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UniProtKB/Swiss-Prot entry P51635

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AK1A1_RAT
Primary accession number P51635
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 53)
Name and origin of the protein
Protein name Alcohol dehydrogenase [NADP+]
Synonyms EC 1.1.1.2
Aldehyde reductase
Aldo-keto reductase family 1 member A1
3-DG-reducing enzyme
Gene name
Name: Akr1a1
Synonyms: Alr
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Kidney, and Liver;
DOI=10.1016/0378-1119(93)90728-L; PubMed=8500767 [NCBI, ExPASy, EBI, Israel, Japan]
Takahashi M., Fujii J., Teshima T., Suzuki K., Shiba T., Taniguchi N.;
"Identity of a major 3-deoxyglucosone-reducing enzyme with aldehyde reductase in rat liver established by amino acid sequencing and cDNA expression.";
Gene 127:249-253(1993).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
 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, AND 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.
DOI=10.1021/bi00004a038; PubMed=7827091 [NCBI, ExPASy, EBI, Israel, Japan]
Takahashi M., Lu Y.B., Myint T., Fujii J., Wada Y., Taniguchi N.;
"In vivo glycation of aldehyde reductase, a major 3-deoxyglucosone reducing enzyme: identification of glycation sites.";
Biochemistry 34:1433-1438(1995).
[4]
 PROTEIN SEQUENCE OF 204-218; 222-240; 270-287 AND 313-325, AND MASS SPECTROMETRY.
STRAIN=Sprague-Dawley;
TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (NOV-2006) to UniProtKB.
[5]
 ACETYLATION AT THR-2, AND MASS SPECTROMETRY.
Lubec G., Chen W.-Q.;
Submitted (FEB-2007) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D10854; BAA01627.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC059133; AAH59133.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JN0629; JN0629.
RefSeq NP_112262.1; -.
UniGene Rn.835
3D structure databases
HSSP P14550; 2ALR. [HSSP ENTRY / PDB]
SMR P51635; 3-325.
ModBase P51635.
Organism-specific databases
RGD 68346; Akr1a1.
Gene expression databases
ArrayExpress P51635; -.
GermOnline ENSRNOG00000016727; Rattus norvegicus.
Ontologies
GO
GO:0008106; Molecular function: alcohol dehydrogenase (NADP+) activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR001395; Aldo/ket_red.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.100; Aldo/ket_red; 1.
PANTHER PTHR11732; Aldo/ket_red; 1.
Pfam PF00248; Aldo_ket_red; 1.
Pfam graphical view of domain structure.
PRINTS PR00069; ALDKETRDTASE.
ProDom PD000288; Aldo/ket_red; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00798; ALDOKETO_REDUCTASE_1; 1.
PS00062; ALDOKETO_REDUCTASE_2; 1.
PS00063; ALDOKETO_REDUCTASE_3; 1.
BLOCKS P51635.
Genome annotation databases
Ensembl ENSRNOG00000016727; Rattus norvegicus. [Contig view]
GeneID 78959; -.
KEGG rno:78959; -.
Phylogenomic databases
HOVERGEN P51635; -.
Other
ProtoNet P51635.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; Glycation; Glycoprotein; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   325  324     Alcohol dehydrogenase [NADP+]. PRO_0000124620
NP_BIND   11    20  10     NADP (Potential). 
NP_BIND   211   273  63     NADP (By similarity). 
ACT_SITE   50    50        Proton donor (By similarity). 
BINDING   113   113        Substrate (By similarity). 
SITE   13    13  1     Not glycated. 
SITE   30    30  1     Not glycated. 
SITE   34    34  1     Not glycated. 
SITE   61    61  1     Not glycated. 
SITE   80    80  1     Lowers pKa of active site Tyr (By similarity). 
SITE   80    80  1     Not glycated. 
SITE   97    97  1     Not glycated. 
SITE   127   127  1     Not glycated. 
SITE   134   134  1     Not glycated. 
SITE   145   145  1     Not glycated. 
SITE   157   157  1     Not glycated. 
SITE   240   240  1     Not glycated. 
SITE   257   257  1     Not glycated. 
SITE   263   263  1     Not glycated. 
SITE   287   287  1     Not glycated. 
SITE   294   294  1     Not glycated. 
SITE   308   308  1     Not glycated. 
MOD_RES   2     2        N-acetylthreonine. 
CARBOHYD   23    23        N-linked (Glc) (glycation). 
CARBOHYD   68    68        N-linked (Glc) (glycation). 
CARBOHYD   85    85        N-linked (Glc) (glycation). 
CARBOHYD   141   141        N-linked (Glc) (glycation). 
CARBOHYD   153   153        N-linked (Glc) (glycation). 
Sequence information
Length: 325 AA [This is the length of the unprocessed precursor] Molecular weight: 36506 Da [This is the MW of the unprocessed precursor] CRC64: F95573B7411884DA [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTASSVLLHT GQKMPLIGLG TWKSEPGQVK AAIKYALSVG YRHIDCASVY GNETEIGEAL 

        70         80         90        100        110        120 
KESVGAGKAV PREELFVTSK LWNTKHHPED VEPAVRKTLA DLQLEYLDLY LMHWPYAFER 

       130        140        150        160        170        180 
GDNPFPKNAD GTVKYDSTHY KETWKALEAL VAKGLVKALG LSNFSSRQID DVLSVASVRP 

       190        200        210        220        230        240 
AVLQVECHPY LAQNELIAHC QARGLEVTAY SPLGSSDRAW RHPDEPVLLE EPVVLALAEK 

       250        260        270        280        290        300 
HGRSPAQILL RWQVQRKVIC IPKSITPSRI LQNIQVFDFT FSPEEMKQLD ALNKNWRYIV 

       310        320 
PMITVDGKRV PRDAGHPLYP FNDPY
P51635 in FASTA format

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