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Protein

Alcohol dehydrogenase [NADP(+)]

Gene

Akr1a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity). Catalyzes the NADPH-dependent reduction of 3-deoxyglucosone (3-DG).By similarity

Catalytic activityi

An alcohol + NADP+ = an aldehyde + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501Proton donorBy similarity
Sitei80 – 801Lowers pKa of active site TyrBy similarity
Binding sitei113 – 1131SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 2010NADPSequence analysis
Nucleotide bindingi211 – 27363NADPBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiR-RNO-156590. Glutathione conjugation.
R-RNO-5661270. Catabolism of glucuronate to xylulose-5-phosphate.
SABIO-RKP51635.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase [NADP(+)] (EC:1.1.1.2)
Alternative name(s):
3-DG-reducing enzyme
Aldehyde reductase
Aldo-keto reductase family 1 member A1
Gene namesi
Name:Akr1a1
Synonyms:Alr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi68346. Akr1a1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3871.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 325324Alcohol dehydrogenase [NADP(+)]PRO_0000124620Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Modified residuei4 – 41PhosphoserineCombined sources
Glycosylationi23 – 231N-linked (Glc) (glycation)
Modified residuei38 – 381PhosphoserineBy similarity
Glycosylationi68 – 681N-linked (Glc) (glycation)
Glycosylationi85 – 851N-linked (Glc) (glycation)
Modified residuei127 – 1271N6-acetyllysine; alternateBy similarity
Modified residuei127 – 1271N6-succinyllysine; alternateBy similarity
Glycosylationi141 – 1411N-linked (Glc) (glycation)
Modified residuei145 – 1451N6-succinyllysineBy similarity
Glycosylationi153 – 1531N-linked (Glc) (glycation)

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei13 – 131Not glycated
Sitei30 – 301Not glycated
Sitei34 – 341Not glycated
Sitei61 – 611Not glycated
Sitei80 – 801Not glycated
Sitei97 – 971Not glycated
Sitei127 – 1271Not glycated
Sitei134 – 1341Not glycated
Sitei145 – 1451Not glycated
Sitei157 – 1571Not glycated
Sitei240 – 2401Not glycated
Sitei257 – 2571Not glycated
Sitei263 – 2631Not glycated
Sitei287 – 2871Not glycated
Sitei294 – 2941Not glycated
Sitei308 – 3081Not glycated

Keywords - PTMi

Acetylation, Glycation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP51635.
PRIDEiP51635.

2D gel databases

World-2DPAGE0004:P51635.

PTM databases

iPTMnetiP51635.

Expressioni

Gene expression databases

GenevisibleiP51635. RN.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

MINTiMINT-4564842.
STRINGi10116.ENSRNOP00000023072.

Chemistry

BindingDBiP51635.

Structurei

3D structure databases

ProteinModelPortaliP51635.
SMRiP51635. Positions 3-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP51635.
KOiK00002.
OMAiRKHHLDE.
OrthoDBiEOG70KGQF.
PhylomeDBiP51635.
TreeFamiTF106492.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
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.

P51635-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTASSVLLHT GQKMPLIGLG TWKSEPGQVK AAIKYALSVG YRHIDCASVY
60 70 80 90 100
GNETEIGEAL KESVGAGKAV PREELFVTSK LWNTKHHPED VEPAVRKTLA
110 120 130 140 150
DLQLEYLDLY LMHWPYAFER GDNPFPKNAD GTVKYDSTHY KETWKALEAL
160 170 180 190 200
VAKGLVKALG LSNFSSRQID DVLSVASVRP AVLQVECHPY LAQNELIAHC
210 220 230 240 250
QARGLEVTAY SPLGSSDRAW RHPDEPVLLE EPVVLALAEK HGRSPAQILL
260 270 280 290 300
RWQVQRKVIC IPKSITPSRI LQNIQVFDFT FSPEEMKQLD ALNKNWRYIV
310 320
PMITVDGKRV PRDAGHPLYP FNDPY
Length:325
Mass (Da):36,506
Last modified:January 23, 2007 - v2
Checksum:iF95573B7411884DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10854 mRNA. Translation: BAA01627.1.
BC059133 mRNA. Translation: AAH59133.1.
PIRiJN0629.
RefSeqiNP_112262.1. NM_031000.3.
UniGeneiRn.835.

Genome annotation databases

EnsembliENSRNOT00000023072; ENSRNOP00000023072; ENSRNOG00000016727.
GeneIDi78959.
KEGGirno:78959.
UCSCiRGD:68346. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10854 mRNA. Translation: BAA01627.1.
BC059133 mRNA. Translation: AAH59133.1.
PIRiJN0629.
RefSeqiNP_112262.1. NM_031000.3.
UniGeneiRn.835.

3D structure databases

ProteinModelPortaliP51635.
SMRiP51635. Positions 3-325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4564842.
STRINGi10116.ENSRNOP00000023072.

Chemistry

BindingDBiP51635.
ChEMBLiCHEMBL3871.

PTM databases

iPTMnetiP51635.

2D gel databases

World-2DPAGE0004:P51635.

Proteomic databases

PaxDbiP51635.
PRIDEiP51635.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023072; ENSRNOP00000023072; ENSRNOG00000016727.
GeneIDi78959.
KEGGirno:78959.
UCSCiRGD:68346. rat.

Organism-specific databases

CTDi10327.
RGDi68346. Akr1a1.

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP51635.
KOiK00002.
OMAiRKHHLDE.
OrthoDBiEOG70KGQF.
PhylomeDBiP51635.
TreeFamiTF106492.

Enzyme and pathway databases

ReactomeiR-RNO-156590. Glutathione conjugation.
R-RNO-5661270. Catabolism of glucuronate to xylulose-5-phosphate.
SABIO-RKP51635.

Miscellaneous databases

PROiP51635.

Gene expression databases

GenevisibleiP51635. RN.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
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

« Hide 'large scale' publications
  1. "Identity of a major 3-deoxyglucosone-reducing enzyme with aldehyde reductase in rat liver established by amino acid sequencing and cDNA expression."
    Takahashi M., Fujii J., Teshima T., Suzuki K., Shiba T., Taniguchi N.
    Gene 127:249-253(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Kidney and Liver.
  2. "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: Pituitary.
  3. "In vivo glycation of aldehyde reductase, a major 3-deoxyglucosone reducing enzyme: identification of glycation sites."
    Takahashi M., Lu Y.B., Myint T., Fujii J., Wada Y., Taniguchi N.
    Biochemistry 34:1433-1438(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 14-30; 62-77; 81-97; 135-145 AND 146-157, GLYCATION AT LYS-23; LYS-68; LYS-85; LYS-141 AND LYS-153, ABSENCE OF GLYCATION AT LYS-13; LYS-30; LYS-34; LYS-61; LYS-80; LYS-97; LYS-127; LYS-134; LYS-145; LYS-157; LYS-240; LYS-257; LYS-263; LYS-287; LYS-294 AND LYS-308.
  4. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 204-218; 222-240; 270-287 AND 313-325, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  5. Lubec G., Chen W.-Q.
    Submitted (FEB-2007) to UniProtKB
    Cited for: ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAK1A1_RAT
AccessioniPrimary (citable) accession number: P51635
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 118 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.