[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1006/geno.1994.1276; PubMed=8088829 [NCBI, ExPASy, EBI, Israel, Japan] Lee F.K., Cheung M.C., Chung S.; "The human sorbitol dehydrogenase gene: cDNA cloning, sequence determination, and mapping by fluorescence in situ hybridization."; Genomics 21:354-358(1994).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. DOI=10.1016/0888-7543(95)80082-W; PubMed=7782086 [NCBI, ExPASy, EBI, Israel, Japan] Iwata T., Popescu N.C., Zimonjic D.B., Karlsson C., Hoeoeg J.-O., Vaca G., Rodriguez I.R., Carper D.; "Structural organization of the human sorbitol dehydrogenase gene (SORD)."; Genomics 26:55-62(1995).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=9183016 [NCBI, ExPASy, EBI, Israel, Japan] Carr I.M., Markham A.F., Coletta P.L.; "Identification and characterisation of a sequence related to human sorbitol dehydrogenase."; Eur. J. Biochem. 245:760-767(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-239. TISSUE=Brain, and Lymph; 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).
[5]	PROTEIN SEQUENCE OF 2-357. TISSUE=Liver; PubMed=2691249 [NCBI, ExPASy, EBI, Israel, Japan] Karlsson C., Maret W., Auld D.S., Hoeoeg J.-O., Joernvall H.; "Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzyme."; Eur. J. Biochem. 186:543-550(1989).
[6]	PROTEIN SEQUENCE OF 2-21. TISSUE=Platelet; DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan] Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.; "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."; Nat. Biotechnol. 21:566-569(2003).
[7]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). DOI=10.1016/S0969-2126(03)00167-9; PubMed=12962626 [NCBI, ExPASy, EBI, Israel, Japan] Pauly T.A., Ekstrom J.L., Beebe D.A., Chrunyk B., Cunningham D., Griffor M., Kamath A., Lee S.E., Madura R., Mcguire D., Subashi T., Wasilko D., Watts P., Mylari B.L., Oates P.J., Adams P.D., Rath V.L.; "X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase."; Structure 11:1071-1085(2003).

Comments

CATALYTIC ACTIVITY: L-iditol + NAD⁺ = L-sorbose + NADH.
COFACTOR: Binds 1 zinc ion per subunit.
SUBUNIT: Homotetramer.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.

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

U07361; AAA66064.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L29008; AAA80565.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L29254; AAA80566.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L29249; AAA80566.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L29250; AAA80566.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L29251; AAA80566.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L29252; AAA80566.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L29253; AAA80566.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U67243; AAB61898.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U67236; AAB61898.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U67237; AAB61898.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U67238; AAB61898.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U67239; AAB61898.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U67240; AAB61898.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U67241; AAB61898.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U67242; AAB61898.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021085; AAH21085.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC025295; AAH25295.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A54674; A54674.

NP_003095.2; -.

3D structure databases

PDB

1PL6; X-ray; 2.00 A; A/B/C/D=1-357.	[ExPASy / RCSB / EBI]
1PL7; X-ray; 2.20 A; A/B/C/D=1-357.	[ExPASy / RCSB / EBI]
1PL8; X-ray; 1.90 A; A/B/C/D=1-357.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1PL6; -.
1PL7; -.
1PL8; -.

ModBase

Q00796.

Protein-protein interaction databases

IntAct

Q00796; -.

PTM databases

PhosphoSite

Q00796; -.

2D gel databases

REPRODUCTION-2DPAGE

IPI00216057; -.

Organism-specific databases

HIX0012204; -.

HGNC:11184; SORD.

182500; gene. [NCBI / EBI]

PharmGKB

PA36021; -.

GeneCards

Q00796.

Gene expression databases

ArrayExpress

Q00796; -.

CleanEx

HS_SORD; -.

GermOnline

ENSG00000140263; Homo sapiens.

