.1 PublicationCorresponds to variant rs8187929dbSNPEnsembl.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. Translation: CAI12257.1.
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

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. Translation: CAI12257.1.
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[»]
ProteinModelPortaliP00352.
SMRiP00352.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106718. 6 interactors.
IntActiP00352. 6 interactors.
MINTiMINT-4999613.
STRINGi9606.ENSP00000297785.

Chemistry databases

BindingDBiP00352.
ChEMBLiCHEMBL3577.
DrugBankiDB00755. Tretinoin.
DB00162. Vitamin A.

PTM databases

iPTMnetiP00352.
PhosphoSitePlusiP00352.
SwissPalmiP00352.

Polymorphism and mutation databases

BioMutaiALDH1A1.
DMDMi118495.

2D gel databases

DOSAC-COBS-2DPAGEP00352.
REPRODUCTION-2DPAGEIPI00218914.
P00352.
SWISS-2DPAGEP00352.
UCD-2DPAGEP00352.

Proteomic databases

EPDiP00352.
PaxDbiP00352.
PeptideAtlasiP00352.
PRIDEiP00352.

Protocols and materials databases

DNASUi216.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000297785; ENSP00000297785; ENSG00000165092.
GeneIDi216.
KEGGihsa:216.

Organism-specific databases

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

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00912.
BioCyciMetaCyc:HS09183-MONOMER.
ZFISH:HS09183-MONOMER.
ReactomeiR-HSA-5365859. RA biosynthesis pathway.
R-HSA-70350. Fructose catabolism.
R-HSA-71384. Ethanol oxidation.
SABIO-RKP00352.

Miscellaneous databases

ChiTaRSiALDH1A1. human.
GeneWikiiALDH1A1.
GenomeRNAii216.
PROiP00352.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000165092.
CleanExiHS_ALDH1A1.
ExpressionAtlasiP00352. baseline and differential.
GenevisibleiP00352. HS.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. 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]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAL1A1_HUMAN
AccessioniPrimary (citable) accession number: P00352
Secondary accession number(s): O00768, Q5SYR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 181 of the entry and version 2 of the sequence. [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. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.