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Protein

Retinal dehydrogenase 1

Gene

Aldh1a1

Organism
Rattus norvegicus (Rat)
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 (PubMed:7832787). May have a broader specificity and oxidize other aldehydes in vivo (By similarity).By similarity1 Publication

Catalytic activityi

Retinal + NAD+ + H2O = retinoate + NADH.1 Publication

Enzyme regulationi

Inhibited by chloral hydrate.1 Publication

Kineticsi

Has more than 2-fold higher catalytic efficiency for 9-cis retinal compared to all-trans retinal and 11-cis retinal.1 Publication
  1. KM=5.7 µM for 9-cis retinal (at pH 7.5 and 25 degrees Celsius)1 Publication
  2. KM=9.8 µM for all-trans retinal (at pH 7.5 and 25 degrees Celsius)1 Publication
  3. KM=10.5 µM for 11-cis retinal (at pH 7.5 and 25 degrees Celsius)1 Publication

    Pathwayi: retinol metabolism

    This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.1 Publication
    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
    Active sitei303NucleophilePROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi167 – 170NADBy similarity4
    Nucleotide bindingi193 – 196NADBy similarity4
    Nucleotide bindingi226 – 227NADBy similarity2
    Nucleotide bindingi246 – 247NADBy similarity2
    Nucleotide bindingi269 – 271NADBy similarity3
    Nucleotide bindingi349 – 353NADBy similarity5
    Nucleotide bindingi400 – 402NADBy similarity3

    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
    • NAD binding Source: CAFA
    • retinal dehydrogenase activity Source: UniProtKB

    GO - Biological processi

    • 9-cis-retinoic acid metabolic process Source: RGD
    • estrous cycle Source: RGD
    • kidney development Source: RGD
    • liver development Source: RGD
    • midgut development Source: RGD
    • oxidation-reduction process Source: UniProtKB
    • 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
    • retinoid metabolic process Source: UniProtKB
    • retinol metabolic process Source: UniProtKB-UniPathway

    Keywordsi

    Molecular functionOxidoreductase
    LigandNAD

    Enzyme and pathway databases

    BRENDAi1.2.1.36 5301
    SABIO-RKiP51647
    UniPathwayiUPA00912

    Chemistry databases

    SwissLipidsiSLP:000000800

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinal dehydrogenase 1Curated (EC:1.2.1.-By similarity, EC:1.2.1.361 Publication)
    Short name:
    RALDH 11 Publication
    Short name:
    RalDH11 Publication
    Alternative name(s):
    ALDH-E1
    ALHDII
    Aldehyde dehydrogenase family 1 member A1Imported
    Aldehyde dehydrogenase, cytosolic1 Publication
    Gene namesi
    Name:Aldh1a1Imported
    Synonyms:Aldh1 Publication
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Unplaced

    Organism-specific databases

    RGDi2087 Aldh1a1

    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

    Chemistry databases

    ChEMBLiCHEMBL2931

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedBy similarity1 Publication
    ChainiPRO_00000564192 – 501Retinal dehydrogenase 1Add BLAST500

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylserineBy similarity1
    Modified residuei91N6-acetyllysineBy similarity1
    Modified residuei128N6-acetyllysineBy similarity1
    Modified residuei252N6-acetyllysineBy similarity1
    Modified residuei337PhosphothreonineBy similarity1
    Modified residuei353N6-acetyllysineBy similarity1
    Modified residuei367N6-acetyllysineBy similarity1
    Modified residuei410N6-acetyllysineBy similarity1
    Modified residuei413PhosphoserineCombined sources1
    Modified residuei419N6-acetyllysineBy similarity1
    Modified residuei435N6-acetyllysineBy similarity1
    Modified residuei495N6-acetyllysineBy similarity1

    Post-translational modificationi

    The N-terminus is blocked most probably by acetylation.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP51647
    PRIDEiP51647

    PTM databases

    iPTMnetiP51647
    PhosphoSitePlusiP51647

    Expressioni

    Tissue specificityi

    Strongly expressed in kidney, lung, testis, intestine, stomach, and trachea, but weakly in the liver.1 Publication

    Gene expression databases

    GenevisibleiP51647 RN

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    GO - Molecular functioni

    • identical protein binding Source: RGD

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000024000

    Chemistry databases

    BindingDBiP51647

    Structurei

    3D structure databases

    ProteinModelPortaliP51647
    SMRiP51647
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiKOG2450 Eukaryota
    COG1012 LUCA
    HOGENOMiHOG000271505
    HOVERGENiHBG000097
    InParanoidiP51647
    KOiK07249
    OrthoDBiEOG091G05E8
    PhylomeDBiP51647
    TreeFamiTF300455

    Family and domain databases

    Gene3Di3.40.309.10, 1 hit
    3.40.605.10, 2 hits
    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

    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)DescriptionActionsGraphical viewLength
    Sequence conflicti100R → C in AAA96657 (PubMed:8543180).Curated1
    Sequence conflicti106I → M AA sequence (PubMed:7832787).Curated1
    Sequence conflicti170N → E in AAA96657 (PubMed:8543180).Curated1

    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

    Similar proteinsi

    Entry informationi

    Entry nameiAL1A1_RAT
    AccessioniPrimary (citable) accession number: P51647
    Secondary accession number(s): O09184
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: May 23, 2018
    This is version 141 of the entry and version 3 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health