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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

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

Manual assertion based on experiment ini

  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
    • retinal dehydrogenase activity Source: RGD

    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
    • 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.
    SABIO-RKP51647.
    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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Unplaced

    Organism-specific databases

    RGDi2087. Aldh1a1.

    Subcellular locationi

    • Cytoplasmcytosol By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Chemistry databases

    ChEMBLiCHEMBL2931.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 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

    BgeeiENSRNOG00000017619.
    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.
    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. 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)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.

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000024000.

    Chemistry databases

    BindingDBiP51647.
    ChEMBLiCHEMBL2931.
    SwissLipidsiSLP:000000800.

    PTM databases

    iPTMnetiP51647.
    PhosphoSitePlusiP51647.

    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

    eggNOGiKOG2450. Eukaryota.
    COG1012. LUCA.
    HOGENOMiHOG000271505.
    HOVERGENiHBG000097.
    InParanoidiP51647.
    KOiK07249.
    OrthoDBiEOG091G05E8.
    PhylomeDBiP51647.
    TreeFamiTF300455.

    Enzyme and pathway databases

    UniPathwayiUPA00912.
    BRENDAi1.2.1.36. 5301.
    SABIO-RKP51647.

    Miscellaneous databases

    PROiP51647.

    Gene expression databases

    BgeeiENSRNOG00000017619.
    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...

    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: November 30, 2016
    This is version 133 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

    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.