Reviewed, UniProtKB/Swiss-Prot Q64442 (DHSO_MOUSE)

Names and origin

Protein names

Recommended name:
    Sorbitol dehydrogenase
    EC=1.1.1.14
Alternative name(s):
    L-iditol 2-dehydrogenase

Gene names

Name:	Sord
Synonyms:	Sdh1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Oxidizes sorbitol and other polyols such as xylitol, D-mannitol, L-iditol.
Catalytic activity	L-iditol + NAD+ = L-sorbose + NADH.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Homotetramer By similarity.
Tissue specificity	Testis has the highest level of expression, followed by kidney, liver, and lung. Low levels of expression are also observed in lens, brain, and skeletal muscle.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	soluble fraction Inferred from direct assay. Source: MGI
Molecular function	L-iditol 2-dehydrogenase activity Inferred from direct assay. Source: MGI zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 357	357	Sorbitol dehydrogenase		PRO_0000000882
Sites
	Metal binding	45	1	Zinc; catalytic By similarity
	Metal binding	70	1	Zinc; catalytic By similarity
	Metal binding	71	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	169	1	Phosphoserine Ref.5 Ref.6
Experimental info
	Sequence conflict	49	1	V → L in AAA79043. Ref.1
	Sequence conflict	259	1	T → S in AAA79043. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q64442-1 [UniParc]. Last modified July 10, 2007. Version 3. Checksum: FDAA462EF1EB6C21	FASTA	357	38,249
	10 20 30 40 50 60 MAAPAKGENL SLVVHGPGDI RLENYPIPEL GPNDVLLKMH SVGICGSDVH YWEHGRIGDF 70 80 90 100 110 120 VVKKPMVLGH EAAGTVTKVG ELVKHLKPGD RVAIEPGVPR EVDEYCKIGR YNLTPTIFFC 130 140 150 160 170 180 ATPPDDGNLC RFYKHNADFC YKLPDSVTFE EGALIEPLSV GIYACRRGSV SLGNKVLVCG 190 200 210 220 230 240 AGPVGMVTLL VAKAMGAAQV VVTDLSASRL TKAKEVGADF TIQVGKETPQ EIASKVESLL 250 260 270 280 290 300 GSKPEVTIEC TGAESSVQTG IYATHSGGTL VIVGMGAEMV NLPLVHAAIR EVDIKGVFRY 310 320 330 340 350 CNTWPMAISM LASKTLNVKP LVTHRFPLEK AVEAFETAKK GVGLKVMIKC DPNDQNP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequencing, and determination of the sites of expression of mouse sorbitol dehydrogenase cDNA." Lee F.K., Lee A.Y.W., Lin C.X.F., Chung S.S.-M., Chung S.K. Eur. J. Biochem. 230:1059-1065(1995) [PubMed: 7601136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Liver.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Blastocyst, Lung and Testis.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney and Liver.
[5]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed: 18630941] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U27014 mRNA. Translation: AAA79043.1. Different initiation. AK004692 mRNA. Translation: BAB23478.1. AK015059 mRNA. Translation: BAB29695.1. AK166988 mRNA. Translation: BAE39168.1. AK166996 mRNA. Translation: BAE39175.1. AL844566, AL844573 Genomic DNA. Translation: CAM16325.1. AL844573, AL844566 Genomic DNA. Translation: CAM19389.1. BC024124 mRNA. Translation: AAH24124.1. BC030875 mRNA. Translation: AAH30875.1. BC092291 mRNA. Translation: AAH92291.1.
IPI	IPI00753038.
PIR	S65956.
RefSeq	NP_666238.1.
UniGene	Mm.371580 Mm.471786
3D structure databases
SMR	Q64442. Positions 2-357.
ModBase	Search...
Protein-protein interaction databases
STRING	Q64442.
PTM databases
PhosphoSite	Q64442.
2-D gel databases
REPRODUCTION-2DPAGE	Q64442.
Proteomic databases
PRIDE	Q64442.
Genome annotation databases
Ensembl	ENSMUST00000028657; ENSMUSP00000028657; ENSMUSG00000027227; Mus musculus. [Genome view] ENSMUST00000110551; ENSMUSP00000106180; ENSMUSG00000027227; Mus musculus. [Genome view]
GeneID	20322.
KEGG	mmu:20322.
NMPDR	fig|10090.3.peg.6788.
UCSC	uc008maj.1. mouse.
Organism-specific databases
CTD	20322.
MGI	MGI:98266. Sord.
Phylogenomic databases
eggNOG	roNOG08081.
HOGENOM	HBG753318.
HOVERGEN	Q64442.
InParanoid	Q64442.
OrthoDB	EOG9K0T6S.
Enzyme and pathway databases
BRENDA	1.1.1.14. 244.
Gene expression databases
ArrayExpress	Q64442.
Bgee	Q64442.
CleanEx	MM_SORD.
Genevestigator	Q64442.
GermOnline	ENSMUSG00000027227. Mus musculus.
Family and domain databases
InterPro	IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. IPR011032. GroES-like. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	298123.
SOURCE	Search...

Entry information

Entry name

DHSO_MOUSE

Accession

Primary (citable) accession number: Q64442
Secondary accession number(s): Q569V5, Q9CPS0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 10, 2007
Last modified:	January 19, 2010
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)