Reviewed,
UniProtKB/Swiss-Prot Q60HG4 (NB5R3_MACFA)
Last modified
June 16, 2009.
Version 43.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: NADH-cytochrome b5 reductase 3 Short name=Cytochrome b5 reductase Short name=B5R EC=1.6.2.2 Alternative name(s): Diaphorase-1 Cleaved into the following 2 chains: 1- Recommended name: NADH-cytochrome b5 reductase 3 membrane-bound form 2- Recommended name: NADH-cytochrome b5 reductase 3 soluble form | ||||||
| Gene names |
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| Organism | Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey) | ||||||
| Taxonomic identifier | 9541 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca |
Protein attributes
| Sequence length | 301 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction By similarity. |
| Catalytic activity | NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5. |
| Cofactor | FAD By similarity. |
| Subunit structure | Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MOSC2 By similarity. |
| Subcellular location | Isoform 1: Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side By similarity. Mitochondrion outer membrane; Lipid-anchor; Cytoplasmic side By similarity. Isoform 2: Cytoplasm. Note: Produces the soluble form found in erythrocytes By similarity. |
| Sequence similarities | Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cholesterol biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis |
| Cellular component | Cytoplasm Endoplasmic reticulum Membrane Mitochondrion Mitochondrion outer membrane |
| Coding sequence diversity | Alternative promoter usage |
| Ligand | FAD Flavoprotein NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Lipoprotein Myristate Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | cytochrome-b5 reductase activity Inferred from electronic annotation. Source: EC electron carrier activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q60HG4-1) Also known as: M; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q60HG4-2) Also known as: S; The sequence of this isoform differs from the canonical sequence as follows: 1-23: Missing. | ||||||
| Note: Produces the soluble form found in erythrocytes (By similarity). |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 301 | 300 | NADH-cytochrome b5 reductase 3 membrane-bound form | PRO_0000019395 | |||||
| Chain | 27 – 301 | 275 | NADH-cytochrome b5 reductase 3 soluble form | PRO_0000019397 | |||||
Regions | |||||||||
| Domain | 40 – 152 | 113 | FAD-binding FR-type | ||||||
| Nucleotide binding | 132 – 147 | 16 | FAD By similarity | ||||||
| Nucleotide binding | 171 – 206 | 36 | FAD By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 42 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 43 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 120 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 130 | 1 | Phosphotyrosine By similarity | ||||||
| Lipidation | 2 | 1 | N-myristoyl glycine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 23 | 23 | Missing in isoform 2. | VSP_013359 | |||||
Sequences
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References
| [1] | "Isolation and characterization of cDNA for macaque neurological disease genes." Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex. |
Cross-references
Sequence databases | |
|---|---|
| AB125163 mRNA. Translation: BAD51951.1. | |
3D structure databases | |
| SMR | Q60HG4. Positions 30-300, 31-301. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | Q60HG4. |
Enzyme and pathway databases | |
| BRENDA | 1.6.2.2. 3438. |
Family and domain databases | |
| InterPro | IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR001834. NADH-Cyt_B5_reductase. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view] |
| Pfam | PF00970. FAD_binding_6. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] |
| PRINTS | PR00406. CYTB5RDTASE. PR00371. FPNCR. |
| PROSITE | PS51384. FAD_FR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NB5R3_MACFA | ||||||||
| Accession | Primary (citable) accession number: Q60HG4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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