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Protein

Retinal dehydrogenase 1

Gene

Aldh1a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Is capable of converting 9-cis and all-trans retinal to corresponding retinoic acid with high efficiency, 9-cis retinal being 2-fold more active than all-trans retinal.

Catalytic activityi

Retinal + NAD+ + H2O = retinoate + NADH.

Enzyme regulationi

Inhibited by chloral hydrate.

Pathway:iretinol metabolism

This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.
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)LengthDescriptionGraphical viewFeature identifierActions
Sitei170 – 1701Transition state stabilizerBy similarity
Active sitei269 – 2691Proton acceptorPROSITE-ProRule annotation
Active sitei303 – 3031NucleophilePROSITE-ProRule annotation
Binding sitei456 – 4561NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi246 – 2516NADBy similarity

GO - Molecular functioni

  • 3-chloroallyl aldehyde dehydrogenase activity Source: RGD
  • aldehyde dehydrogenase (NAD) activity Source: RGD
  • benzaldehyde dehydrogenase (NAD+) activity Source: RGD
  • identical protein binding Source: RGD
  • retinal dehydrogenase activity Source: RGD

GO - Biological processi

  • 9-cis-retinoic acid biosynthetic process Source: Ensembl
  • 9-cis-retinoic acid metabolic process Source: RGD
  • estrous cycle Source: RGD
  • kidney development Source: RGD
  • liver development Source: RGD
  • midgut development Source: RGD
  • optic cup morphogenesis involved in camera-type eye development Source: Ensembl
  • positive regulation of apoptotic process Source: Ensembl
  • protein homotetramerization Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to ethanol Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to oxidative stress Source: RGD
  • response to retinoic acid Source: RGD
  • retinoic acid biosynthetic process Source: RGD
  • retinol metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.2.1.36. 5301.
ReactomeiREACT_288510. Ethanol oxidation.
REACT_299215. RA biosynthesis pathway.
SABIO-RKP51647.
UniPathwayiUPA00912.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinal dehydrogenase 1 (EC:1.2.1.36)
Short name:
RALDH 1
Short name:
RalDH1
Alternative name(s):
ALDH-E1
ALHDII
Aldehyde dehydrogenase family 1 member A1
Aldehyde dehydrogenase, cytosolic
Gene namesi
Name:Aldh1a1
Synonyms:Aldh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2087. Aldh1a1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 501500Retinal dehydrogenase 1PRO_0000056419Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCurated
Modified residuei91 – 911N6-acetyllysineBy similarity
Modified residuei128 – 1281N6-acetyllysineBy similarity
Modified residuei252 – 2521N6-acetyllysineBy similarity
Modified residuei337 – 3371PhosphothreonineBy similarity
Modified residuei353 – 3531N6-acetyllysineBy similarity
Modified residuei367 – 3671N6-acetyllysineBy similarity
Modified residuei410 – 4101N6-acetyllysineBy similarity
Modified residuei413 – 4131PhosphoserineBy similarity
Modified residuei419 – 4191N6-acetyllysineBy similarity
Modified residuei435 – 4351N6-acetyllysineBy similarity
Modified residuei495 – 4951N6-acetyllysineBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP51647.
PRIDEiP51647.

PTM databases

PhosphoSiteiP51647.

Expressioni

Tissue specificityi

Strongly expressed in kidney, lung, testis, intestine, stomach, and trachea, but weakly in the liver.

Gene expression databases

GenevisibleiP51647. RN.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024000.

Structurei

3D structure databases

ProteinModelPortaliP51647.
SMRiP51647. Positions 9-501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiP51647.
KOiK07249.
OMAiEWHSSVS.
OrthoDBiEOG7PS1F7.
PhylomeDBiP51647.
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.

P51647-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSPAQPAVP APLANLKIQH TKIFINNEWH DSVSGKKFPV LNPATEEVIC
60 70 80 90 100
HVEEGDKADV DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLMERDR
110 120 130 140 150
LLLATIEAIN GGKVFANAYL SDLGGSIKAL KYCAGWADKI HGQTIPSDGD
160 170 180 190 200
IFTFTRREPI GVCGQIIPWN FPLLMFIWKI GPALSCGNTV VVKPAEQTPL
210 220 230 240 250
TALHMASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD KVAFTGSTQV
260 270 280 290 300
GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDIAVEF AHHGVFYHQG
310 320 330 340 350
QCCVAASRIF VEESVYDEFV RKSVERAKKY VLGNPLTQGI NQGPQIDKEQ
360 370 380 390 400
HDKILDLIES GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE
410 420 430 440 450
IFGPVQQIMK FKSIDDVIKR ANNTTYGLAA GVFTKDLDRA ITVSSALQAG
460 470 480 490 500
VVWVNCYMIL SAQCPFGGFK MSGNGRELGE HGLYEYTELK TVAMKISQKN

