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O08782

- ALD2_CRIGR

UniProt

O08782 - ALD2_CRIGR

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Protein

Aldose reductase-related protein 2

Gene
AKR1B8
Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Reductase with a preference for aliphatic substrates. Can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates.1 Publication

Catalytic activityi

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

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi211 – 27363NADPAdd
BLAST

GO - Molecular functioni

  1. alditol:NADP+ 1-oxidoreductase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Aldose reductase-related protein 2 (EC:1.1.1.21)
Short name:
AR
Alternative name(s):
Aldehyde reductase
Aldo-keto reductase
Gene namesi
Name:AKR1B8
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Aldose reductase-related protein 2PRO_0000124630Add
BLAST

Expressioni

Tissue specificityi

Detected at very low levels in urinary bladder, testis and jejunum.1 Publication

Inductioni

By FGF-1 By similarity. Up-regulated by calpain inhibitor I (N-acetyl-leucyl-leucyl-norleucinal/ALLN).1 Publication

Interactioni

Subunit structurei

Monomer By similarity.

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 – 10015
Beta strandi105 – 1117
Helixi138 – 15013
Beta strandi153 – 1553
Beta strandi157 – 1615
Helixi164 – 1718
Beta strandi182 – 1865
Helixi194 – 2029
Beta strandi206 – 2105
Beta strandi218 – 2203
Turni228 – 2303
Helixi232 – 2409
Helixi245 – 25410
Turni255 – 2573
Helixi267 – 2737
Helixi283 – 2908
Helixi302 – 3043
Beta strandi305 – 3073

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C9WX-ray2.40A2-316[»]
ProteinModelPortaliO08782.
SMRiO08782. Positions 2-315.

Miscellaneous databases

EvolutionaryTraceiO08782.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG000020.
KOiK00011.

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.

O08782-1 [UniParc]FASTAAdd to Basket

« Hide

MSTFVELSTK AKMPIVGLGT WQSPPGQVKE AVKVAIDAGY RHIDCAYAYY    50
NEHEVGEAIQ EKIKEKAVRR EDLFIVSKLW PTCFERKLLK EAFQKTLTDL 100
KLDYLDLYLI HWPQGLQPGK ELFPKDDQGN VLTSKITFLD AWEVMEELVD 150
EGLVKALGVS NFNHFQIERI LNKPGLKHKP VTNQVECHPY LTQEKLIEYC 200
HSKGITVTAY SPLGSPNRPW AKPEDPSLLE DPKIKEIAAK HKKTSAQVLI 250
RFHIQRNVVV IPKSVTPARI HENFQVFDFQ LSDQEMATIL GFNRNWRACL 300
LPETVNMEEY PYDAEY 316
Length:316
Mass (Da):36,340
Last modified:January 23, 2007 - v3
Checksum:i80B4B8BF0F4FDDAE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U81045 mRNA. Translation: AAC53199.1.
RefSeqiNP_001233680.1. NM_001246751.1.

Genome annotation databases

GeneIDi100689318.
KEGGicge:100689318.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U81045 mRNA. Translation: AAC53199.1 .
RefSeqi NP_001233680.1. NM_001246751.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C9W X-ray 2.40 A 2-316 [» ]
ProteinModelPortali O08782.
SMRi O08782. Positions 2-315.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100689318.
KEGGi cge:100689318.

Organism-specific databases

CTDi 14187.

Phylogenomic databases

HOVERGENi HBG000020.
KOi K00011.

Miscellaneous databases

EvolutionaryTracei O08782.

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. "Cloning, sequencing, and enzymatic activity of an inducible aldo-keto reductase from Chinese hamster ovary cells."
    Hyndman D.J., Takenoshita R., Vera N.L., Pang S.C., Flynn T.G.
    J. Biol. Chem. 272:13286-13291(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY.
    Tissue: Ovary.
  2. "Crystal structure of CHO reductase, a member of the aldo-keto reductase superfamily."
    Ye Q., Hyndman D.J., Li X., Flynn T.G., Jia Z.
    Proteins 38:41-48(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NADPH.

Entry informationi

Entry nameiALD2_CRIGR
AccessioniPrimary (citable) accession number: O08782
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: December 11, 2013
This is version 71 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

3D-structure

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

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