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UniProtKB/Swiss-Prot entry P80276


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

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Entry information
Entry name ALDR_PIG
Primary accession number P80276
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 71)
Name and origin of the protein
Protein name Aldose reductase
Synonyms AR
EC 1.1.1.21
Aldehyde reductase
Gene name
Name: AKR1B1
Synonyms: ALR2
From
Sus scrofa (Pig) [TaxID: 9823] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8493902 [NCBI, ExPASy, EBI, Israel, Japan]
Kubiseski T.J., Green N.C., Flynn T.G.;
"Location of an essential arginine residue in the primary structure of pig aldose reductase.";
Adv. Exp. Med. Biol. 328:259-265(1993).
[2]
PROTEIN SEQUENCE OF 2-316, MASS SPECTROMETRY, AND DISULFIDE BOND.
TISSUE=Lens;
DOI=10.1111/j.1432-1033.1993.tb18445.x; PubMed=8281941 [NCBI, ExPASy, EBI, Israel, Japan]
Jaquinod M., Potier N., Klarskov K., Reymann J.-M., Sorokine O., Kieffer S., Barth P., Andriantomanga V., Biellmann J.-F., van Dorsselaer A.;
"Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes.";
Eur. J. Biochem. 218:893-903(1993).
[3]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1038/355469a0; PubMed=1734286 [NCBI, ExPASy, EBI, Israel, Japan]
Rondeau J.-M., Tete-Favier F., Podjarny A., Reymann J.-M., Barth P., Biellmann J.-F., Moras D.;
"Novel NADPH-binding domain revealed by the crystal structure of aldose reductase.";
Nature 355:469-472(1992).
[4]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1016/S0969-2126(97)00216-5; PubMed=9195881 [NCBI, ExPASy, EBI, Israel, Japan]
Urzhumtsev A., Tete-Favier F., Mitschler A., Barbanton J., Barth P., Urzhumtseva L., Biellmann J.-F., Podjarny A.D., Moras D.;
"A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil.";
Structure 5:601-612(1997).
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
L14950; AAA30989.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U46065; AAC48515.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A59021; A59021.
RefSeq NP_001001539.1; -.
UniGene Ssc.3059
3D structure databases
PDB
1AH0; X-ray; 2.30 A; A=1-316.[ExPASy / RCSB / EBI]
1AH3; X-ray; 2.30 A; A=3-316.[ExPASy / RCSB / EBI]
1AH4; X-ray; 2.00 A; A=3-316.[ExPASy / RCSB / EBI]
1DLA; X-ray; 3.00 A; A/B/C/D=3-316.[ExPASy / RCSB / EBI]
1EKO; X-ray; 2.20 A; A=3-316.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AH0; -.
1AH3; -.
1AH4; -.
1DLA; -.
1EKO; -.
ModBase P80276.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004032; Molecular function: aldehyde reductase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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 P80276.
ProtoNet P80276.
Genome annotation databases
GeneID 396816; -.
KEGG ssc:396816; -.
Phylogenomic databases
HOVERGEN P80276; -.
Other
LinkHub P80276; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   316  315     Aldose reductase. PRO_0000124625
NP_BIND   10    19  10     NADP (Potential). 
NP_BIND   211   273  63     NADP. 
ACT_SITE   49    49        Proton donor. 
BINDING   111   111        Substrate. 
SITE   78    78  1     Lowers pKa of active site Tyr (By similarity). 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   23    23        Phosphoserine (By similarity). 
MOD_RES   40    40        Phosphotyrosine (By similarity). 
DISULFID   299   304         
CONFLICT   99    99        D -> N (in Ref. 1; AAA30989/AAC48515). 
STRAND   4     6  3      
STRAND   12    16  5      
HELIX   25    37  13      
STRAND   42    44  3      
HELIX   47    49  3      
HELIX   52    64  13      
HELIX   70    72  3      
STRAND   74    79  6      
HELIX   81    83  3      
HELIX   86    88  3      
HELIX   89   100  12      
STRAND   105   110  6      
HELIX   138   150  13      
STRAND   153   155  3      
STRAND   157   161  5      
HELIX   164   171  8      
STRAND   181   186  6      
HELIX   194   203  10      
STRAND   206   210  5      
STRAND   223   225  3      
HELIX   232   241  10      
HELIX   245   255  11      
HELIX   267   274  8      
TURN   275   278  4      
HELIX   283   291  9      
HELIX   302   304  3      
HELIX   311   313  3      
Sequence information
Length: 316 AA [This is the length of the unprocessed precursor] Molecular weight: 35868 Da [This is the MW of the unprocessed precursor] CRC64: 7218B663AC1B4E92 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASHLVLYTG AKMPILGLGT WKSPPGKVTE AVKVAIDLGY RHIDCAHVYQ NENEVGLGLQ 

        70         80         90        100        110        120 
EKLQGQVVKR EDLFIVSKLW CTDHEKNLVK GACQTTLRDL KLDYLDLYLI HWPTGFKPGK 

       130        140        150        160        170        180 
DPFPLDGDGN VVPDESDFVE TWEAMEELVD EGLVKAIGVS NFNHLQVEKI LNKPGLKYKP 

       190        200        210        220        230        240 
AVNQIEVHPY LTQEKLIEYC KSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK 

       250        260        270        280        290        300 
YNKTTAQVLI RFPMQRNLIV IPKSVTPERI AENFQVFDFE LSPEDMNTLL SYNRNWRVCA 

       310 
LMSCASHKDY PFHEEY 

P80276 in FASTA format

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