ID AK1A1_RAT Reviewed; 325 AA. AC P51635; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 16-JUN-2009, entry version 62. DE RecName: Full=Alcohol dehydrogenase [NADP+]; DE EC=1.1.1.2; DE AltName: Full=Aldehyde reductase; DE AltName: Full=Aldo-keto reductase family 1 member A1; DE AltName: Full=3-DG-reducing enzyme; GN Name=Akr1a1; Synonyms=Alr; 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 [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Kidney, and Liver; RX MEDLINE=93273240; PubMed=8500767; DOI=10.1016/0378-1119(93)90728-L; RA Takahashi M., Fujii J., Teshima T., Suzuki K., Shiba T., Taniguchi N.; RT "Identity of a major 3-deoxyglucosone-reducing enzyme with aldehyde RT reductase in rat liver established by amino acid sequencing and cDNA RT expression."; RL Gene 127:249-253(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pituitary; 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 [3] RP PROTEIN SEQUENCE OF 14-30; 62-77; 81-97; 135-145 AND 146-157, RP GLYCATION AT LYS-23; LYS-68; LYS-85; LYS-141 AND LYS-153, AND ABSENCE RP OF GLYCATION AT LYS-13; LYS-30; LYS-34; LYS-61; LYS-80; LYS-97; RP LYS-127; LYS-134; LYS-145; LYS-157; LYS-240; LYS-257; LYS-263; RP LYS-287; LYS-294 AND LYS-308. RX PubMed=7827091; DOI=10.1021/bi00004a038; RA Takahashi M., Lu Y.B., Myint T., Fujii J., Wada Y., Taniguchi N.; RT "In vivo glycation of aldehyde reductase, a major 3-deoxyglucosone RT reducing enzyme: identification of glycation sites."; RL Biochemistry 34:1433-1438(1995). RN [4] RP PROTEIN SEQUENCE OF 204-218; 222-240; 270-287 AND 313-325, AND MASS RP SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord; RA Lubec G., Afjehi-Sadat L.; RL Submitted (NOV-2006) to UniProtKB. RN [5] RP ACETYLATION AT THR-2, AND MASS SPECTROMETRY. RA Lubec G., Chen W.-Q.; RL Submitted (FEB-2007) to UniProtKB. CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 3- CC deoxyglucosone (3-DG). CC -!- CATALYTIC ACTIVITY: An alcohol + NADP(+) = an aldehyde + NADPH. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D10854; BAA01627.1; -; mRNA. DR EMBL; BC059133; AAH59133.1; -; mRNA. DR IPI; IPI00230859; -. DR PIR; JN0629; JN0629. DR RefSeq; NP_112262.1; -. DR UniGene; Rn.835; -. DR HSSP; P14550; 2ALR. DR SMR; P51635; 3-325. DR PRIDE; P51635; -. DR Ensembl; ENSRNOG00000016727; Rattus norvegicus. DR GeneID; 78959; -. DR KEGG; rno:78959; -. DR RGD; 68346; Akr1a1. DR HOVERGEN; P51635; -. DR OMA; P51635; WRHPDEP. DR BRENDA; 1.1.1.2; 248. DR NextBio; 614380; -. DR ArrayExpress; P51635; -. DR GermOnline; ENSRNOG00000016727; Rattus norvegicus. DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001395; Aldo/ket_red. DR InterPro; IPR018170; Aldo/ket_reductase_CS. 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 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; Direct protein sequencing; Glycation; Glycoprotein; NADP; KW Oxidoreductase. FT INIT_MET 1 1 Removed. FT CHAIN 2 325 Alcohol dehydrogenase [NADP+]. FT /FTId=PRO_0000124620. FT NP_BIND 11 20 NADP (Potential). FT NP_BIND 211 273 NADP (By similarity). FT ACT_SITE 50 50 Proton donor (By similarity). FT BINDING 113 113 Substrate (By similarity). FT SITE 13 13 Not glycated. FT SITE 30 30 Not glycated. FT SITE 34 34 Not glycated. FT SITE 61 61 Not glycated. FT SITE 80 80 Lowers pKa of active site Tyr (By FT similarity). FT SITE 80 80 Not glycated. FT SITE 97 97 Not glycated. FT SITE 127 127 Not glycated. FT SITE 134 134 Not glycated. FT SITE 145 145 Not glycated. FT SITE 157 157 Not glycated. FT SITE 240 240 Not glycated. FT SITE 257 257 Not glycated. FT SITE 263 263 Not glycated. FT SITE 287 287 Not glycated. FT SITE 294 294 Not glycated. FT SITE 308 308 Not glycated. FT MOD_RES 2 2 N-acetylthreonine. FT CARBOHYD 23 23 N-linked (Glc) (glycation). FT CARBOHYD 68 68 N-linked (Glc) (glycation). FT CARBOHYD 85 85 N-linked (Glc) (glycation). FT CARBOHYD 141 141 N-linked (Glc) (glycation). FT CARBOHYD 153 153 N-linked (Glc) (glycation). SQ SEQUENCE 325 AA; 36506 MW; F95573B7411884DA CRC64; MTASSVLLHT GQKMPLIGLG TWKSEPGQVK AAIKYALSVG YRHIDCASVY GNETEIGEAL KESVGAGKAV PREELFVTSK LWNTKHHPED VEPAVRKTLA DLQLEYLDLY LMHWPYAFER GDNPFPKNAD GTVKYDSTHY KETWKALEAL VAKGLVKALG LSNFSSRQID DVLSVASVRP AVLQVECHPY LAQNELIAHC QARGLEVTAY SPLGSSDRAW RHPDEPVLLE EPVVLALAEK HGRSPAQILL RWQVQRKVIC IPKSITPSRI LQNIQVFDFT FSPEEMKQLD ALNKNWRYIV PMITVDGKRV PRDAGHPLYP FNDPY //