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Q5RJP0

- ALD1_RAT

UniProt

Q5RJP0 - ALD1_RAT

Protein

Aldose reductase-related protein 1

Gene

Akr1b7

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    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

    1. alditol:NADP+ 1-oxidoreductase activity Source: RGD
    2. aldo-keto reductase (NADP) activity Source: RGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    ReactomeiREACT_199015. 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: Chromosome 4

    Organism-specific databases

    RGDi620257. Akr1b7.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. mitochondrion Source: Ensembl

    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

    GenevestigatoriQ5RJP0.

    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 – 63
    Beta strandi12 – 198
    Helixi27 – 3711
    Beta strandi42 – 443
    Helixi47 – 493
    Helixi52 – 6413
    Helixi70 – 723
    Beta strandi74 – 796
    Helixi81 – 833
    Helixi86 – 10015
    Beta strandi105 – 1117
    Helixi138 – 15013
    Beta strandi153 – 1619
    Helixi164 – 1718
    Beta strandi182 – 1865
    Helixi194 – 2018
    Turni202 – 2043
    Beta strandi206 – 2105
    Helixi228 – 2303
    Helixi232 – 24110
    Helixi245 – 25410
    Turni255 – 2573
    Helixi267 – 2737
    Helixi283 – 2908
    Helixi302 – 3043
    Helixi311 – 3133

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00670000097881.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiQ5RJP0.
    KOiK00011.
    OMAiFQIENIL.
    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

    MTTFVKLRTK AKMPLVGLGT WKSPPGQVKE AVKAAIDAGY RHFDCAYVYQ    50
    NESEVGEAIQ EKIKEKAVRR EDLFIVSKLW STFFEKSLMK EAFQKTLSDL 100
    KLDYLDLYLI HWPQGLQAGK EFLPKDSQGK VLMSKSTFLD AWEGMEELVD 150
    QGLVKALGVS NFNHFQIERL LNKPGLKHKP VTNQVECHPY LTQEKLIQYC 200
    HSKGIAVIAY SPLGSPDRPY AKPEDPVVLE IPKIKEIAAK HKKTIAQVLI 250
    RFHVQRNVAV IPKSVTLSHI KENIQVFDFQ LSEEDMAAIL SLNRNWRACG 300
    LFVTSDEEDF PFHEEY 316
    Length:316
    Mass (Da):36,122
    Last modified:December 21, 2004 - v1
    Checksum:iE5733ADA0ED5FF21
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH473959 Genomic DNA. Translation: EDM15308.1 .
    BC086563 mRNA. Translation: AAH86563.1 .
    RefSeqi NP_446233.2. NM_053781.2.
    UniGenei Rn.32702.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3O3R X-ray 1.86 A/B 1-316 [» ]
    3QKZ X-ray 1.87 A/B 1-316 [» ]
    ProteinModelPortali Q5RJP0.
    SMRi Q5RJP0. Positions 1-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000013423.

    Proteomic databases

    PaxDbi Q5RJP0.
    PRIDEi Q5RJP0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000013423 ; ENSRNOP00000013423 ; ENSRNOG00000009875 .
    GeneIDi 116463.
    KEGGi rno:116463.
    UCSCi RGD:620257. rat.

    Organism-specific databases

    CTDi 11997.
    RGDi 620257. Akr1b7.

    Phylogenomic databases

    eggNOGi COG0656.
    GeneTreei ENSGT00670000097881.
    HOGENOMi HOG000250272.
    HOVERGENi HBG000020.
    InParanoidi Q5RJP0.
    KOi K00011.
    OMAi FQIENIL.
    OrthoDBi EOG70KGQF.
    PhylomeDBi Q5RJP0.
    TreeFami TF106492.

    Enzyme and pathway databases

    Reactomei REACT_199015. Retinoid metabolism and transport.

    Miscellaneous databases

    EvolutionaryTracei Q5RJP0.
    NextBioi 618984.
    PROi Q5RJP0.

    Gene expression databases

    Genevestigatori Q5RJP0.

    Family and domain databases

    Gene3Di 3.20.20.100. 1 hit.
    InterProi IPR001395. Aldo/ket_red.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase_subgr.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view ]
    PANTHERi PTHR11732. PTHR11732. 1 hit.
    Pfami PF00248. Aldo_ket_red. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000097. AKR. 1 hit.
    PRINTSi PR00069. ALDKETRDTASE.
    SUPFAMi SSF51430. SSF51430. 1 hit.
    PROSITEi PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 71 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