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Protein

Aldose reductase-related protein 1

Gene

Akr1b7

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

Functioni

Reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. May play a role in the metabolism of xenobiotic aromatic aldehydes.1 Publication

Catalytic activityi

Alditol + NAD(P)+ = aldose + NAD(P)H.2 Publications

Enzyme regulationi

Inhibited by tolrestat and epalrestat.1 Publication

Kineticsi

  1. KM=1.5 µM for NADPH2 Publications
  2. KM=220 µM for NADH2 Publications
  3. KM=0.16 µM for 4-oxo-2-nonenal2 Publications
  4. KM=37 µM for geraniol2 Publications
  5. KM=1.5 µM for 4-nitrobenzaldehyde2 Publications

    pH dependencei

    Optimum pH is 6.5-7.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei44NADP1 Publication1
    Active sitei49Proton donorBy similarity1
    Sitei78Lowers pKa of active site TyrBy similarity1
    Binding sitei184NADP1 Publication1
    Binding sitei273NADP1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi20 – 21NADP1 Publication2
    Nucleotide bindingi160 – 161NADP1 Publication2
    Nucleotide bindingi210 – 215NADP1 Publication6
    Nucleotide bindingi263 – 269NADP1 Publication7

    GO - Molecular functioni

    • alditol:NADP+ 1-oxidoreductase activity Source: RGD
    • aldo-keto reductase (NADP) activity Source: RGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    ReactomeiR-RNO-193144. Estrogen biosynthesis.
    R-RNO-975634. Retinoid metabolism and transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldose reductase-related protein 1 (EC:1.1.1.21)
    Alternative name(s):
    Aldehyde reductase
    Aldo-keto reductase family 1 member B7
    Aldose reductase-like protein AKR1B14
    Gene namesi
    Name:Akr1b7
    Synonyms:Akr1b14
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Chromosome 4

    Organism-specific databases

    RGDi620257. Akr1b7.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi269H → F or R: Reduced affinity for NADP. 1 Publication1
    Mutagenesisi269H → M: Strongly reduced affinity for NADP. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL3421523.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedBy similarity
    ChainiPRO_00004153512 – 316Aldose reductase-related protein 1Add BLAST315

    Proteomic databases

    PaxDbiQ5RJP0.
    PRIDEiQ5RJP0.

    PTM databases

    iPTMnetiQ5RJP0.
    PhosphoSitePlusiQ5RJP0.

    Expressioni

    Gene expression databases

    BgeeiENSRNOG00000009875.
    GenevisibleiQ5RJP0. RN.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000013423.

    Chemistry databases

    BindingDBiQ5RJP0.

    Structurei

    Secondary structure

    1316
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 6Combined sources3
    Beta strandi12 – 19Combined sources8
    Helixi27 – 37Combined sources11
    Beta strandi42 – 44Combined sources3
    Helixi47 – 49Combined sources3
    Helixi52 – 64Combined sources13
    Helixi70 – 72Combined sources3
    Beta strandi74 – 79Combined sources6
    Helixi81 – 83Combined sources3
    Helixi86 – 100Combined sources15
    Beta strandi105 – 111Combined sources7
    Helixi138 – 150Combined sources13
    Beta strandi153 – 161Combined sources9
    Helixi164 – 171Combined sources8
    Beta strandi182 – 186Combined sources5
    Helixi194 – 201Combined sources8
    Turni202 – 204Combined sources3
    Beta strandi206 – 210Combined sources5
    Helixi228 – 230Combined sources3
    Helixi232 – 241Combined sources10
    Helixi245 – 254Combined sources10
    Turni255 – 257Combined sources3
    Helixi267 – 273Combined sources7
    Helixi283 – 290Combined sources8
    Helixi302 – 304Combined sources3
    Helixi311 – 313Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3O3RX-ray1.86A/B1-316[»]
    3QKZX-ray1.87A/B1-316[»]
    ProteinModelPortaliQ5RJP0.
    SMRiQ5RJP0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5RJP0.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiKOG1577. Eukaryota.
    COG0656. LUCA.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiQ5RJP0.
    KOiK00011.
    OMAiPDRPYAK.
    OrthoDBiEOG091G0D69.
    PhylomeDBiQ5RJP0.
    TreeFamiTF106492.

