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Protein

Cytochrome c oxidase assembly factor 6 homolog

Gene

COA6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the maturation of the mitochondrial respiratory chain complex IV subunit MT-CO2/COX2. Thereby, may regulate early steps of complex IV assembly. Mitochondrial respiratory chain complex IV or cytochrome c oxidase is the component of the respiratory chain that catalyzes the transfer of electrons from intermembrane space cytochrome c to molecular oxygen in the matrix and as a consequence contributes to the proton gradient involved in mitochondrial ATP synthesis. May also be required for efficient formation of respiratory supercomplexes comprised of complexes III and IV.3 Publications

GO - Molecular functioni

  • copper ion binding Source: UniProtKB
  • cytochrome-c oxidase activity Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • plasma membrane ATP synthesis coupled electron transport Source: UniProtKB
  • respiratory chain complex IV assembly Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase assembly factor 6 homolog
Gene namesi
Name:COA6
Synonyms:C1orf31
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18025. COA6.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial intermembrane space Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • plasma membrane Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Cardioencephalomyopathy, fatal infantile, due to cytochrome c oxidase deficiency 4 (CEMCOX4)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn infantile disorder with a fatal course in the first weeks of life, characterized by hypertrophic cardiomyopathy, left ventricular non-compaction, lactic acidosis, metabolic hypotonia, and mitochondrial complex IV deficiency.
See also OMIM:616501
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591W → C in CEMCOX4; mistargeted to the mitochondrial matrix; loss of interaction with SCO2 and MT-CO2. 2 Publications
VAR_075046
Natural varianti66 – 661W → R in CEMCOX4. 1 Publication
VAR_075047

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi616501. phenotype.
PharmGKBiPA25617.

Polymorphism and mutation databases

BioMutaiCOA6.
DMDMi74742178.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 125125Cytochrome c oxidase assembly factor 6 homologPRO_0000280399Add
BLAST
Isoform 3 (identifier: Q5JTJ3-3)
Initiator methionineiRemovedCombined sources

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 90By similarity
Disulfide bondi68 ↔ 79By similarity
Isoform 3 (identifier: Q5JTJ3-3)
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

EPDiQ5JTJ3.
MaxQBiQ5JTJ3.
PaxDbiQ5JTJ3.
PRIDEiQ5JTJ3.

PTM databases

iPTMnetiQ5JTJ3.
PhosphoSiteiQ5JTJ3.

Expressioni

Gene expression databases

BgeeiQ5JTJ3.
CleanExiHS_C1orf31.
ExpressionAtlasiQ5JTJ3. baseline and differential.
GenevisibleiQ5JTJ3. HS.

Organism-specific databases

HPAiHPA028588.

Interactioni

Subunit structurei

Interacts with COA1 (PubMed:22356826). Interacts with MT-CO2 (PubMed:25959673). Interacts with SCO2 (PubMed:25959673). Interacts with SCO1 (PubMed:26160915).3 Publications

Protein-protein interaction databases

BioGridi132839. 2 interactions.
IntActiQ5JTJ3. 3 interactions.
STRINGi9606.ENSP00000355572.

Structurei

3D structure databases

ProteinModelPortaliQ5JTJ3.
SMRiQ5JTJ3. Positions 43-111.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3057. Eukaryota.
ENOG41121WM. LUCA.
GeneTreeiENSGT00390000004094.
HOGENOMiHOG000196422.
HOVERGENiHBG056284.
InParanoidiQ5JTJ3.
KOiK18179.
OMAiLLGDCGP.
OrthoDBiEOG74R1T7.
PhylomeDBiQ5JTJ3.
TreeFamiTF335992.

