Sorbitol dehydrogenase - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q00796 (DHSO_HUMAN)

Last modified November 25, 2008. Version 97. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	L-iditol + NAD(+) = L-sorbose + NADH.
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.

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Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	L-xylitol catabolic process Inferred from direct assay. Source: UniProtKB fructose biosynthetic process Inferred from direct assay. Source: UniProtKB glucose metabolic process Traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: InterPro sorbitol catabolic process Ref.7 Inferred from direct assay. Source: UniProtKB sperm motility Non-traceable author statement. Source: UniProtKB
Cellular component	extracellular space Traceable author statement. Source: UniProtKB membrane fraction Inferred from direct assay. Source: UniProtKB soluble fraction Inferred from direct assay. Source: UniProtKB
Molecular function	L-iditol 2-dehydrogenase activity Inferred from direct assay. Source: UniProtKB NAD binding Ref.7 Inferred from direct assay. Source: UniProtKB sugar binding Ref.7 Non-traceable author statement. Source: UniProtKB zinc ion binding Ref.7 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 357

356

Sorbitol dehydrogenase

PRO_0000160817

Sites

Metal binding

Zinc; catalytic

Metal binding

Zinc; catalytic

Metal binding

Zinc; catalytic

Amino acid modifications

Modified residue

N-acetylalanine

Natural variations

Natural variant

239

L → Q

VAR_000430

Experimental info

Sequence conflict

Missing AA sequence Ref.5

Sequence conflict

N → D AA sequence Ref.5

Sequence conflict

186

M → E AA sequence Ref.5

Sequence conflict

281

T → S AA sequence Ref.5

Sequence conflict

289

I → T AA sequence Ref.5

Secondary structure

357

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q00796-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 99A9C6744CFFC4C6
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FASTA

357

38,297

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human sorbitol dehydrogenase gene: cDNA cloning, sequence determination, and mapping by fluorescence in situ hybridization." Lee F.K., Cheung M.C., Chung S. Genomics 21:354-358(1994) [PubMed: 8088829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Structural organization of the human sorbitol dehydrogenase gene (SORD)." Iwata T., Popescu N.C., Zimonjic D.B., Karlsson C., Hoeoeg J.-O., Vaca G., Rodriguez I.R., Carper D. Genomics 26:55-62(1995) [PubMed: 7782086] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]	"Identification and characterisation of a sequence related to human sorbitol dehydrogenase." Carr I.M., Markham A.F., Coletta P.L. Eur. J. Biochem. 245:760-767(1997) [PubMed: 9183016] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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], VARIANT GLN-239. Tissue: Brain and Lymph.
[5]	"Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzyme." Karlsson C., Maret W., Auld D.S., Hoeoeg J.-O., Joernvall H. Eur. J. Biochem. 186:543-550(1989) [PubMed: 2691249] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-357. Tissue: Liver.
[6]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21. Tissue: Platelet.
[7]	"X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase." 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. Structure 11:1071-1085(2003) [PubMed: 12962626] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

U07361 mRNA. Translation: AAA66064.1.
L29008 mRNA. Translation: AAA80565.1.
L29254

L29253 Genomic DNA. Translation: AAA80566.1.
U67243

U67242 Genomic DNA. Translation: AAB61898.1.
BC021085 mRNA. Translation: AAH21085.1.
BC025295 mRNA. Translation: AAH25295.1.

PIR

A54674.

RefSeq

NP_003095.2.

UniGene

Hs.878

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PL6	X-ray	2.00	A/B/C/D	1-357	[»]
1PL7	X-ray	2.20	A/B/C/D	1-357	[»]
1PL8	X-ray	1.90	A/B/C/D	1-357	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q00796.

PTM databases

PhosphoSite

Q00796.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00216057.

Genome annotation databases

Ensembl

ENSG00000140263. Homo sapiens. [Contig view]

GeneID

6652.

KEGG

hsa:6652.

Organism-specific databases

H-InvDB

HIX0012204.

HGNC

HGNC:11184. SORD.

MIM

182500. gene.

PharmGKB

PA36021.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

Q00796.

HOVERGEN

Q00796.

Gene expression databases

ArrayExpress

Q00796.

CleanEx

HS_SORD.

GermOnline

ENSG00000140263. Homo sapiens.

Family and domain databases

InterPro

IPR013154. AlcDHase_GroES-like.
IPR002085. AlcDHase_SF_Zn.
IPR013149. AlcDHase_Zn-bd.
IPR002328. AlcDHase_Zn_CS.
[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

DrugBank

DB00157. NADH.

LinkHub

Q00796.

NextBio

25929.

SOURCE

Search...

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Entry information

Entry name

DHSO_HUMAN

Accession

Primary (citable) accession number: Q00796
Secondary accession number(s): Q16682, Q9UMD6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 97 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents