ID   ALDR_RAT                Reviewed;         316 AA.
AC   P07943;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   04-NOV-2008, entry version 75.
DE   RecName: Full=Aldose reductase;
DE            Short=AR;
DE            EC=1.1.1.21;
DE   AltName: Full=Aldehyde reductase;
GN   Name=Akr1b1; Synonyms=Akr1b4, Aldr1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Sprague-Dawley; TISSUE=Lens;
RX   MEDLINE=87276556; PubMed=3111886; DOI=10.1016/0014-5793(87)80905-5;
RA   Carper D., Nishimura C., Shinohara T., Dietzchold B., Wistow G.,
RA   Craft C., Kador P., Kinoshita J.H.;
RT   "Aldose reductase and p-crystallin belong to the same protein
RT   superfamily as aldehyde reductase.";
RL   FEBS Lett. 220:209-213(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92084118; PubMed=1748296; DOI=10.1016/0378-1119(91)90326-7;
RA   Graham C.E., Szpirer C., Levan G., Carper D.;
RT   "Characterization of the aldose reductase-encoding gene family in
RT   rat.";
RL   Gene 107:259-267(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 42-53; 156-169; 178-195; 276-294 AND 307-316, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (NOV-2006) to UniProtKB.
RN   [5]
RP   PROTEIN SEQUENCE OF 156-169 AND 205-210.
RC   TISSUE=Astrocyte;
RX   MEDLINE=96007949; PubMed=7498172; DOI=10.1002/elps.11501601205;
RA   Laeng P., Bouillon P., Taupenot L., Labourdette G.;
RT   "Long-term induction of an aldose reductase protein by basic
RT   fibroblast growth factor in rat astrocytes in vitro.";
RL   Electrophoresis 16:1240-1250(1995).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of a wide
CC       variety of carbonyl-containing compounds to their corresponding
CC       alcohols with a broad range of catalytic efficiencies.
CC   -!- CATALYTIC ACTIVITY: Alditol + NAD(P)(+) = aldose + NAD(P)H.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family.
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DR   EMBL; X05884; CAA29308.1; -; mRNA.
DR   EMBL; M60322; AAA40721.1; -; Genomic_DNA.
DR   EMBL; BC062034; AAH62034.1; -; mRNA.
DR   PIR; A60603; A60603.
DR   RefSeq; NP_036630.1; -.
DR   UniGene; Rn.107801; -.
DR   HSSP; P15121; 2ACQ.
DR   SMR; P07943; 1-315.
DR   Ensembl; ENSRNOG00000009513; Rattus norvegicus.
DR   GeneID; 24192; -.
DR   KEGG; rno:24192; -.
DR   RGD; 2092; Akr1b1.
DR   HOVERGEN; P07943; -.
DR   NextBio; 602571; -.
DR   ArrayExpress; P07943; -.
DR   GermOnline; ENSRNOG00000009513; Rattus norvegicus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004032; F:aldehyde reductase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001395; Aldo/ket_red.
DR   Gene3D; G3DSA:3.20.20.100; Aldo/ket_red; 1.
DR   PANTHER; PTHR11732; Aldo/ket_red; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   ProDom; PD000288; Aldo/ket_red; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; NADP;
KW   Oxidoreductase; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    316       Aldose reductase.
FT                                /FTId=PRO_0000124627.
FT   NP_BIND      10     19       NADP (Potential).
FT   NP_BIND     211    273       NADP (By similarity).
FT   ACT_SITE     49     49       Proton donor (By similarity).
FT   BINDING     111    111       Substrate (By similarity).
FT   SITE         78     78       Lowers pKa of active site Tyr (By
FT                                similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      23     23       Phosphoserine (By similarity).
FT   MOD_RES      40     40       Phosphotyrosine (By similarity).
SQ   SEQUENCE   316 AA;  35797 MW;  D6D07843B6850002 CRC64;
     MASHLELNNG TKMPTLGLGT WKSPPGQVTE AVKVAIDMGY RHIDCAQVYQ NEKEVGVALQ
     EKLKEQVVKR QDLFIVSKLW CTFHDQSMVK GACQKTLSDL QLDYLDLYLI HWPTGFKPGP
     DYFPLDASGN VIPSDTDFVD TWTAMEQLVD EGLVKAIGVS NFNPLQIERI LNKPGLKYKP
     AVNQIECHPY LTQEKLIEYC HCKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKEIAAK
     YNKTTAQVLI RFPIQRNLVV IPKSVTPARI AENFKVFDFE LSNEDMATLL SYNRNWRVCA
     LMSCAKHKDY PFHAEV
//