    Family and domain databases

    CDDicd06660. Aldo_ket_red. 1 hit.
    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 2 hits.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q5RJP0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTTFVKLRTK AKMPLVGLGT WKSPPGQVKE AVKAAIDAGY RHFDCAYVYQ
    60 70 80 90 100
    NESEVGEAIQ EKIKEKAVRR EDLFIVSKLW STFFEKSLMK EAFQKTLSDL
    110 120 130 140 150
    KLDYLDLYLI HWPQGLQAGK EFLPKDSQGK VLMSKSTFLD AWEGMEELVD
    160 170 180 190 200
    QGLVKALGVS NFNHFQIERL LNKPGLKHKP VTNQVECHPY LTQEKLIQYC
    210 220 230 240 250
    HSKGIAVIAY SPLGSPDRPY AKPEDPVVLE IPKIKEIAAK HKKTIAQVLI
    260 270 280 290 300
    RFHVQRNVAV IPKSVTLSHI KENIQVFDFQ LSEEDMAAIL SLNRNWRACG
    310
    LFVTSDEEDF PFHEEY
    Length:316
    Mass (Da):36,122
    Last modified:December 21, 2004 - v1
    Checksum:iE5733ADA0ED5FF21
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CH473959 Genomic DNA. Translation: EDM15308.1.
    BC086563 mRNA. Translation: AAH86563.1.
    RefSeqiNP_446233.2. NM_053781.2.
    UniGeneiRn.32702.

    Genome annotation databases

    EnsembliENSRNOT00000013423; ENSRNOP00000013423; ENSRNOG00000009875.
    GeneIDi116463.
    KEGGirno:116463.
    UCSCiRGD:620257. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CH473959 Genomic DNA. Translation: EDM15308.1.
    BC086563 mRNA. Translation: AAH86563.1.
    RefSeqiNP_446233.2. NM_053781.2.
    UniGeneiRn.32702.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3O3RX-ray1.86A/B1-316[»]
    3QKZX-ray1.87A/B1-316[»]
    ProteinModelPortaliQ5RJP0.
    SMRiQ5RJP0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000013423.

    Chemistry databases

    BindingDBiQ5RJP0.
    ChEMBLiCHEMBL3421523.

    PTM databases

    iPTMnetiQ5RJP0.
    PhosphoSitePlusiQ5RJP0.

    Proteomic databases

    PaxDbiQ5RJP0.
    PRIDEiQ5RJP0.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000013423; ENSRNOP00000013423; ENSRNOG00000009875.
    GeneIDi116463.
    KEGGirno:116463.
    UCSCiRGD:620257. rat.

    Organism-specific databases

    CTDi11997.
    RGDi620257. Akr1b7.

    Phylogenomic databases

    eggNOGiKOG1577. Eukaryota.
    COG0656. LUCA.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiQ5RJP0.
    KOiK00011.
    OMAiPDRPYAK.
    OrthoDBiEOG091G0D69.
    PhylomeDBiQ5RJP0.
    TreeFamiTF106492.

    Enzyme and pathway databases

    ReactomeiR-RNO-193144. Estrogen biosynthesis.
    R-RNO-975634. Retinoid metabolism and transport.

    Miscellaneous databases

    EvolutionaryTraceiQ5RJP0.
    PROiQ5RJP0.

    Gene expression databases

    BgeeiENSRNOG00000009875.
    GenevisibleiQ5RJP0. RN.

    Family and domain databases

    CDDicd06660. Aldo_ket_red. 1 hit.
    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 2 hits.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiALD1_RAT
    AccessioniPrimary (citable) accession number: Q5RJP0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: December 21, 2004
    Last modified: November 2, 2016
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    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.