P86203 (NDUS1_MESAU) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 7.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial EC=1.6.5.3 EC=1.6.99.3 Alternative name(s): Complex I-75kD Short name=CI-75kD | ||
| Gene names |
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| Organism | Mesocricetus auratus (Golden hamster) | ||
| Taxonomic identifier | 10036 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus![]() |
Protein attributes
| Sequence length | 190 AA. |
| Sequence status | Fragments. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized By similarity. UniProtKB P15690 |
| Catalytic activity | NADH + ubiquinone = NAD+ + ubiquinol. UniProtKB P15690 NADH + acceptor = NAD+ + reduced acceptor. UniProtKB P15690 |
| Cofactor | Binds 1 2Fe-2S cluster per subunit By similarity. UniProtKB P29915 Binds 2 4Fe-4S clusters per subunit By similarity. UniProtKB P29915 |
| Subunit structure | Complex I is composed of 45 different subunits By similarity. UniProtKB P15690 |
| Subcellular location | Mitochondrion inner membrane By similarity. Note: Matrix and cytoplasmic side of the mitochondrial inner membrane By similarity. UniProtKB Q91VD9 |
| Sequence similarities | Belongs to the complex I 75 kDa subunit family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Respiratory chain Transport |
| Cellular component | Membrane Mitochondrion Mitochondrion inner membrane |
| Ligand | 2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological_process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chainInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | 2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster bindingInferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activityInferred from electronic annotation. Source: EC metal ion bindingInferred 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 – ›190 | ›190 | NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial | PRO_0000394295 | |||||
Experimental info | |||||||||
| Non-adjacent residues | 16 – 17 | 2 | |||||||
| Non-adjacent residues | 36 – 37 | 2 | |||||||
| Non-adjacent residues | 44 – 45 | 2 | |||||||
| Non-adjacent residues | 53 – 54 | 2 | |||||||
| Non-adjacent residues | 67 – 68 | 2 | |||||||
| Non-adjacent residues | 76 – 77 | 2 | |||||||
| Non-adjacent residues | 98 – 99 | 2 | |||||||
| Non-adjacent residues | 137 – 138 | 2 | |||||||
| Non-adjacent residues | 147 – 148 | 2 | |||||||
| Non-adjacent residues | 161 – 162 | 2 | |||||||
| Non-adjacent residues | 180 – 181 | 2 | |||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 190 | 1 | |||||||
Sequences
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References
| [1] | "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa." Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S. Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P86203. |
| ProMEX | P86203. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| PROSITE | PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. Partial match. PS00641. COMPLEX1_75K_1. Partial match. PS00642. COMPLEX1_75K_2. Partial match. PS00643. COMPLEX1_75K_3. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NDUS1_MESAU | ||||||||
| Accession | Primary (citable) accession number: P86203 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
