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P80276

- ALDR_PIG

UniProt

P80276 - ALDR_PIG

Protein

Aldose reductase

Gene

AKR1B1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei49 – 491Proton donor
    Sitei78 – 781Lowers pKa of active site TyrBy similarity
    Binding sitei111 – 1111Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 1910NADPSequence Analysis
    Nucleotide bindingi211 – 27363NADPAdd
    BLAST

    GO - Molecular functioni

    1. alditol:NADP+ 1-oxidoreductase activity Source: UniProtKB-EC
    2. glyceraldehyde oxidoreductase activity Source: Ensembl

    GO - Biological processi

    1. daunorubicin metabolic process Source: Ensembl
    2. doxorubicin metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    ReactomeiREACT_205037. Pregnenolone biosynthesis.
    SABIO-RKP80276.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldose reductase (EC:1.1.1.21)
    Short name:
    AR
    Alternative name(s):
    Aldehyde reductase
    Gene namesi
    Name:AKR1B1
    Synonyms:ALR2
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Chromosome 18

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 316315Aldose reductasePRO_0000124625Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei222 – 2221N6-acetyllysineBy similarity
    Modified residuei263 – 2631N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP80276.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000017525.

    Structurei

    Secondary structure

    1
    316
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63
    Beta strandi12 – 165
    Helixi25 – 3814
    Beta strandi42 – 443
    Helixi47 – 493
    Helixi52 – 6413
    Helixi70 – 723
    Beta strandi74 – 796
    Helixi81 – 833
    Helixi86 – 883
    Helixi89 – 10012
    Beta strandi105 – 1106
    Beta strandi118 – 1203
    Beta strandi129 – 1313
    Helixi138 – 15013
    Beta strandi153 – 1553
    Beta strandi157 – 1615
    Helixi164 – 1718
    Beta strandi181 – 1866
    Helixi194 – 20310
    Beta strandi206 – 2105
    Beta strandi223 – 2253
    Helixi228 – 2303
    Helixi232 – 24110
    Helixi245 – 25511
    Helixi267 – 2726
    Turni273 – 2786
    Helixi283 – 2908
    Helixi302 – 3043
    Helixi311 – 3133

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AH0X-ray2.30A2-316[»]
    1AH3X-ray2.30A2-316[»]
    1AH4X-ray2.00A2-316[»]
    1DLAX-ray3.00A/B/C/D3-316[»]
    1EKOX-ray2.20A2-316[»]
    ProteinModelPortaliP80276.
    SMRiP80276. Positions 2-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP80276.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0656.
    GeneTreeiENSGT00670000097881.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    KOiK00011.
    OrthoDBiEOG70KGQF.
    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.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P80276-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASHLVLYTG AKMPILGLGT WKSPPGKVTE AVKVAIDLGY RHIDCAHVYQ    50
    NENEVGLGLQ EKLQGQVVKR EDLFIVSKLW CTDHEKNLVK GACQTTLRDL 100
    KLDYLDLYLI HWPTGFKPGK DPFPLDGDGN VVPDESDFVE TWEAMEELVD 150
    EGLVKAIGVS NFNHLQVEKI LNKPGLKYKP AVNQIEVHPY LTQEKLIEYC 200
    KSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK YNKTTAQVLI 250
    RFPMQRNLIV IPKSVTPERI AENFQVFDFE LSPEDMNTLL SYNRNWRVCA 300
    LMSCASHKDY PFHEEY 316
    Length:316
    Mass (Da):35,868
    Last modified:January 23, 2007 - v2
    Checksum:i7218B663AC1B4E92
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti99 – 991D → N in AAA30989. (PubMed:8493902)Curated
    Sequence conflicti99 – 991D → N in AAC48515. (PubMed:8493902)Curated

    Mass spectrometryi

    Molecular mass is 35778±3 Da from positions 2 - 316. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14950 mRNA. Translation: AAA30989.1.
    U46065 mRNA. Translation: AAC48515.1.
    PIRiA59021.
    RefSeqiNP_001001539.1. NM_001001539.2.
    UniGeneiSsc.3059.

    Genome annotation databases

    EnsembliENSSSCT00000018009; ENSSSCP00000017525; ENSSSCG00000016539.
    GeneIDi396816.
    KEGGissc:396816.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14950 mRNA. Translation: AAA30989.1 .
    U46065 mRNA. Translation: AAC48515.1 .
    PIRi A59021.
    RefSeqi NP_001001539.1. NM_001001539.2.
    UniGenei Ssc.3059.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AH0 X-ray 2.30 A 2-316 [» ]
    1AH3 X-ray 2.30 A 2-316 [» ]
    1AH4 X-ray 2.00 A 2-316 [» ]
    1DLA X-ray 3.00 A/B/C/D 3-316 [» ]
    1EKO X-ray 2.20 A 2-316 [» ]
    ProteinModelPortali P80276.
    SMRi P80276. Positions 2-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000017525.

    Chemistry

    BindingDBi P80276.
    ChEMBLi CHEMBL4559.

    Proteomic databases

    PaxDbi P80276.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSSSCT00000018009 ; ENSSSCP00000017525 ; ENSSSCG00000016539 .
    GeneIDi 396816.
    KEGGi ssc:396816.

    Organism-specific databases

    CTDi 231.

    Phylogenomic databases

    eggNOGi COG0656.
    GeneTreei ENSGT00670000097881.
    HOGENOMi HOG000250272.
    HOVERGENi HBG000020.
    KOi K00011.
    OrthoDBi EOG70KGQF.
    TreeFami TF106492.

    Enzyme and pathway databases

    Reactomei REACT_205037. Pregnenolone biosynthesis.
    SABIO-RK P80276.

    Miscellaneous databases

    EvolutionaryTracei P80276.

    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.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Location of an essential arginine residue in the primary structure of pig aldose reductase."
      Kubiseski T.J., Green N.C., Flynn T.G.
      Adv. Exp. Med. Biol. 328:259-265(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes."
      Jaquinod M., Potier N., Klarskov K., Reymann J.-M., Sorokine O., Kieffer S., Barth P., Andriantomanga V., Biellmann J.-F., van Dorsselaer A.
      Eur. J. Biochem. 218:893-903(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-316, MASS SPECTROMETRY.
      Tissue: Lens.
    3. "Novel NADPH-binding domain revealed by the crystal structure of aldose reductase."
      Rondeau J.-M., Tete-Favier F., Podjarny A., Reymann J.-M., Barth P., Biellmann J.-F., Moras D.
      Nature 355:469-472(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    4. "A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil."
      Urzhumtsev A., Tete-Favier F., Mitschler A., Barbanton J., Barth P., Urzhumtseva L., Biellmann J.-F., Podjarny A.D., Moras D.
      Structure 5:601-612(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

    Entry informationi

    Entry nameiALDR_PIG
    AccessioniPrimary (citable) accession number: P80276
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 109 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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