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P15122

- ALDR_RABIT

UniProt

P15122 - ALDR_RABIT

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Protein

Aldose reductase

Gene

AKR1B1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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 donorBy similarity
Sitei78 – 781Lowers pKa of active site TyrBy similarity
Binding sitei111 – 1111SubstrateBy similarity

Regions

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

GO - Molecular functioni

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

SABIO-RKP15122.

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 316315Aldose reductasePRO_0000124626Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei95 – 951N6-acetyllysineBy similarity
Modified residuei222 – 2221N6-acetyllysineBy similarity
Modified residuei263 – 2631N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP15122.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000014272.

Structurei

3D structure databases

ProteinModelPortaliP15122.
SMRiP15122. Positions 1-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiCOG0656.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP15122.

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.

P15122-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATHLVLYNG AKMPILGLGT WKSPPGQVTE AVKTAIDLGY RHIDCAHVYQ
60 70 80 90 100
NENEVGVALQ EKLKEQVVKR EELFIVSKLW CTSHDKSLVK GACQKTLNDL
110 120 130 140 150
KLDYLDLYLI HWPTGFKHGS EYFPLDAAGN VIPSDTDFLD TWEAMEGLVD
160 170 180 190 200
EGLVKSIGVS NFNHLQIERI LNKPGLKYKP AVNQIECHPY LTQEKLIQYC
210 220 230 240 250
HSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIADK HKKTTAQVLI
260 270 280 290 300
RFPMQRNLVV IPKSVTPARI AENFQVFDFE LSSEDMTTLL SYNRNWRVCA
310
LVSCASHKDY PFHAEF
Length:316
Mass (Da):35,763
Last modified:January 23, 2007 - v3
Checksum:iE52C078822BC2DFB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U13694
, U13689, U13690, U13691, U13692, U13693 Genomic DNA. Translation: AAB60687.1.
M32818 mRNA. Translation: AAA31160.1.
U12316 mRNA. Translation: AAA50833.1.
J05048 mRNA. Translation: AAA31157.1.
PIRiA34406.
RefSeqiNP_001075756.1. NM_001082287.1.
UniGeneiOcu.1743.

Genome annotation databases

GeneIDi100009122.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U13694
, U13689 , U13690 , U13691 , U13692 , U13693 Genomic DNA. Translation: AAB60687.1 .
M32818 mRNA. Translation: AAA31160.1 .
U12316 mRNA. Translation: AAA50833.1 .
J05048 mRNA. Translation: AAA31157.1 .
PIRi A34406.
RefSeqi NP_001075756.1. NM_001082287.1.
UniGenei Ocu.1743.

3D structure databases

ProteinModelPortali P15122.
SMRi P15122. Positions 1-316.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000014272.

Chemistry

ChEMBLi CHEMBL3567.

Proteomic databases

PRIDEi P15122.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009122.

Organism-specific databases

CTDi 231.

Phylogenomic databases

eggNOGi COG0656.
HOGENOMi HOG000250272.
HOVERGENi HBG000020.
InParanoidi P15122.

Enzyme and pathway databases

SABIO-RK P15122.

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, genomic organization, and osmotic response of the aldose reductase gene."
    Ferraris J.D., Williams C.K., Martin B.M., Burg M.B., Garcia-Perez A.
    Proc. Natl. Acad. Sci. U.S.A. 91:10742-10746(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Spleen.
  2. "Molecular cloning of cDNA coding for kidney aldose reductase. Regulation of specific mRNA accumulation by NaCl-mediated osmotic stress."
    Garcia-Perez A., Martin B., Murphy H.R., Uchida S., Murer H., Cowley B.D. Jr., Handler J.S., Burg M.B.
    J. Biol. Chem. 264:16815-16821(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-316.
    Tissue: Kidney.

Entry informationi

Entry nameiALDR_RABIT
AccessioniPrimary (citable) accession number: P15122
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 94 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3