P86250 (NDUS2_MESAU) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 3, 2012.
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 dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial EC=1.6.5.3 EC=1.6.99.3 Alternative name(s): Complex I-49kD Short name=CI-49kD NADH-ubiquinone oxidoreductase 49 kDa subunit | ||
| 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 | 138 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 By similarity. UniProtKB P17694 |
| Catalytic activity | NADH + ubiquinone = NAD+ + ubiquinol. UniProtKB P17694 NADH + acceptor = NAD+ + reduced acceptor. UniProtKB P17694 |
| Cofactor | Binds 1 4Fe-4S cluster By similarity. UniProtKB P17694 |
| Subunit structure | Complex I is composed of 45 different subunits. Component of the iron-sulfur (IP) fragment of the enzyme. Interacts with NDUFAF3 By similarity. UniProtKB O75306 |
| Subcellular location | Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity UniProtKB P17694. |
| Sequence similarities | Belongs to the complex I 49 kDa subunit family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Respiratory chain Transport |
| Cellular component | Membrane Mitochondrion Mitochondrion inner membrane |
| Ligand | 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 | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NAD bindingInferred from electronic annotation. Source: InterPro NADH dehydrogenase (ubiquinone) activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW quinone bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – 138 | ›138 | NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial | PRO_0000394421 | |||||
Experimental info | |||||||||
| Non-adjacent residues | 11 – 12 | 2 | |||||||
| Non-adjacent residues | 20 – 21 | 2 | |||||||
| Non-adjacent residues | 29 – 30 | 2 | |||||||
| Non-adjacent residues | 74 – 75 | 2 | |||||||
| Non-adjacent residues | 94 – 95 | 2 | |||||||
| Non-adjacent residues | 115 – 116 | 2 | |||||||
| Non-terminal residue | 1 | 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 | P86250. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR001135. NADH_Q_OxRdtase_suD. [Graphical view] |
| Pfam | PF00346. Complex1_49kDa. 2 hits. [Graphical view] |
| PROSITE | PS00535. COMPLEX1_49K. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NDUS2_MESAU | ||||||||
| Accession | Primary (citable) accession number: P86250 | ||||||||
| 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
