Reviewed,
UniProtKB/Swiss-Prot P35571 (GPDM_RAT)
Last modified
June 16, 2009.
Version 79.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glycerol-3-phosphate dehydrogenase, mitochondrial Short name=GPDH-M Short name=GPD-M EC=1.1.5.3 | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 727 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol. |
| Cofactor | FAD. |
| Enzyme regulation | Calcium-binding enhance the activity of the enzyme. |
| Pathway | |
| Subcellular location | |
| Sequence similarities | Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family. Contains 2 EF-hand domains. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Repeat Transit peptide |
| Ligand | Calcium FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | NADH metabolic process Inferred from direct assay. Source: RGD glycerol-3-phosphate metabolic processInferred from direct assay. Source: RGD oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro mitochondrionInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW glycerol-3-phosphate dehydrogenase (NAD+) activityInferred from direct assay. Source: RGD glycerol-3-phosphate dehydrogenase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 42 | 42 | Mitochondrion Ref.1 | ||||||
| Chain | 43 – 727 | 685 | Glycerol-3-phosphate dehydrogenase, mitochondrial | PRO_0000010431 | |||||
Regions | |||||||||
| Domain | 623 – 658 | 36 | EF-hand 1 | ||||||
| Domain | 659 – 694 | 36 | EF-hand 2 | ||||||
| Nucleotide binding | 71 – 99 | 29 | FAD Potential | ||||||
| Calcium binding | 672 – 683 | 12 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 600 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 601 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence of rat mitochondrial glycerol-3-phosphate dehydrogenase cDNA. Evidence for EF-hand calcium-binding domains." Brown L.J., McDonald M.J., Lehn D.A., Moran S.M. J. Biol. Chem. 269:14363-14366(1994) [PubMed: 8182039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-58. Strain: Sprague-Dawley. Tissue: Testis. |
| [2] | "Cloning of a cDNA for the FAD-linked glycerol-3-phosphate dehydrogenase from rat liver and its regulation by thyroid hormones." Mueller S., Seitz H.J. Proc. Natl. Acad. Sci. U.S.A. 91:10581-10585(1994) [PubMed: 7937996] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar. Tissue: Liver. |
| [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis. |
Cross-references
Sequence databases | |
|---|---|
| U08027 mRNA. Translation: AAB60443.1. X78593 mRNA. Translation: CAA55329.1. BC083565 mRNA. Translation: AAH83565.1. | |
| IPI | IPI00199663. |
| PIR | A54051. |
| RefSeq | NP_036868.1. |
| UniGene | Rn.89705 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CDM based on UniProtKB P02593. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P35571. |
Proteomic databases | |
| PRIDE | P35571. |
Genome annotation databases | |
| GeneID | 25062. |
| KEGG | rno:25062. |
Organism-specific databases | |
| RGD | 2726. Gpd2. |
Phylogenomic databases | |
| HOVERGEN | P35571. |
Enzyme and pathway databases | |
| BRENDA | 1.1.99.5. 248. |
Gene expression databases | |
| ArrayExpress | P35571. |
Family and domain databases | |
| InterPro | IPR011992. EF-Hand_type. IPR018248. EF_hand. IPR018247. EF_HAND_1. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca_bd. IPR000447. FAD-dep_Gly3P_DH. IPR006076. FAD-dep_OxRdtase. [Graphical view] |
| Gene3D | G3DSA:1.10.238.10. EF-Hand_type. 1 hit. |
| Pfam | PF01266. DAO. 1 hit. PF00036. efhand. 1 hit. [Graphical view] |
| PRINTS | PR01001. FADG3PDH. |
| ProDom | PD000012. EF-hand. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00054. EFh. 2 hits. [Graphical view] |
| PROSITE | PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 2 hits. PS00977. FAD_G3PDH_1. 1 hit. PS00978. FAD_G3PDH_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 605290. |
Entry information
| Entry name | GPDM_RAT | ||||||||
| Accession | Primary (citable) accession number: P35571 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


