COX1
entrez
4512
canonical
uniprot
P00395
canonical
ensembl
ENSG00000198804
resolver
ensp
ENSP00000354499
resolver
enst
ENST00000361624
resolver
genesymbol
COX1
resolver
genesymbol
MT-CO1
resolver
genesymbol_syn
CO1
resolver
genesymbol_syn
COI
resolver
genesymbol_syn
COXI
resolver
genesymbol_syn
MTCO1
resolver
hgnc
HGNC:7419
resolver
uniprot
A0A1X7RBG2
resolver
uniprot
Q34770
resolver
uniprot
U5YWV7
resolver
uniprot_entry
COX1_HUMAN
resolver
uniprot_entry
U5YWV7_HUMAN
resolver
uniprot_sec
A0A1X7RBG2
resolver
uniprot_sec
Q34770
resolver
amino_acid_sequence
MFADRWLFSTNHKDIGTLYLLFGAWAGVLGTALSLLIRAELGQPGNLLGNDHIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASAMVEAGAGTGWTVYPPLAGNYSHPGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMTQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGSNMKWSAAVLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFSGYTLDQTYAKIHFTIMFIGVNLTFFPQHFLGLSGMPRRYSDYPDAYTTWNILSSVGSFISLTAVMLMIFMIWEAFASKRKVLMVEEPSMNLEWLYGCPPPYHTFEEPVYMKS
uniprot
proteins
disease_involvement
DISEASE: Leber hereditary optic neuropathy (LHON) [MIM:535000]: A maternally inherited form of Leber hereditary optic neuropathy, a mitochondrial disease resulting in bilateral painless loss of central vision due to selective degeneration of the retinal ganglion cells and their axons. The disorder shows incomplete penetrance and male predominance. Cardiac conduction defects and neurological defects have also been described in some LHON patients. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes. {ECO:0000269|PubMed:1322638}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=MT-CO1 may play a role in the pathogenesis of acquired idiopathic sideroblastic anemia, a disease characterized by inadequate formation of heme and excessive accumulation of iron in mitochondria. Mitochondrial iron overload may be attributable to mutations of mitochondrial DNA because these can cause respiratory chain dysfunction, thereby impairing reduction of ferric iron to ferrous iron. The reduced form of iron is essential to the last step of mitochondrial heme biosynthesis. {ECO:0000269|PubMed:9389715, ECO:0000269|PubMed:9851701}.; DISEASE: Mitochondrial complex IV deficiency (MT-C4D) [MIM:220110]: A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs. Features include hypertrophic cardiomyopathy, hepatomegaly and liver dysfunction, hypotonia, muscle weakness, exercise intolerance, developmental delay, delayed motor development and intellectual disability. Some affected individuals manifest a fatal hypertrophic cardiomyopathy resulting in neonatal death. A subset of patients manifest Leigh syndrome. {ECO:0000269|PubMed:12140182, ECO:0000269|PubMed:16284789}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Recurrent myoglobinuria mitochondrial (RM-MT) [MIM:550500]: Recurrent myoglobinuria is characterized by recurrent attacks of rhabdomyolysis (necrosis or disintegration of skeletal muscle) associated with muscle pain and weakness, and followed by excretion of myoglobin in the urine. {ECO:0000269|PubMed:10980727}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Deafness, sensorineural, mitochondrial (DFNM) [MIM:500008]: A form of non-syndromic deafness with maternal inheritance. Affected individuals manifest progressive, postlingual, sensorineural hearing loss involving high frequencies. {ECO:0000269|PubMed:10577941}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. {ECO:0000269|PubMed:16407113, ECO:0000269|PubMed:19218458}. Note=The gene represented in this entry may be involved in disease pathogenesis.
uniprot
proteins
ec_number
7.1.1.9
uniprot
proteins
function
FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00401}.
uniprot
proteins
mass_dalton
57041
uniprot
proteins
pathway_participation
PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P00401}.
uniprot
proteins
protein_family
Heme-copper respiratory oxidase family
uniprot
proteins
pubmed
10577941
uniprot
proteins
pubmed
10980727
uniprot
proteins
pubmed
11130070
uniprot
proteins
pubmed
12140182
uniprot
proteins
pubmed
12840039
uniprot
proteins
pubmed
12949126
uniprot
proteins
pubmed
1322638
uniprot
proteins
pubmed
14760490
uniprot
proteins
pubmed
16284789
uniprot
proteins
pubmed
16407113
uniprot
proteins
pubmed
1757091
uniprot
proteins
pubmed
19218458
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26321642
uniprot
proteins
pubmed
28844695
uniprot
proteins
pubmed
29154948
uniprot
proteins
pubmed
30030519
uniprot
proteins
pubmed
6260957
uniprot
proteins
pubmed
7219534
uniprot
proteins
pubmed
7530363
uniprot
proteins
pubmed
9389715
uniprot
proteins
pubmed
9851701
uniprot
proteins
sequence_length
513
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Multi-pass membrane protein {ECO:0000269|PubMed:30030519}.
uniprot
proteins
transmembrane_region
TRANSMEM 12..40; /note="Helical; Name=I"; /evidence="ECO:0000250|UniProtKB:P00396"; TRANSMEM 51..86; /note="Helical; Name=II"; /evidence="ECO:0000250|UniProtKB:P00396"; TRANSMEM 95..117; /note="Helical; Name=III"; /evidence="ECO:0000250|UniProtKB:P00396"; TRANSMEM 141..170; /note="Helical; Name=IV"; /evidence="ECO:0000250|UniProtKB:P00396"; TRANSMEM 183..212; /note="Helical; Name=V"; /evidence="ECO:0000250|UniProtKB:P00396"; TRANSMEM 228..261; /note="Helical; Name=VI"; /evidence="ECO:0000250|UniProtKB:P00396"; TRANSMEM 270..286; /note="Helical; Name=VII"; /evidence="ECO:0000250|UniProtKB:P00396"; TRANSMEM 299..327; /note="Helical; Name=VIII"; /evidence="ECO:0000250|UniProtKB:P00396"; TRANSMEM 336..357; /note="Helical; Name=IX"; /evidence="ECO:0000250|UniProtKB:P00396"; TRANSMEM 371..400; /note="Helical; Name=X"; /evidence="ECO:0000250|UniProtKB:P00396"; TRANSMEM 407..433; /note="Helical; Name=XI"; /evidence="ECO:0000250|UniProtKB:P00396"; TRANSMEM 447..478; /note="Helical; Name=XII"; /evidence="ECO:0000250|UniProtKB:P00396
uniprot
proteins