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Identification
HMDB Protein ID HMDBP01631
Secondary Accession Numbers
  • 6954
Name Protoheme IX farnesyltransferase, mitochondrial
Synonyms
  1. Heme O synthase
Gene Name COX10
Protein Type Unknown
Biological Properties
General Function Involved in protoheme IX farnesyltransferase activity
Specific Function Converts protoheme IX and farnesyl diphosphate to heme O (By similarity).
Pathways
  • Acute Intermittent Porphyria
  • Congenital Erythropoietic Porphyria (CEP) or Gunther Disease
  • Hereditary Coproporphyria (HCP)
  • Oxidative phosphorylation
  • Porphyria Variegata (PV)
  • Porphyrin and chlorophyll metabolism
  • Porphyrin Metabolism
Reactions
Heme + Water + Farnesyl pyrophosphate → Heme O + Pyrophosphate details
GO Classification
Biological Process
cytochrome complex assembly
heme a biosynthetic process
heme O biosynthetic process
mitochondrial electron transport, cytochrome c to oxygen
mitochondrial fission
respiratory chain complex IV assembly
aerobic respiration
Cellular Component
mitochondrial membrane
mitochondrion
integral to membrane
Component
membrane
cell part
membrane part
organelle membrane
intrinsic to membrane
integral to membrane
mitochondrial membrane
Function
catalytic activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
prenyltransferase activity
farnesyltranstransferase activity
protoheme ix farnesyltransferase activity
Molecular Function
farnesyltranstransferase activity
protoheme IX farnesyltransferase activity
Process
metabolic process
nitrogen compound metabolic process
tetrapyrrole metabolic process
porphyrin metabolic process
heme biosynthetic process
porphyrin biosynthetic process
heme o biosynthetic process
Cellular Location
  1. Mitochondrion membrane
  2. Multi-pass membrane protein
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs COX10
Gene Sequence
>1332 bp
ATGGCCGCATCTCCGCACACTCTCTCCTCACGCCTCCTGACAGGTTGCGTAGGAGGCTCT
GTCTGGTATCTTGAAAGAAGAACTATACAGGACTCCCCTCACAAGTTCTTACATCTTCTC
AGGAATGTCAATAAGCAGTGGATTACATTTCAGCACTTTAGCTTCCTCAAACGCATGTAT
GTCACACAGCTGAACAGAAGCCACAACCAGCAAGTAAGACCCAAGCCAGAACCAGTAGCA
TCTCCTTTCCTTGAAAAAACATCTTCAGGTCAAGCCAAAGCAGAAATATATGAGATGAGA
CCTCTCTCACCGCCCAGCCTATCTTTGTCCAGAAAGCCAAATGAAAAGGAATTGATAGAA
CTAGAGCCAGACTCAGTAATTGAAGACTCAATAGATGTAGGGAAAGAGACAAAAGAGGAA
AAGCGGTGGAAAGAGATGAAGCTGCAAGTGTATGATTTGCCAGGAATTTTGGCTCGACTA
TCCAAAATCAAACTCACAGCTCTGGTTGTAAGTACCACTGCAGCTGGATTTGCATTGGCT
CCGGGCCCTTTTGACTGGCCCTGTTTCCTGCTTACTTCTGTTGGGACAGGCCTTGCATCC
TGTGCTGCCAACTCCATCAATCAGTTTTTTGAGGTGCCATTTGACTCAAACATGAATAGG
ACAAAGAACAGACCGCTGGTTCGTGGACAGATCAGCCCATTGCTAGCTGTGTCCTTTGCC
ACTTGTTGTGCTGTTCCGGGAGTTGCCATTCTGACCTTGGGGGTGAATCCACTCACAGGA
GCCCTGGGGCTCTTCAACATTTTCCTGTATACCTGCTGCTACACACCACTGAAAAGGATC
AGCATTGCCAACACATGGGTCGGAGCTGTGGTTGGGGCCATCCCGCCTGTCATGGGCTGG
ACAGCGGCCACGGGCAGCCTCGATGCTGGCGCATTTCTCCTGGGAGGAATCCTCTACTCC
TGGCAGTTTCCTCATTTCAACGCCCTGAGCTGGGGCCTCCGTGAAGACTACTCCCGGGGC
GGCTACTGCATGATGTCGGTCACCCACCCGGGCCTGTGCCGGCGCGTGGCGCTGCGCCAC
TGCCTGGCCCTGCTCGTGCTGTCCGCAGCAGCCCCTGTGCTGGACATCACCACATGGACC
TTCCCCATCATGGCCCTTCCCATCAATGCGTACATCTCCTACCTCGGCTTCCGCTTCTAC
GTGGACGCAGACCGCAGGAGCTCGCGGAGACTGTTCTTCTGCAGCCTGTGGCACCTGCCG
CTGCTGCTGCTGCTCATGCTCACCTGCAAGCGGCCGAGCGGAGGCGGGGACGCAGGGCCC
CCTCCCAGCTGA
Protein Properties
Number of Residues 443
Molecular Weight Not Available
Theoretical pI Not Available
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Protoheme IX farnesyltransferase, mitochondrial
MAASPHTLSSRLLTGCVGGSVWYLERRTIQDSPHKFLHLLRNVNKQWITFQHFSFLKRMY
VTQLNRSHNQQVRPKPEPVASPFLEKTSSGQAKAEIYEMRPLSPPSLSLSRKPNEKELIE
LEPDSVIEDSIDVGKETKEEKRWKEMKLQVYDLPGILARLSKIKLTALVVSTTAAGFALA
PGPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFA
TCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTPLKRISIANTWVGAVVGAIPPVMGW
TAATGSLDAGAFLLGGILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPGLCRRVALRH
CLALLVLSAAAPVLDITTWTFPIMALPINAYISYLGFRFYVDADRRSSRRLFFCSLWHLP
LLLLLMLTCKRPSGGGDAGPPPS
GenBank ID Protein 17921982
UniProtKB/Swiss-Prot ID Q12887
UniProtKB/Swiss-Prot Entry Name COX10_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_001303.3
GeneCard ID COX10
GenAtlas ID COX10
HGNC ID HGNC:2260
References
General References
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  3. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed:16625196 ]
  4. Glerum DM, Tzagoloff A: Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant. Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8452-6. [PubMed:8078902 ]
  5. Murakami T, Reiter LT, Lupski JR: Genomic structure and expression of the human heme A:farnesyltransferase (COX10) gene. Genomics. 1997 May 15;42(1):161-4. [PubMed:9177788 ]
  6. Valnot I, von Kleist-Retzow JC, Barrientos A, Gorbatyuk M, Taanman JW, Mehaye B, Rustin P, Tzagoloff A, Munnich A, Rotig A: A mutation in the human heme A:farnesyltransferase gene (COX10 ) causes cytochrome c oxidase deficiency. Hum Mol Genet. 2000 May 1;9(8):1245-9. [PubMed:10767350 ]
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