[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; PubMed=2050152 [NCBI, ExPASy, EBI, Israel, Japan] Karlsson C., Joernvall H., Heoeog J.O.; "Sorbitol dehydrogenase: cDNA coding for the rat enzyme. Variations within the alcohol dehydrogenase family independent of quaternary structure and metal content."; Eur. J. Biochem. 198:761-765(1991).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Testis; PubMed=8223590 [NCBI, ExPASy, EBI, Israel, Japan] Wen Y., Bekhor I.; "Sorbitol dehydrogenase. Full-length cDNA sequencing reveals a mRNA coding for a protein containing an additional 42 amino acids at the N-terminal end."; Eur. J. Biochem. 217:83-87(1993).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Embryonic liver, Liver, and Testis; 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).
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr0503073; PubMed=16396499 [NCBI, ExPASy, EBI, Israel, Japan] Moser K., White F.M.; "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."; J. Proteome Res. 5:98-104(2006).

Comments

CATALYTIC ACTIVITY: L-iditol + NAD⁺ = L-sorbose + NADH.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
SUBUNIT: Homotetramer.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.
CAUTION: PubMed:8223590 reports a cDNA predicted to encode a protein with an extended N-terminus but there is no further evidence for the existence of such a protein.

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

X59037; CAA41761.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X74593; CAA52670.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC088398; AAH88398.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC098919; AAH98919.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC128707; AAI28708.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S38363; S16132.

NP_058748.2; -.

3D structure databases

HSSP

O96496; 1E3J. [HSSP ENTRY / PDB]

P27867; 44-399.

PTM databases

P27867; -.

Organism-specific databases

RGD

3734; Sord.

Gene expression databases

GermOnline

ENSRNOG00000017291; Rattus norvegicus.

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.

ProDom

PD040557; GroES_related; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00059; ADH_ZINC; 1.

BLOCKS

P27867.

Genome annotation databases

Ensembl

ENSRNOG00000017291; Rattus norvegicus. [Contig view]

GeneID

24788; -.

KEGG

rno:24788; -.

NMPDR

fig|10116.3.peg.19584; -.

Phylogenomic databases

HOVERGEN

P27867; -.

Other

ProtoNet

P27867.

UniRef

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

Keywords

Acetylation; Metal-binding; NAD; Oxidoreductase; Phosphoprotein; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 357`	`356`	`Sorbitol dehydrogenase.`	`PRO_0000000884`
`METAL`	`45 45`		`Zinc; catalytic (By similarity).`
`METAL`	`70 70`		`Zinc; catalytic (By similarity).`
`METAL`	`71 71`		`Zinc; catalytic (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`MOD_RES`	`169 169`		`Phosphoserine.`
`CONFLICT`	`259 259`		`T -> D (in Ref. 1; CAA41761).`

Sequence information

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

Molecular weight: 38235 Da [This is the MW of the unprocessed precursor]

CRC64: E6F535775EF73D36 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAPAKGENL SLVVHGPGDI RLENYPIPEL GPNDVLLKMH SVGICGSDVH YWEHGRIGDF 

        70         80         90        100        110        120 
VVKKPMVLGH EAAGTVTKVG PMVKHLKPGD RVAIEPGVPR EIDEFCKIGR YNLTPSIFFC 

       130        140        150        160        170        180 
ATPPDDGNLC RFYKHSADFC YKLPDSVTFE EGALIEPLSV GIYACRRGSV SLGNKVLVCG 

       190        200        210        220        230        240 
AGPIGIVTLL VAKAMGASQV VVIDLSASRL AKAKEVGADF TIQVAKETPH DIAKKVESVL 

       250        260        270        280        290        300 
GSKPEVTIEC TGAESSVQTG IYATHSGGTL VVVGMGPEMI NLPLVHAAVR EVDIKGVFRY 

       310        320        330        340        350 
CNTWPMAVSM LASKTLNVKP LVTHRFPLEK AVEAFETAKK GLGLKVMIKC DPNDQNP

P27867 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