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P51647

- AL1A1_RAT

UniProt

P51647 - AL1A1_RAT

Protein

Retinal dehydrogenase 1

Gene

Aldh1a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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.

    Pathwayi

    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

    1. 3-chloroallyl aldehyde dehydrogenase activity Source: RGD
    2. aldehyde dehydrogenase (NAD) activity Source: RGD
    3. benzaldehyde dehydrogenase (NAD+) activity Source: RGD
    4. identical protein binding Source: RGD
    5. retinal dehydrogenase activity Source: RGD

    GO - Biological processi

    1. 9-cis-retinoic acid biosynthetic process Source: Ensembl
    2. 9-cis-retinoic acid metabolic process Source: RGD
    3. estrous cycle phase Source: RGD
    4. kidney development Source: RGD
    5. liver development Source: RGD
    6. midgut development Source: RGD
    7. optic cup morphogenesis involved in camera-type eye development Source: Ensembl
    8. positive regulation of apoptotic process Source: Ensembl
    9. protein homotetramerization Source: RGD
    10. response to drug Source: RGD
    11. response to estradiol Source: RGD
    12. response to ethanol Source: RGD
    13. response to organic cyclic compound Source: RGD
    14. response to oxidative stress Source: RGD
    15. response to retinoic acid Source: RGD
    16. retinoic acid biosynthetic process Source: RGD
    17. retinol metabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BRENDAi1.2.1.36. 5301.
    ReactomeiREACT_226337. Ethanol oxidation.
    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: Chromosome 1

    Organism-specific databases

    RGDi2087. Aldh1a1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: RGD
    2. nucleus Source: RGD

    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 residuei353 – 3531N6-acetyllysineBy similarity
    Modified residuei367 – 3671N6-acetyllysineBy similarity
    Modified residuei410 – 4101N6-acetyllysineBy 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

    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

    GenevestigatoriP51647.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    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.
    GeneTreeiENSGT00550000074289.
    HOGENOMiHOG000271505.
    HOVERGENiHBG000097.
    KOiK07249.
    OMAiEWHDSAS.
    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

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    MSSPAQPAVP APLANLKIQH TKIFINNEWH DSVSGKKFPV LNPATEEVIC    50
    HVEEGDKADV DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLMERDR 100
    LLLATIEAIN GGKVFANAYL SDLGGSIKAL KYCAGWADKI HGQTIPSDGD 150
    IFTFTRREPI GVCGQIIPWN FPLLMFIWKI GPALSCGNTV VVKPAEQTPL 200
    TALHMASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD KVAFTGSTQV 250
    GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDIAVEF AHHGVFYHQG 300
    QCCVAASRIF VEESVYDEFV RKSVERAKKY VLGNPLTQGI NQGPQIDKEQ 350
    HDKILDLIES GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE 400
    IFGPVQQIMK FKSIDDVIKR ANNTTYGLAA GVFTKDLDRA ITVSSALQAG 450
    VVWVNCYMIL SAQCPFGGFK MSGNGRELGE HGLYEYTELK TVAMKISQKN 500
    S 501
    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:
    EMBL
    GenBank
    DDBJ
    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.
    XP_006231218.1. XM_006231156.1.
    XP_006231219.1. XM_006231157.1.
    XP_006231220.1. XM_006231158.1.
    UniGeneiRn.6132.

    Genome annotation databases

    EnsembliENSRNOT00000024000; ENSRNOP00000024000; ENSRNOG00000017619.
    GeneIDi24188.
    KEGGirno:24188.
    UCSCiRGD:2087. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi JC4524.
    JC5553.
    RefSeqi NP_071852.2. NM_022407.3.
    XP_006231218.1. XM_006231156.1.
    XP_006231219.1. XM_006231157.1.
    XP_006231220.1. XM_006231158.1.
    UniGenei Rn.6132.

    3D structure databases

    ProteinModelPortali P51647.
    SMRi P51647. Positions 9-501.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P51647.
    ChEMBLi CHEMBL2931.

    PTM databases

    PhosphoSitei P51647.

    Proteomic databases

    PaxDbi P51647.
    PRIDEi P51647.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000024000 ; ENSRNOP00000024000 ; ENSRNOG00000017619 .
    GeneIDi 24188.
    KEGGi rno:24188.
    UCSCi RGD:2087. rat.

    Organism-specific databases

    CTDi 216.
    RGDi 2087. Aldh1a1.

    Phylogenomic databases

    eggNOGi COG1012.
    GeneTreei ENSGT00550000074289.
    HOGENOMi HOG000271505.
    HOVERGENi HBG000097.
    KOi K07249.
    OMAi EWHDSAS.
    OrthoDBi EOG7PS1F7.
    PhylomeDBi P51647.
    TreeFami TF300455.

    Enzyme and pathway databases

    UniPathwayi UPA00912 .
    BRENDAi 1.2.1.36. 5301.
    Reactomei REACT_226337. Ethanol oxidation.
    SABIO-RK P51647.

    Miscellaneous databases

    NextBioi 602555.

    Gene expression databases

    Genevestigatori P51647.

    Family and domain databases

    Gene3Di 3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProi 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.
    [Graphical view ]
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 115 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