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UniProtKB/Swiss-Prot entry P14550


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

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Entry information
Entry name AK1A1_HUMAN
Primary accession number P14550
Secondary accession numbers None
Integrated into Swiss-Prot on January 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 93)
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
Gene name
Name: AKR1A1
Synonyms: ALDR1, ALR
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=2498333 [NCBI, ExPASy, EBI, Israel, Japan]
Bohren K.M., Bullock B., Wermuth B., Gabbay K.H.;
"The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases.";
J. Biol. Chem. 264:9547-9551(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10393438 [NCBI, ExPASy, EBI, Israel, Japan]
Fujii J., Hamaoka R., Matsumoto A., Fujii T., Yamaguchi Y., Egashira M., Miyoshi O., Niikawa N., Taniguchi N.;
"The structural organization of the human aldehyde reductase gene, AKR1A1, and mapping to chromosome 1p33-->p32.";
Cytogenet. Cell Genet. 84:230-232(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/geno.1999.5915; PubMed=10486210 [NCBI, ExPASy, EBI, Israel, Japan]
Barski O.A., Gabbay K.H., Bohren K.M.;
"Characterization of the human aldehyde reductase gene and promoter.";
Genomics 60:188-198(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, and Kidney;
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).
[6]
PROTEIN SEQUENCE OF 2-325.
TISSUE=Liver;
PubMed=3615425 [NCBI, ExPASy, EBI, Israel, Japan]
Wermuth B., Omar A., Forster A., di Francesco C., Wolf M., von Wartburg J.-P., Bullock B., Gabbay K.H.;
"Primary structure of aldehyde reductase from human liver.";
Prog. Clin. Biol. Res. 232:297-307(1987).
[7]
MUTAGENESIS OF TYR-50; LYS-80; HIS-113; ILE-299 AND VAL-300.
DOI=10.1021/bi00035a036; PubMed=7669785 [NCBI, ExPASy, EBI, Israel, Japan]
Barski O.A., Gabbay K.H., Grimshaw C.E., Bohren K.M.;
"Mechanism of human aldehyde reductase: characterization of the active site pocket.";
Biochemistry 34:11264-11275(1995).
[8]
X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS).
DOI=10.1107/S0907444994005275; PubMed=15299353 [NCBI, ExPASy, EBI, Israel, Japan]
El-Kabbani O., Green N.C., Lin G., Carson M., Narayana S.V.L., Moore K.M., Flynn T.G., DeLucas L.J.;
"Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications.";
Acta Crystallogr. D 50:859-868(1994).
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
J04794; AAA51711.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF036683; AAB92369.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF036680; AAB92369.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF036681; AAB92369.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF036682; AAB92369.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF112485; AAF01260.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF112484; AAF01260.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007003; AAP35649.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000670; AAH00670.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005394; AAH05394.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A33851; A33851.
RefSeq NP_006057.1; -.
NP_697021.1; -.
UniGene Hs.654435
3D structure databases
PDB
2ALR; X-ray; 2.48 A; A=1-325.[ExPASy / RCSB / EBI]
PDBsum 2ALR; -.
ModBase P14550.
Protein-protein interaction databases
IntAct P14550; -.
PTM databases
PhosphoSite P14550; -.
2D gel databases
SWISS-2DPAGE P14550; -.
REPRODUCTION-2DPAGE IPI00220271; -.
P14550; -.
Organism-specific databases
H-InvDB HIX0000534; -.
HGNC HGNC:380; AKR1A1.
GenAtlas AKR1A1.
HPA CAB006246; -.
HPA017919; -.
MIM 103830; gene. [NCBI / EBI]
PharmGKB PA24674; -.
GeneCards P14550.
Gene expression databases
ArrayExpress P14550; -.
CleanEx HS_AKR1A1; -.
GermOnline ENSG00000117448; Homo sapiens.
Ontologies
GO
GO:0004032; Molecular function: aldehyde reductase activity (traceable author statement from ProtInc).
GO:0009055; Molecular function: electron carrier activity (traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006081; Biological process: cellular aldehyde metabolic process (traceable author statement from ProtInc).
GO:0006006; Biological process: glucose metabolic process (traceable author statement from ProtInc).
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 P14550.
ProtoNet P14550.
Proteomic databases
PeptideAtlas P14550; -.
Genome annotation databases
Ensembl ENSG00000117448; Homo sapiens. [Contig view]
GeneID 10327; -.
KEGG hsa:10327; -.
Phylogenomic databases
HOGENOM P14550; -.
HOVERGEN P14550; -.
Other
LinkHub P14550; -.
NextBio 39151; -.
SOURCE AKR1A1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Direct protein sequencing; 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_0000124617
NP_BIND   211   273  63     NADP (By similarity). 
ACT_SITE   50    50        Proton donor. 
BINDING   113   113        Substrate. 
SITE   80    80  1     Lowers pKa of active site Tyr. 
MOD_RES   2     2        N-acetylalanine. 
MUTAGEN   50    50        Y->F: Complete loss of enzymatic activity. 
MUTAGEN   50    50        Y->H: Complete loss of enzymatic activity. 
MUTAGEN   80    80        K->M: Complete loss of enzymatic activity. 
MUTAGEN   113   113        H->Q: Strong decrease in enzymatic activity. 
MUTAGEN   299   299        I->A: No change in enzymatic activity. 
MUTAGEN   299   299        I->C: No change in enzymatic activity. 
MUTAGEN   300   300        V->C: No change in enzymatic activity. 
STRAND   5     7  3      
STRAND   13    17  5      
HELIX   26    39  14      
STRAND   43    45  3      
HELIX   48    50  3      
HELIX   53    63  11      
STRAND   68    70  3      
HELIX   72    74  3      
STRAND   76    81  6      
HELIX   83    85  3      
HELIX   88   102  15      
STRAND   107   113  7      
STRAND   115   118  4      
STRAND   120   122  3      
HELIX   140   153  14      
STRAND   155   163  9      
HELIX   166   173  8      
STRAND   182   186  5      
HELIX   194   203  10      
STRAND   206   210  5      
HELIX   232   241  10      
HELIX   245   255  11      
HELIX   267   274  8      
HELIX   283   290  8      
STRAND   302   305  4      
STRAND   308   313  6      
STRAND   320   323  4      
Sequence information
Length: 325 AA [This is the length of the unprocessed precursor] Molecular weight: 36573 Da [This is the MW of the unprocessed precursor] CRC64: F6B27517EB754E37 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAASCVLLHT GQKMPLIGLG TWKSEPGQVK AAVKYALSVG YRHIDCAAIY GNEPEIGEAL 

        70         80         90        100        110        120 
KEDVGPGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA DLQLEYLDLY LMHWPYAFER 

       130        140        150        160        170        180 
GDNPFPKNAD GTICYDSTHY KETWKALEAL VAKGLVQALG LSNFNSRQID DILSVASVRP 

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

       250        260        270        280        290        300 
YGRSPAQILL RWQVQRKVIC IPKSITPSRI LQNIKVFDFT FSPEEMKQLN ALNKNWRYIV 

       310        320 
PMLTVDGKRV PRDAGHPLYP FNDPY 

P14550 in FASTA format

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