| Identification |
|---|
| HMDB Protein ID
| HMDBP07034 |
| Secondary Accession Numbers
| |
| Name
| Cytochrome c oxidase subunit 3 |
| Synonyms
|
- Cytochrome c oxidase polypeptide III
|
| Gene Name
| MT-CO3 |
| Protein Type
| Enzyme |
| Biological Properties |
|---|
| General Function
| Involved in cytochrome-c oxidase activity |
| Specific Function
| Subunits I, II and III form the functional core of the enzyme complex |
| Pathways
|
Not Available
|
| Reactions
| Not Available |
| GO Classification
|
| Component |
| cell part |
| membrane |
| Function |
| catalytic activity |
| oxidoreductase activity |
| heme-copper terminal oxidase activity |
| cytochrome-c oxidase activity |
| Process |
| metabolic process |
| cellular metabolic process |
| generation of precursor metabolites and energy |
| electron transport chain |
| respiratory electron transport chain |
| mitochondrial electron transport, cytochrome c to oxygen |
|
| Cellular Location
|
- Mitochondrion inner membrane
- Multi-pass membrane protein
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| MT-CO3 |
| Gene Sequence
|
>784 bp
ATGACCCACCAATCACATGCCTATCATATAGTAAAACCCAGCCCATGACCCCTAACAGGG
GCCCTCTCAGCCCTCCTAATGACCTCCGGCCTAGCCATGTGATTTCACTTCCACTCCATA
ACGCTCCTCATACTAGGCCTACTAACCAACACACTAACCATATACCAATGATGGCGCGAT
GTAACACGAGAAAGCACATACCAAGGCCACCACACACCACCTGTCCAAAAAGGCCTTCGA
TACGGGATAATCCTATTTATTACCTCAGAAGTTTTTTTCTTCGCAGGATTTTTCTGAGCC
TTTTACCACTCCAGCCTAGCCCCTACCCCCCAATTAGGAGGGCACTGGCCCCCAACAGGC
ATCACCCCGCTAAATCCCCTAGAAGTCCCACTCCTAAACACATCCGTATTACTCGCATCA
GGAGTATCAATCACCTGAGCTCACCATAGTCTAATAGAAAACAACCGAAACCAAATAATT
CAAGCACTGCTTATTACAATTTTACTGGGTCTCTATTTTACCCTCCTACAAGCCTCAGAG
TACTTCGAGTCTCCCTTCACCATTTCCGACGGCATCTACGGCTCAACATTTTTTGTAGCC
ACAGGCTTCCACGGACTTCACGTCATTATTGGCTCAACTTTCCTCACTATCTGCTTCATC
CGCCAACTAATATTTCACTTTACATCCAAACATCACTTTGGCTTCGAAGCCGCCGCCTGA
TACTGGCATTTTGTAGATGTGGTTTGACTATTTCTGTATGTCTCCATCTATTGATGAGGG
TCTT
|
| Protein Properties |
|---|
| Number of Residues
| 261 |
| Molecular Weight
| 29950.6 |
| Theoretical pI
| 7.34 |
| Pfam Domain Function
|
|
| Signals
|
|
|
Transmembrane Regions
|
- 15-35
- 42-59
- 81-101
- 127-147
- 159-179
- 197-217
- 239-259
|
| Protein Sequence
|
>Cytochrome c oxidase subunit 3
MTHQSHAYHMVKPSPWPLTGALSALLMTSGLAMWFHFHSMTLLMLGLLTNTLTMYQWWRD
VTRESTYQGHHTPPVQKGLRYGMILFITSEVFFFAGFFWAFYHSSLAPTPQLGGHWPPTG
ITPLNPLEVPLLNTSVLLASGVSITWAHHSLMENNRNQMIQALLITILLGLYFTLLQASE
YFESPFTISDGIYGSTFFVATGFHGLHVIIGSTFLTICFIRQLMFHFTSKHHFGFEAAAW
YWHFVDVVWLFLYVSIYWWGS
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| P00414 |
| UniProtKB/Swiss-Prot Entry Name
| COX3_HUMAN |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| J01415 |
| GeneCard ID
| MT-CO3 |
| GenAtlas ID
| MT-CO3 |
| HGNC ID
| HGNC:7422 |
| References |
|---|
| General References
| - Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG: Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457-65. [PubMed:7219534 ]
- Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E: Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. Hum Genet. 1991 Dec;88(2):139-45. [PubMed:1757091 ]
- Rieder MJ, Taylor SL, Tobe VO, Nickerson DA: Automating the identification of DNA variations using quality-based fluorescence re-sequencing: analysis of the human mitochondrial genome. Nucleic Acids Res. 1998 Feb 15;26(4):967-73. [PubMed:9461455 ]
- Thangaraj K, Chaubey G, Singh VK, Vanniarajan A, Thanseem I, Reddy AG, Singh L: In situ origin of deep rooting lineages of mitochondrial Macrohaplogroup 'M' in India. BMC Genomics. 2006 Jun 15;7:151. [PubMed:16776823 ]
- Johns DR, Neufeld MJ: Cytochrome c oxidase mutations in Leber hereditary optic neuropathy. Biochem Biophys Res Commun. 1993 Oct 29;196(2):810-5. [PubMed:8240356 ]
- Manfredi G, Schon EA, Moraes CT, Bonilla E, Berry GT, Sladky JT, DiMauro S: A new mutation associated with MELAS is located in a mitochondrial DNA polypeptide-coding gene. Neuromuscul Disord. 1995 Sep;5(5):391-8. [PubMed:7496173 ]
- Keightley JA, Hoffbuhr KC, Burton MD, Salas VM, Johnston WS, Penn AM, Buist NR, Kennaway NG: A microdeletion in cytochrome c oxidase (COX) subunit III associated with COX deficiency and recurrent myoglobinuria. Nat Genet. 1996 Apr;12(4):410-6. [PubMed:8630495 ]
|