Ontologies

GO:0005615;	Cellular component: extracellular space (traceable author statement from UniProtKB).
GO:0005624;	Cellular component: membrane fraction (inferred from direct assay from UniProtKB).
GO:0005625;	Cellular component: soluble fraction (inferred from direct assay from UniProtKB).
GO:0003939;	Molecular function: L-iditol 2-dehydrogenase activity (inferred from direct assay from UniProtKB).
GO:0051287;	Molecular function: NAD binding (inferred from direct assay from UniProtKB).
GO:0005529;	Molecular function: sugar binding (non-traceable author statement from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (inferred from direct assay from UniProtKB).
GO:0046370;	Biological process: fructose biosynthetic process (inferred from direct assay from UniProtKB).
GO:0006006;	Biological process: glucose metabolic process (traceable author statement from UniProtKB).
GO:0051160;	Biological process: L-xylitol catabolic process (inferred from direct assay from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
GO:0006062;	Biological process: sorbitol catabolic process (inferred from direct assay from UniProtKB).
GO:0030317;	Biological process: sperm motility (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00059; ADH_ZINC; 1.

ProtoNet

Q00796.

Genome annotation databases

Ensembl

ENSG00000140263; Homo sapiens. [Contig view]

GeneID

6652; -.

KEGG

hsa:6652; -.

Phylogenomic databases

HOGENOM

Q00796; -.

HOVERGEN

Q00796; -.

Other

DB00157; NADH.

Q00796; -.

25929; -.

SORD; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Polymorphism; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 357`	`356`	`Sorbitol dehydrogenase.`	`PRO_0000160817`
`METAL`	`45 45`		`Zinc; catalytic.`
`METAL`	`70 70`		`Zinc; catalytic.`
`METAL`	`71 71`		`Zinc; catalytic.`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`VARIANT`	`239 239`	`1`	`L -> Q.`	`VAR_000430 [3D]`
`CONFLICT`	`5 5`		`Missing (in Ref. 5; AA sequence).`
`CONFLICT`	`59 59`		`N -> D (in Ref. 5; AA sequence).`
`CONFLICT`	`186 186`		`M -> E (in Ref. 5; AA sequence).`
`CONFLICT`	`281 281`		`T -> S (in Ref. 5; AA sequence).`
`CONFLICT`	`289 289`		`I -> T (in Ref. 5; AA sequence).`
`STRAND`	`10 16`	`7`
`STRAND`	`19 24`	`6`
`STRAND`	`34 43`	`10`
`HELIX`	`46 54`	`9`
`STRAND`	`55 57`	`3`
`STRAND`	`71 79`	`9`
`STRAND`	`91 94`	`4`
`STRAND`	`96 98`	`3`
`HELIX`	`104 107`	`4`
`HELIX`	`111 113`	`3`
`STRAND`	`130 136`	`7`
`HELIX`	`137 139`	`3`
`STRAND`	`140 142`	`3`
`HELIX`	`149 168`	`20`
`STRAND`	`175 179`	`5`
`HELIX`	`183 194`	`12`
`STRAND`	`198 205`	`8`
`HELIX`	`207 215`	`9`
`STRAND`	`219 223`	`5`
`HELIX`	`229 240`	`12`
`STRAND`	`245 249`	`5`
`HELIX`	`254 263`	`10`
`STRAND`	`269 272`	`4`
`STRAND`	`278 282`	`5`
`HELIX`	`284 288`	`5`
`TURN`	`289 291`	`3`
`STRAND`	`293 296`	`4`
`HELIX`	`304 312`	`9`
`HELIX`	`319 321`	`3`
`STRAND`	`322 327`	`6`
`HELIX`	`328 330`	`3`
`HELIX`	`331 339`	`9`
`STRAND`	`343 349`	`7`

Sequence information

Length: 357 AA [This is the length of the unprocessed precursor]

Molecular weight: 38297 Da [This is the MW of the unprocessed precursor]

CRC64: 99A9C6744CFFC4C6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAAAKPNNL SLVVHGPGDL RLENYPIPEP GPNEVLLRMH SVGICGSDVH YWEYGRIGNF 

        70         80         90        100        110        120 
IVKKPMVLGH EASGTVEKVG SSVKHLKPGD RVAIEPGAPR ENDEFCKMGR YNLSPSIFFC 

       130        140        150        160        170        180 
ATPPDDGNLC RFYKHNAAFC YKLPDNVTFE EGALIEPLSV GIHACRRGGV TLGHKVLVCG 

       190        200        210        220        230        240 
AGPIGMVTLL VAKAMGAAQV VVTDLSATRL SKAKEIGADL VLQISKESPQ EIARKVEGLL 

       250        260        270        280        290        300 
GCKPEVTIEC TGAEASIQAG IYATRSGGTL VLVGLGSEMT TVPLLHAAIR EVDIKGVFRY 

       310        320        330        340        350 
CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC DPSDQNP

Q00796 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools