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Primary Information | |
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| BoMiProt ID | Bomi255 |
| Protein Name | Cytochrome c oxidase subunit 4 isoform 1, mitochondrial |
| Organism | Bos taurus |
| Uniprot ID | P00423 |
| Milk Fraction | MFGM |
| Ref Sequence ID | NP_001001439.1 |
| Aminoacid Length | 169 |
| Molecular Weight | 19572 |
| FASTA Sequence | Download |
| Gene Name | COX4I1 |
| Gene ID | 281090 |
| Protein Existence Status | Reviewed: Experimental evidence at protein level |
Secondary Information | |
| Protein Function | terminal enzyme of the respiratory chains of mitochondria; use the electrons of cytochrome c to reduce molecular oxygen; central role in aerobic metabolism- participates in respiratory control |
| Biochemical Properties | members of the superfamily of heme/copper containing terminal oxidases; |
| PTMs | phoshorylated |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
| SCOP | Class : All alpha proteins Fold : Single transmembrane helix Superfamily : Mitochondrial cytochrome c oxidase subunit IV Family : Mitochondrial cytochrome c oxidase subunit IV Domain Name : 1V54 D:4-147 |
| CATH | Matched CATH superfamily 1.10.442.10 |
| Predicted Disorder Regions | NA |
| DisProt Annotation | |
| TM Helix Prediction | 1TMH; (102-120) |
| Significance of PTMs | activity can be modulated according to the energetic requirement of the cell through isoform subunits composition and physiologically controlled phosphorylation |
| PDB ID | 1OCC, 1OCO, 1OCR, 1OCZ, 1V54, 1V55, 2DYR, 2DYS, 2EIJ, 2EIK, 2EIL, 2EIM, 2EIN, 2OCC, 2Y69, 2YBB, 2ZXW, 3ABK, 3ABL, 3ABM, 3AG1, 3AG2, 3AG3, 3AG4, 3ASN, 3ASO, 3WG7, 3X2Q, 5B1A, 5B1B, 5GPN, 5IY5, 5LUF, 5W97, 5WAU, 5X19, 5X1B, 5X1F, 5XDQ, 5XDX, 5XTH, 5XTI, 5Z84, 5Z85, 5Z86, 5ZCO, 5ZCP, 5ZCQ, 6NKN, 6NMF, 6NMP, 7COH, 7CP5, 7D5W, 7D5X,7EV7, |
| Bibliography | 1. Zong, S. et al. (2018) ‘Structure of the intact 14-subunit human cytochrome c oxidase.’, Cell research, 28(10), pp. 1026–1034. doi: 10.1038/s41422-018-0071-1. 2. Tsukihara, T. et al. (1996) ‘The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 A’, Science, 272(5265), pp. 1136–1144. doi: 10.1126/science.272.5265.1136. 3. Linder, D., Freund, R. and Kadenbach, B. (1995) ‘Species-specific expression of cytochrome c oxidase isozymes’, Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 112(3), pp. 461–469. doi: 10.1016/0305-0491(95)00093-3. |