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Q00796 (DHSO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sorbitol dehydrogenase

EC=1.1.1.14
Alternative name(s):
L-iditol 2-dehydrogenase
Gene names
Name:SORD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length357 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm By similarity. Ref.9

Catalytic activity

L-iditol + NAD+ = L-sorbose + NADH.

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Homotetramer. Ref.14

Subcellular location

Mitochondrion membrane; Peripheral membrane protein. Cell projectionciliumflagellum. Note: Associated with mitochondria of the midpiece and near the plasma membrane in the principal piece of the flagellum. Also found in the epididymosome, secreted by the epididymal epithelium and that transfers proteins from the epididymal fluid to the sperm surface By similarity.

Tissue specificity

Expressed in kidney and epithelial cells of both benign and malignant prostate tissue. Expressed in epididymis (at protein level). Ref.9 Ref.11 Ref.12

Induction

Up-regulated by androgens and down-regulated by castration. Ref.11

Miscellaneous

The polyol pathway is proposed to be involved the cellular toxicity of diabetic hyperglycemia.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
   Cellular componentCell projection
Cilium
Flagellum
Membrane
Mitochondrion
   Coding sequence diversityPolymorphism
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processL-xylitol catabolic process

Inferred from direct assay PubMed 8487505. Source: UniProtKB

L-xylitol metabolic process

Inferred from direct assay PubMed 3365415. Source: UniProtKB

fructose biosynthetic process

Inferred from direct assay PubMed 3365415PubMed 6870831PubMed 8487505. Source: UniProtKB

glucose metabolic process

Traceable author statement PubMed 14965227. Source: UniProtKB

sorbitol catabolic process

Inferred from direct assay Ref.14PubMed 3365415PubMed 6870831PubMed 8487505. Source: UniProtKB

sperm motility

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentextracellular space

Traceable author statement PubMed 6177277. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

membrane

Inferred from direct assay PubMed 8487505. Source: UniProtKB

mitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

motile cilium

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionL-iditol 2-dehydrogenase activity

Inferred from direct assay PubMed 3365415PubMed 6870831PubMed 8487505. Source: UniProtKB

NAD binding

Inferred from direct assay Ref.14. Source: UniProtKB

carbohydrate binding

Non-traceable author statement Ref.14. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.14. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7 Ref.8 Ref.10
Chain2 – 357356Sorbitol dehydrogenase
PRO_0000160817

Sites

Metal binding451Zinc; catalytic
Metal binding701Zinc; catalytic
Metal binding711Zinc; catalytic
Binding site511Substrate By similarity
Binding site1561Substrate By similarity
Binding site2991Substrate By similarity
Binding site3001Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.1 Ref.10

Natural variations

Natural variant2391Q → L. Ref.2
Corresponds to variant rs55739437 [ dbSNP | Ensembl ].
VAR_000430
Natural variant2691N → T. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6
Corresponds to variant rs2229659 [ dbSNP | Ensembl ].
VAR_060351

Experimental info

Sequence conflict51Missing AA sequence Ref.7
Sequence conflict591N → D AA sequence Ref.7
Sequence conflict1861M → E AA sequence Ref.7
Sequence conflict2811T → S AA sequence Ref.7
Sequence conflict2891I → T AA sequence Ref.7

Secondary structure

......................................................... 357
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00796 [UniParc].

Last modified March 23, 2010. Version 4.
Checksum: FF13DDD5EBE47754

FASTA35738,325
        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 EIARKVEGQL 

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

       310        320        330        340        350 
CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC DPSDQNP 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-269.
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS LEU-239 AND THR-269.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-269.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-269.
Tissue: Brain.
[5]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-269.
Tissue: Brain and Lymph.
[7]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-357.
Tissue: Liver.
[8]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
Tissue: Platelet.
[9]"Polyol pathway in human epididymis and semen."
Frenette G., Thabet M., Sullivan R.
J. Androl. 27:233-239(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"Sorbitol dehydrogenase expression is regulated by androgens in the human prostate."
Szabo Z., Hamalainen J., Loikkanen I., Moilanen A.M., Hirvikoski P., Vaisanen T., Paavonen T.K., Vaarala M.H.
Oncol. Rep. 23:1233-1239(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[12]"ZAC1 is up-regulated by hypertonicity and decreases sorbitol dehydrogenase expression, allowing accumulation of sorbitol in kidney cells."
Lanaspa M.A., Andres-Hernando A., Rivard C.J., Dai Y., Li N., Berl T.
J. Biol. Chem. 284:19974-19981(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U07361 mRNA. Translation: AAA66064.1.
L29008 mRNA. Translation: AAA80565.1.
L29254 expand/collapse EMBL AC list , L29249, L29250, L29251, L29252, L29253 Genomic DNA. Translation: AAA80566.1.
U67243 expand/collapse EMBL AC list , U67236, U67237, U67238, U67239, U67240, U67241, U67242 Genomic DNA. Translation: AAB61898.1.
AK312444 mRNA. Translation: BAG35352.1.
AC090888 Genomic DNA. No translation available.
AC091117 Genomic DNA. No translation available.
BC021085 mRNA. Translation: AAH21085.1.
BC025295 mRNA. Translation: AAH25295.1.
PIRA54674.
RefSeqNP_003095.2. NM_003104.5.
UniGeneHs.878.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PL6X-ray2.00A/B/C/D2-357[»]
1PL7X-ray2.20A/B/C/D2-357[»]
1PL8X-ray1.90A/B/C/D2-357[»]
ProteinModelPortalQ00796.
SMRQ00796. Positions 2-357.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112535. 33 interactions.
IntActQ00796. 1 interaction.
MINTMINT-5004436.
STRING9606.ENSP00000267814.

Chemistry

ChEMBLCHEMBL2275.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteQ00796.

Polymorphism databases

DMDM292495088.

2D gel databases

REPRODUCTION-2DPAGEIPI00216057.

Proteomic databases

PaxDbQ00796.
PRIDEQ00796.

Protocols and materials databases

DNASU6652.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267814; ENSP00000267814; ENSG00000140263.
GeneID6652.
KEGGhsa:6652.
UCSCuc001zul.4. human.

Organism-specific databases

CTD6652.
GeneCardsGC15P045315.
HGNCHGNC:11184. SORD.
HPAHPA040260.
HPA040621.
MIM182500. gene.
neXtProtNX_Q00796.
PharmGKBPA36021.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1063.
HOGENOMHOG000294670.
HOVERGENHBG005484.
InParanoidQ00796.
KOK00008.
OMAMHNTREI.
OrthoDBEOG7DRJ36.
PhylomeDBQ00796.
TreeFamTF313060.

Enzyme and pathway databases

SABIO-RKQ00796.

Gene expression databases

ArrayExpressQ00796.
BgeeQ00796.
CleanExHS_SORD.
GenevestigatorQ00796.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ00796.
GeneWikiSORD.
GenomeRNAi6652.
NextBio25929.
PROQ00796.
SOURCESearch...

Entry information

Entry nameDHSO_HUMAN
AccessionPrimary (citable) accession number: Q00796
Secondary accession number(s): B2R655 expand/collapse secondary AC list , J3JZZ5, Q16682, Q9UMD6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: March 23, 2010
Last modified: April 16, 2014
This is version 158 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

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