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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei44 – 441NADP1 Publication
    Active sitei49 – 491Proton donorBy similarity
    Sitei78 – 781Lowers pKa of active site TyrBy similarity
    Binding sitei184 – 1841NADP1 Publication
    Binding sitei273 – 2731NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi20 – 212NADP1 Publication
    Nucleotide bindingi160 – 1612NADP1 Publication
    Nucleotide bindingi210 – 2156NADP1 Publication
    Nucleotide bindingi263 – 2697NADP1 Publication

    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

    ReactomeiREACT_319671. 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
    ProteomesiUP000002494 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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi269 – 2691H → F or R: Reduced affinity for NADP. 1 Publication
    Mutagenesisi269 – 2691H → M: Strongly reduced affinity for NADP. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 316316Aldose reductase-related protein 1PRO_0000415351Add
    BLAST

    Proteomic databases

    PaxDbiQ5RJP0.
    PRIDEiQ5RJP0.

    Expressioni

    Gene expression databases

    GenevisibleiQ5RJP0. RN.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000013423.

    Structurei

    Secondary structure

    1
    316
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63Combined sources
    Beta strandi12 – 198Combined sources
    Helixi27 – 3711Combined sources
    Beta strandi42 – 443Combined sources
    Helixi47 – 493Combined sources
    Helixi52 – 6413Combined sources
    Helixi70 – 723Combined sources
    Beta strandi74 – 796Combined sources
    Helixi81 – 833Combined sources
    Helixi86 – 10015Combined sources
    Beta strandi105 – 1117Combined sources
    Helixi138 – 15013Combined sources
    Beta strandi153 – 1619Combined sources
    Helixi164 – 1718Combined sources
    Beta strandi182 – 1865Combined sources
    Helixi194 – 2018Combined sources
    Turni202 – 2043Combined sources
    Beta strandi206 – 2105Combined sources
    Helixi228 – 2303Combined sources
    Helixi232 – 24110Combined sources
    Helixi245 – 25410Combined sources
    Turni255 – 2573Combined sources
    Helixi267 – 2737Combined sources
    Helixi283 – 2908Combined sources
    Helixi302 – 3043Combined sources
    Helixi311 – 3133Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3O3RX-ray1.86A/B1-316[»]
    3QKZX-ray1.87A/B1-316[»]
    ProteinModelPortaliQ5RJP0.
    SMRiQ5RJP0. Positions 1-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5RJP0.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0656.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiQ5RJP0.
    KOiK00011.
    OMAiHINCAYV.
    OrthoDBiEOG70KGQF.
    PhylomeDBiQ5RJP0.
    TreeFamiTF106492.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase_subgr.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    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.

    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3O3RX-ray1.86A/B1-316[»]
    3QKZX-ray1.87A/B1-316[»]
    ProteinModelPortaliQ5RJP0.
    SMRiQ5RJP0. Positions 1-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000013423.

    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

    eggNOGiCOG0656.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiQ5RJP0.
    KOiK00011.
    OMAiHINCAYV.
    OrthoDBiEOG70KGQF.
    PhylomeDBiQ5RJP0.
    TreeFamiTF106492.

    Enzyme and pathway databases

    ReactomeiREACT_319671. Retinoid metabolism and transport.

    Miscellaneous databases

    EvolutionaryTraceiQ5RJP0.
    NextBioi618984.
    PROiQ5RJP0.

    Gene expression databases

    GenevisibleiQ5RJP0. RN.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase_subgr.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    3. "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: Ovary.
    4. "Rat aldose reductase-like protein (AKR1B14) efficiently reduces the lipid peroxidation product 4-oxo-2-nonenal."
      Endo S., Matsunaga T., Fujita A., Tajima K., El-Kabbani O., Hara A.
      Biol. Pharm. Bull. 33:1886-1890(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    5. "Structure of rat aldose reductase-like protein AKR1B14 holoenzyme: Probing the role of His269 in coenzyme binding by site-directed mutagenesis."
      Sundaram K., Dhagat U., Endo S., Chung R., Matsunaga T., Hara A., El-Kabbani O.
      Bioorg. Med. Chem. Lett. 21:801-804(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH NADP, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-269.

    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: June 24, 2015
    This is version 76 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

    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.