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Protein

Sorbitol dehydrogenase

Gene

Sord

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Zinc; catalyticBy similarity
Binding sitei51 – 511SubstrateBy similarity
Metal bindingi70 – 701Zinc; catalyticBy similarity
Metal bindingi71 – 711Zinc; catalyticBy similarity
Binding sitei156 – 1561SubstrateBy similarity
Binding sitei299 – 2991SubstrateBy similarity
Binding sitei300 – 3001SubstrateBy similarity

GO - Molecular functioni

  • D-xylulose reductase activity Source: Ensembl
  • identical protein binding Source: RGD
  • L-iditol 2-dehydrogenase activity Source: UniProtKB-EC
  • NAD binding Source: Ensembl
  • zinc ion binding Source: RGD

GO - Biological processi

  • fructose biosynthetic process Source: Ensembl
  • L-xylitol catabolic process Source: Ensembl
  • response to cadmium ion Source: RGD
  • response to copper ion Source: RGD
  • response to drug Source: RGD
  • response to hormone Source: RGD
  • response to nutrient levels Source: RGD
  • response to osmotic stress Source: RGD
  • sorbitol catabolic process Source: Ensembl
  • sperm motility Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-5652227. Fructose biosynthesis.
R-RNO-5661270. Catabolism of glucuronate to xylulose-5-phosphate.
SABIO-RKP27867.

Names & Taxonomyi

Protein namesi
Recommended name:
Sorbitol dehydrogenase (EC:1.1.1.14)
Alternative name(s):
L-iditol 2-dehydrogenase
Gene namesi
Name:Sord
Synonyms:Sdh1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi3734. Sord.

Subcellular locationi

  • Mitochondrion membrane By similarity; Peripheral membrane protein By similarity
  • Cell projectionciliumflagellum By similarity

  • 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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Flagellum, Membrane, Mitochondrion

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4038.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 357356Sorbitol dehydrogenasePRO_0000000884Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei169 – 1691PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP27867.
PRIDEiP27867.

PTM databases

iPTMnetiP27867.
PhosphoSiteiP27867.

Expressioni

Gene expression databases

GenevisibleiP27867. RN.

Interactioni

Subunit structurei

Homotetramer.By similarity

GO - Molecular functioni

  • identical protein binding Source: RGD

Protein-protein interaction databases

MINTiMINT-4566526.
STRINGi10116.ENSRNOP00000023350.

Chemistry

BindingDBiP27867.

Structurei

3D structure databases

ProteinModelPortaliP27867.
SMRiP27867. Positions 2-357.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0024. Eukaryota.
COG1063. LUCA.
GeneTreeiENSGT00550000074781.
HOGENOMiHOG000294670.
HOVERGENiHBG005484.
InParanoidiP27867.
KOiK00008.
OMAiTHNANFC.
OrthoDBiEOG7DRJ36.
PhylomeDBiP27867.
TreeFamiTF313060.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27867-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPAKGENL SLVVHGPGDI RLENYPIPEL GPNDVLLKMH SVGICGSDVH
60 70 80 90 100
YWEHGRIGDF VVKKPMVLGH EAAGTVTKVG PMVKHLKPGD RVAIEPGVPR
110 120 130 140 150
EIDEFCKIGR YNLTPSIFFC ATPPDDGNLC RFYKHSADFC YKLPDSVTFE
160 170 180 190 200
EGALIEPLSV GIYACRRGSV SLGNKVLVCG AGPIGIVTLL VAKAMGASQV
210 220 230 240 250
VVIDLSASRL AKAKEVGADF TIQVAKETPH DIAKKVESVL GSKPEVTIEC
260 270 280 290 300
TGAESSVQTG IYATHSGGTL VVVGMGPEMI NLPLVHAAVR EVDIKGVFRY
310 320 330 340 350
CNTWPMAVSM LASKTLNVKP LVTHRFPLEK AVEAFETAKK GLGLKVMIKC

DPNDQNP
Length:357
Mass (Da):38,235
Last modified:July 10, 2007 - v4
Checksum:iE6F535775EF73D36
GO

Sequence cautioni

The sequence CAA52670.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti259 – 2591T → D in CAA41761 (PubMed:2050152).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59037 mRNA. Translation: CAA41761.1.
X74593 mRNA. Translation: CAA52670.1. Different initiation.
BC088398 mRNA. Translation: AAH88398.2.
BC098919 mRNA. Translation: AAH98919.2.
BC128707 mRNA. Translation: AAI28708.2.
PIRiS38363. S16132.
RefSeqiNP_058748.2. NM_017052.2.
UniGeneiRn.11334.

Genome annotation databases

EnsembliENSRNOT00000023350; ENSRNOP00000023350; ENSRNOG00000017291.
GeneIDi24788.
KEGGirno:24788.
UCSCiRGD:3734. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59037 mRNA. Translation: CAA41761.1.
X74593 mRNA. Translation: CAA52670.1. Different initiation.
BC088398 mRNA. Translation: AAH88398.2.
BC098919 mRNA. Translation: AAH98919.2.
BC128707 mRNA. Translation: AAI28708.2.
PIRiS38363. S16132.
RefSeqiNP_058748.2. NM_017052.2.
UniGeneiRn.11334.

3D structure databases

ProteinModelPortaliP27867.
SMRiP27867. Positions 2-357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4566526.
STRINGi10116.ENSRNOP00000023350.

Chemistry

BindingDBiP27867.
ChEMBLiCHEMBL4038.

PTM databases

iPTMnetiP27867.
PhosphoSiteiP27867.

Proteomic databases

PaxDbiP27867.
PRIDEiP27867.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023350; ENSRNOP00000023350; ENSRNOG00000017291.
GeneIDi24788.
KEGGirno:24788.
UCSCiRGD:3734. rat.

Organism-specific databases

CTDi6652.
RGDi3734. Sord.

Phylogenomic databases

eggNOGiKOG0024. Eukaryota.
COG1063. LUCA.
GeneTreeiENSGT00550000074781.
HOGENOMiHOG000294670.
HOVERGENiHBG005484.
InParanoidiP27867.
KOiK00008.
OMAiTHNANFC.
OrthoDBiEOG7DRJ36.
PhylomeDBiP27867.
TreeFamiTF313060.

Enzyme and pathway databases

ReactomeiR-RNO-5652227. Fructose biosynthesis.
R-RNO-5661270. Catabolism of glucuronate to xylulose-5-phosphate.
SABIO-RKP27867.

Miscellaneous databases

PROiP27867.

Gene expression databases

GenevisibleiP27867. RN.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sorbitol dehydrogenase: cDNA coding for the rat enzyme. Variations within the alcohol dehydrogenase family independent of quaternary structure and metal content."
    Karlsson C., Joernvall H., Heoeog J.O.
    Eur. J. Biochem. 198:761-765(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Sorbitol dehydrogenase. Full-length cDNA sequencing reveals a mRNA coding for a protein containing an additional 42 amino acids at the N-terminal end."
    Wen Y., Bekhor I.
    Eur. J. Biochem. 217:83-87(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Testis.
  3. "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].
    Tissue: Embryonic liver, Liver and Testis.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDHSO_RAT
AccessioniPrimary (citable) accession number: P27867
Secondary accession number(s): A2VCV9, Q4FZY4, Q5I0F3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 10, 2007
Last modified: June 8, 2016
This is version 153 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.