Primary Information | |
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BoMiProt ID | Bomi261 |
Protein Name | Cytochrome b5 |
Organism | Bos taurus |
Uniprot ID | P00171 |
Milk Fraction | Exosome |
Ref Sequence ID | NP_776458.1 |
Aminoacid Length | 134 |
Molecular Weight | 15329 |
FASTA Sequence | Download |
Gene Name | CYB5A |
Gene ID | 281110 |
Protein Existence Status | Reviewed: Experimental evidence at protein level |
Secondary Information | |
Protein Function | reduce hemoglobin in red blood cells; in non-erythrocyte cells cytosolic cytochrome b5 is required for the reduction of a non-heme, iron-containing cytosolic protein; has role in lipid biosynthesis |
Biochemical Properties | heme-containing protein; electron transfer protein with a redox potential of 20 mV which is capable of accepting and transferring a single electron; composed of two domains: a hydrophobic tail which anchors the protein to the membrane, and a hydrophilic portion, the heme-binding domain, which is active in redox reactions |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
SCOP | Class : Alpha and beta proteins (a+b) Fold : Cytochrome b5-like Superfamily : Cytochrome b5-like heme/steroid binding domain Family : Cytochrome b5 Domain Name : 1CYO A:1-88 |
CATH | Matched CATH superfamily 3.10.120.10 |
Predicted Disorder Regions | 1-6,45-70,88-103 |
DisProt Annotation | |
TM Helix Prediction | 1TMH ; (109-131) |
PDB ID | 1CYO, 1EHB, 1ES1, 1F03, 1F04, 1HKO, 1I5U, 1J0Q, 1LQX, 1LR6, 1M20, 1M2I, 1M2M, 1M59, 1NX7, 1SH4, 1U9M, 1U9U, 3OZZ, 4HIN, |
Bibliography | 1. Bart, A. G. and Scott, E. E. (2017) ‘Structural and functional effects of cytochrome b 5 interactions with human cytochrome P450 enzymes’, Journal of Biological Chemistry, 292(51), pp. 20818–20833. doi: 10.1074/jbc.RA117.000220. |