ID DHSO_RAT Reviewed; 357 AA. AC P27867; A2VCV9; Q4FZY4; Q5I0F3; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 4. DT 25-NOV-2008, entry version 89. DE RecName: Full=Sorbitol dehydrogenase; DE EC=1.1.1.14; DE AltName: Full=L-iditol 2-dehydrogenase; GN Name=Sord; Synonyms=Sdh1; 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]. RC TISSUE=Liver; RX MEDLINE=91266961; PubMed=2050152; RA Karlsson C., Joernvall H., Heoeog J.O.; RT "Sorbitol dehydrogenase: cDNA coding for the rat enzyme. Variations RT within the alcohol dehydrogenase family independent of quaternary RT structure and metal content."; RL Eur. J. Biochem. 198:761-765(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Testis; RX MEDLINE=94039079; PubMed=8223590; RA Wen Y., Bekhor I.; RT "Sorbitol dehydrogenase. Full-length cDNA sequencing reveals a mRNA RT coding for a protein containing an additional 42 amino acids at the N- RT terminal end."; RL Eur. J. Biochem. 217:83-87(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryonic liver, Liver, and Testis; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND MASS RP SPECTROMETRY. RC TISSUE=Liver; RX PubMed=16396499; DOI=10.1021/pr0503073; RA Moser K., White F.M.; RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC- RT MS/MS."; RL J. Proteome Res. 5:98-104(2006). CC -!- CATALYTIC ACTIVITY: L-iditol + NAD(+) = L-sorbose + NADH. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. CC -!- CAUTION: PubMed:8223590 reports a cDNA predicted to encode a CC protein with an extended N-terminus but there is no further CC evidence for the existence of such a protein. 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; X59037; CAA41761.1; -; mRNA. DR EMBL; X74593; CAA52670.1; ALT_INIT; mRNA. DR EMBL; BC088398; AAH88398.2; -; mRNA. DR EMBL; BC098919; AAH98919.2; -; mRNA. DR EMBL; BC128707; AAI28708.2; -; mRNA. DR PIR; S38363; S16132. DR RefSeq; NP_058748.2; -. DR UniGene; Rn.11334; -. DR HSSP; O96496; 1E3J. DR SMR; P27867; 44-399. DR PhosphoSite; P27867; -. DR Ensembl; ENSRNOG00000017291; Rattus norvegicus. DR GeneID; 24788; -. DR KEGG; rno:24788; -. DR NMPDR; fig|10116.3.peg.19584; -. DR RGD; 3734; Sord. DR HOVERGEN; P27867; -. DR NextBio; 604416; -. DR GermOnline; ENSRNOG00000017291; Rattus norvegicus. DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:InterPro. DR InterPro; IPR013154; AlcDHase_GroES-like. DR InterPro; IPR002085; AlcDHase_SF_Zn. DR InterPro; IPR013149; AlcDHase_Zn-bd. DR InterPro; IPR002328; AlcDHase_Zn_CS. DR PANTHER; PTHR11695; ADH_Sf_Zn; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR ProDom; PD040557; GroES_related; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 1: Evidence at protein level; KW Acetylation; Metal-binding; NAD; Oxidoreductase; Phosphoprotein; Zinc. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 357 Sorbitol dehydrogenase. FT /FTId=PRO_0000000884. FT METAL 45 45 Zinc; catalytic (By similarity). FT METAL 70 70 Zinc; catalytic (By similarity). FT METAL 71 71 Zinc; catalytic (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 169 169 Phosphoserine. FT CONFLICT 259 259 T -> D (in Ref. 1; CAA41761). SQ SEQUENCE 357 AA; 38235 MW; E6F535775EF73D36 CRC64; MAAPAKGENL SLVVHGPGDI RLENYPIPEL GPNDVLLKMH SVGICGSDVH YWEHGRIGDF VVKKPMVLGH EAAGTVTKVG PMVKHLKPGD RVAIEPGVPR EIDEFCKIGR YNLTPSIFFC ATPPDDGNLC RFYKHSADFC YKLPDSVTFE EGALIEPLSV GIYACRRGSV SLGNKVLVCG AGPIGIVTLL VAKAMGASQV VVIDLSASRL AKAKEVGADF TIQVAKETPH DIAKKVESVL GSKPEVTIEC TGAESSVQTG IYATHSGGTL VVVGMGPEMI NLPLVHAAVR EVDIKGVFRY CNTWPMAVSM LASKTLNVKP LVTHRFPLEK AVEAFETAKK GLGLKVMIKC DPNDQNP //