S
Length:501
Mass (Da):54,459
Last modified:January 23, 2007 - v3
Checksum:iA3614C21BCE7E144
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001R → C in AAA96657 (PubMed:8543180).Curated
Sequence conflicti106 – 1061I → M AA sequence (PubMed:7832787).Curated
Sequence conflicti170 – 1701N → E in AAA96657 (PubMed:8543180).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42009 mRNA. Translation: AAA96657.1.
AF001896 mRNA. Translation: AAC53304.1.
AF001898 mRNA. Translation: AAC53306.1.
AF001897 mRNA. Translation: AAC53305.1.
U79118 mRNA. Translation: AAB63423.1.
BC061526 mRNA. Translation: AAH61526.1.
PIRiJC4524.
JC5553.
RefSeqiNP_071852.2. NM_022407.3.
UniGeneiRn.6132.

Genome annotation databases

GeneIDi24188.
KEGGirno:24188.
UCSCiRGD:2087. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42009 mRNA. Translation: AAA96657.1.
AF001896 mRNA. Translation: AAC53304.1.
AF001898 mRNA. Translation: AAC53306.1.
AF001897 mRNA. Translation: AAC53305.1.
U79118 mRNA. Translation: AAB63423.1.
BC061526 mRNA. Translation: AAH61526.1.
PIRiJC4524.
JC5553.
RefSeqiNP_071852.2. NM_022407.3.
UniGeneiRn.6132.

3D structure databases

ProteinModelPortaliP51647.
SMRiP51647. Positions 9-501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024000.

Chemistry

BindingDBiP51647.
ChEMBLiCHEMBL2931.

PTM databases

PhosphoSiteiP51647.

Proteomic databases

PaxDbiP51647.
PRIDEiP51647.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24188.
KEGGirno:24188.
UCSCiRGD:2087. rat.

Organism-specific databases

CTDi216.
RGDi2087. Aldh1a1.

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiP51647.
KOiK07249.
OMAiEWHSSVS.
OrthoDBiEOG7PS1F7.
PhylomeDBiP51647.
TreeFamiTF300455.

Enzyme and pathway databases

UniPathwayiUPA00912.
BRENDAi1.2.1.36. 5301.
ReactomeiREACT_288510. Ethanol oxidation.
REACT_299215. RA biosynthesis pathway.
SABIO-RKP51647.

Miscellaneous databases

NextBioi602555.
PROiP51647.

Gene expression databases

GenevisibleiP51647. RN.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a cDNA encoding rat aldehyde dehydrogenase with high activity for retinal oxidation."
    Bhat P.V., Labrecque J., Boutin J.-M., Lacroix A., Yoshida A.
    Gene 166:303-306(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Kidney.
  2. "A preliminary report on the cloning of a constitutively expressed rat liver cytosolic ALDH cDNA by PCR."
    Kathmann E.C., Lipsky J.J.
    Adv. Exp. Med. Biol. 414:69-72(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  3. "Cloning of a cDNA encoding a constitutively expressed rat liver cytosolic aldehyde dehydrogenase."
    Kathmann E.C., Lipsky J.J.
    Biochem. Biophys. Res. Commun. 236:527-531(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  4. "Cloning of a rat cDNA encoding retinal dehydrogenase isozyme type I and its expression in E. coli."
    Napoli J.L., Penzes P., Wang X., Sperkova Z.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  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].
    Tissue: Pituitary.
  6. "A novel isoenzyme of aldehyde dehydrogenase specifically involved in the biosynthesis of 9-cis and all-trans retinoic acid."
    Labrecque J., Dumas F., Lacroix A., Bhat P.V.
    Biochem. J. 305:681-684(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19; 80-91; 96-121; 205-225; 237-258 AND 394-438.
    Strain: Sprague-Dawley.
    Tissue: Kidney.

Entry informationi

Entry nameiAL1A1_RAT
AccessioniPrimary (citable) accession number: P51647
Secondary accession number(s): O09184
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.