Family and domain databases

Gene3Di1.10.10.140. 1 hit.
InterProiIPR003213. Cyt_c_oxidase_su6B.
[Graphical view]
PfamiPF02297. COX6B. 1 hit.
[Graphical view]
SUPFAMiSSF47694. SSF47694. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5JTJ3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGPGGPLLSP SRGFLLCKTG WHSNRLLGDC GPHTPVSTAL SFIAVGMAAP
60 70 80 90 100
SMKERQVCWG ARDEYWKCLD ENLEDASQCK KLRSSFESSC PQQWIKYFDK
110 120
RRDYLKFKEK FEAGQFEPSE TTAKS
Length:125
Mass (Da):14,116
Last modified:February 15, 2005 - v1
Checksum:i69192034A460F462
GO
Isoform 2 (identifier: Q5JTJ3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-40: MGPGGPLLSP...GPHTPVSTAL → MVARKGQKSP...KEAGRGRAES

Note: Gene prediction based on EST data.
Show »
Length:156
Mass (Da):18,094
Checksum:i9D5D3FA9B17E51E7
GO
Isoform 3 (identifier: Q5JTJ3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.

Note: Gene prediction based on EST data.Combined sources
Show »
Length:79
Mass (Da):9,428
Checksum:iE743974EE94DA3FE
GO

Sequence cautioni

The sequence AAH25793.1 differs from that shown.Contaminating sequence.Curated
The sequence AAH25793.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591W → C in CEMCOX4; mistargeted to the mitochondrial matrix; loss of interaction with SCO2 and MT-CO2. 2 Publications
VAR_075046
Natural varianti66 – 661W → R in CEMCOX4. 1 Publication
VAR_075047

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4646Missing in isoform 3. CuratedVSP_023655Add
BLAST
Alternative sequencei1 – 4040MGPGG…VSTAL → MVARKGQKSPRFRRVSCFLR LGRSTLLELEPAGRPCSGRT RHRALHRRLVACVTVSSRRH RKEAGRGRAES in isoform 2. CuratedVSP_023656Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL355472 Genomic DNA. Translation: CAI22928.1.
AL355472 Genomic DNA. Translation: CAI22929.1.
AL355472 Genomic DNA. Translation: CAI22930.1.
BC025793 mRNA. Translation: AAH25793.1. Sequence problems.
BC116455 mRNA. Translation: AAI16456.1.
CCDSiCCDS31059.1. [Q5JTJ3-1]
CCDS55690.1. [Q5JTJ3-3]
RefSeqiNP_001013003.1. NM_001012985.2. [Q5JTJ3-1]
NP_001288662.1. NM_001301733.1. [Q5JTJ3-3]
UniGeneiHs.23198.

Genome annotation databases

EnsembliENST00000366612; ENSP00000355571; ENSG00000168275. [Q5JTJ3-3]
ENST00000366613; ENSP00000355572; ENSG00000168275. [Q5JTJ3-1]
ENST00000619305; ENSP00000479686; ENSG00000168275. [Q5JTJ3-3]
GeneIDi388753.
KEGGihsa:388753.
UCSCiuc001hwc.4. human. [Q5JTJ3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

LOVD-Leiden Open Variation Database

cytochrome c oxidase assembly factor 6 homolog (S. cerevisiae) (COA6)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL355472 Genomic DNA. Translation: CAI22928.1.
AL355472 Genomic DNA. Translation: CAI22929.1.
AL355472 Genomic DNA. Translation: CAI22930.1.
BC025793 mRNA. Translation: AAH25793.1. Sequence problems.
BC116455 mRNA. Translation: AAI16456.1.
CCDSiCCDS31059.1. [Q5JTJ3-1]
CCDS55690.1. [Q5JTJ3-3]
RefSeqiNP_001013003.1. NM_001012985.2. [Q5JTJ3-1]
NP_001288662.1. NM_001301733.1. [Q5JTJ3-3]
UniGeneiHs.23198.

3D structure databases

ProteinModelPortaliQ5JTJ3.
SMRiQ5JTJ3. Positions 43-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi132839. 2 interactions.
IntActiQ5JTJ3. 3 interactions.
STRINGi9606.ENSP00000355572.

