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Protein

Aldose reductase

Gene

AKR1B1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_347635. Pregnenolone biosynthesis.
REACT_359116. Fructose 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 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.

Expressioni

Gene expression databases

GenevisibleiP80276. SS.

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 – 63Combined sources
Beta strandi12 – 165Combined sources
Helixi25 – 3814Combined sources
Beta strandi42 – 443Combined sources
Helixi47 – 493Combined sources
Helixi52 – 6413Combined sources
Helixi70 – 723Combined sources
Beta strandi74 – 796Combined sources
Helixi81 – 833Combined sources
Helixi86 – 883Combined sources
Helixi89 – 10012Combined sources
Beta strandi105 – 1106Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi129 – 1313Combined sources
Helixi138 – 15013Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi157 – 1615Combined sources
Helixi164 – 1718Combined sources
Beta strandi181 – 1866Combined sources
Helixi194 – 20310Combined sources
Beta strandi206 – 2105Combined sources
Beta strandi223 – 2253Combined sources
Helixi228 – 2303Combined sources
Helixi232 – 24110Combined sources
Helixi245 – 25511Combined sources
Helixi267 – 2726Combined sources
Turni273 – 2786Combined 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
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.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP80276.
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

        10         20         30         40         50
MASHLVLYTG AKMPILGLGT WKSPPGKVTE AVKVAIDLGY RHIDCAHVYQ
60 70 80 90 100
NENEVGLGLQ EKLQGQVVKR EDLFIVSKLW CTDHEKNLVK GACQTTLRDL
110 120 130 140 150
KLDYLDLYLI HWPTGFKPGK DPFPLDGDGN VVPDESDFVE TWEAMEELVD
160 170 180 190 200
EGLVKAIGVS NFNHLQVEKI LNKPGLKYKP AVNQIEVHPY LTQEKLIEYC
210 220 230 240 250
KSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK YNKTTAQVLI
260 270 280 290 300
RFPMQRNLIV IPKSVTPERI AENFQVFDFE LSPEDMNTLL SYNRNWRVCA
310
LMSCASHKDY PFHEEY
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:
EMBLi
GenBanki
DDBJi
Links Updated
L14950 mRNA. Translation: AAA30989.1.
U46065 mRNA. Translation: AAC48515.1.
PIRiA59021.
RefSeqiNP_001001539.1. NM_001001539.2.
UniGeneiSsc.3059.

Genome annotation databases

GeneIDi396816.
KEGGissc:396816.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14950 mRNA. Translation: AAA30989.1.
U46065 mRNA. Translation: AAC48515.1.
PIRiA59021.
RefSeqiNP_001001539.1. NM_001001539.2.
UniGeneiSsc.3059.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000017525.

Chemistry

BindingDBiP80276.
ChEMBLiCHEMBL4559.

Proteomic databases

PaxDbiP80276.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396816.
KEGGissc:396816.

Organism-specific databases

CTDi231.

Phylogenomic databases

eggNOGiCOG0656.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP80276.
KOiK00011.
OrthoDBiEOG70KGQF.
TreeFamiTF106492.

Enzyme and pathway databases

ReactomeiREACT_347635. Pregnenolone biosynthesis.
REACT_359116. Fructose biosynthesis.
SABIO-RKP80276.

Miscellaneous databases

EvolutionaryTraceiP80276.
PROiP80276.

Gene expression databases

GenevisibleiP80276. SS.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 117 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

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.