PTM databases

iPTMnetiQ5JTJ3.
PhosphoSiteiQ5JTJ3.

Polymorphism and mutation databases

BioMutaiCOA6.
DMDMi74742178.

Proteomic databases

EPDiQ5JTJ3.
MaxQBiQ5JTJ3.
PaxDbiQ5JTJ3.
PRIDEiQ5JTJ3.

Protocols and materials databases

DNASUi388753.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366612; ENSP00000355571; ENSG00000168275. [Q5JTJ3-3]
ENST00000366613; ENSP00000355572; ENSG00000168275. [Q5JTJ3-1]
ENST00000619305; ENSP00000479686; ENSG00000168275. [Q5JTJ3-3]
GeneIDi388753.
KEGGihsa:388753.
UCSCiuc001hwc.4. human. [Q5JTJ3-1]

Organism-specific databases

CTDi388753.
GeneCardsiCOA6.
HGNCiHGNC:18025. COA6.
HPAiHPA028588.
MIMi614772. gene.
616501. phenotype.
neXtProtiNX_Q5JTJ3.
PharmGKBiPA25617.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3057. Eukaryota.
ENOG41121WM. LUCA.
GeneTreeiENSGT00390000004094.
HOGENOMiHOG000196422.
HOVERGENiHBG056284.
InParanoidiQ5JTJ3.
KOiK18179.
OMAiLLGDCGP.
OrthoDBiEOG74R1T7.
PhylomeDBiQ5JTJ3.
TreeFamiTF335992.

Miscellaneous databases

GenomeRNAii388753.
PROiQ5JTJ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ5JTJ3.
CleanExiHS_C1orf31.
ExpressionAtlasiQ5JTJ3. baseline and differential.
GenevisibleiQ5JTJ3. HS.

Family and domain databases

Gene3Di1.10.10.140. 1 hit.
InterProiIPR003213. Cyt_c_oxidase_su6B.
[Graphical view]
PfamiPF02297. COX6B. 1 hit.
[Graphical view]
SUPFAMiSSF47694. SSF47694. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Ovary and Testis.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Iterative orthology prediction uncovers new mitochondrial proteins and identifies C12orf62 as the human ortholog of COX14, a protein involved in the assembly of cytochrome c oxidase."
    Szklarczyk R., Wanschers B.F., Cuypers T.D., Esseling J.J., Riemersma M., van den Brand M.A., Gloerich J., Lasonder E., van den Heuvel L.P., Nijtmans L.G., Huynen M.A.
    Genome Biol. 13:RESEARCH0012.1-RESEARCH0012.14(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COA1.
  5. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 3), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Copper supplementation restores cytochrome c oxidase assembly defect in a mitochondrial disease model of COA6 deficiency."
    Ghosh A., Trivedi P.P., Timbalia S.A., Griffin A.T., Rahn J.J., Chan S.S., Gohil V.M.
    Hum. Mol. Genet. 23:3596-3606(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INVOLVEMENT IN CEMCOX4, VARIANT CEMCOX4 CYS-59.
  7. "Cooperation between COA6 and SCO2 in COX2 maturation during cytochrome c oxidase assembly links two mitochondrial cardiomyopathies."
    Pacheu-Grau D., Bareth B., Dudek J., Juris L., Voegtle F.N., Wissel M., Leary S.C., Dennerlein S., Rehling P., Deckers M.
    Cell Metab. 21:823-833(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MT-CO2 AND SCO2, CHARACTERIZATION OF VARIANT CEMCOX4 CYS-59.
  8. Cited for: FUNCTION, INTERACTION WITH SCO1.
  9. Cited for: SUBCELLULAR LOCATION, INVOLVEMENT IN CEMCOX4, VARIANT CEMCOX4 ARG-66.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCOA6_HUMAN
AccessioniPrimary (citable) accession number: Q5JTJ3
Secondary accession number(s): Q5JTJ2, Q5JTJ4, Q8TA88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: February 15, 2005
Last modified: June 8, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.