U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

COX4I1 cytochrome c oxidase subunit 4I1 [ Bos taurus (domestic cattle) ]

Gene ID: 281090, updated on 9-Feb-2026
Official Symbol
COX4I1provided by VGNC
Official Full Name
cytochrome c oxidase subunit 4I1provided by VGNC
Primary source
VGNC:VGNC:27634
See related
EnsemblRapid:ENSBTAG00070031594
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Bos taurus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Also known as
COX4
Orthologs
all
Try the new Gene page
Try the new Transcripts and proteins table
See COX4I1 in Genome Data Viewer
Location:
chromosome: 18
Exon count:
6
Annotation release Status Assembly Chr Location
RS_2024_12 current ARS-UCD2.0 (GCF_002263795.3) 18 NC_037345.1 (11758912..11767079)

Chromosome 18 - NC_037345.1Genomic Context describing neighboring genes Neighboring gene GINS complex subunit 2 Neighboring gene chromosome 18 C16orf74 homolog Neighboring gene ER membrane protein complex subunit 8 Neighboring gene interferon regulatory factor 8 Neighboring gene uncharacterized LOC132342790

Genomic Sequence:
NC_037345.1 Chromosome 18 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

  • Project title: Dominette sequence data
  • BioProject: PRJNA294306
  • Analysis date: Tue Dec 17 08:57:05 2024

Related articles in PubMed

  1. Structure of bovine cytochrome c oxidase crystallized at a neutral pH using a fluorinated detergent. Luo F, et al. Acta Crystallogr F Struct Biol Commun, 2017 Jul 1. PMID 28695851, Free PMC Article
  2. Studies on cytochrome c oxidase, V. Polypeptide IV: alignment and amino acid sequences on cyanogen bromide fragments. Sacher R, et al. Hoppe Seylers Z Physiol Chem, 1979 Oct. PMID 227779
  3. Studies on cytochrome c oxidase, VI. Polypeptide IV. the complete primary structure. Sacher R, et al. Hoppe Seylers Z Physiol Chem, 1979 Oct. PMID 227780
  4. Isolation and characterization of a cDNA clone for bovine cytochrome c oxidase subunit IV. Lomax MI, et al. Proc Natl Acad Sci U S A, 1984 Oct. PMID 6093095, Free PMC Article
  5. Cytochrome c oxidase: Intermediates of the catalytic cycle and their energy-coupled interconversion. Konstantinov AA. FEBS Lett, 2012 Mar 9. PMID 21889506

See all (24) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Structure of bovine cytochrome c oxidase crystallized at a neutral pH has been reported.
    Title: Structure of bovine cytochrome c oxidase crystallized at a neutral pH using a fluorinated detergent.
  2. Studies indicate that the patterns of charge translocation of cytochrome c oxidase coupled to transfer of the 3rd and 4th electrons are very similar.
    Title: Cytochrome c oxidase: Intermediates of the catalytic cycle and their energy-coupled interconversion.
  3. Studies indicate that time-resolved resonance Raman (RR) spectroscopy of whole mitochondria identified a band at 571cm(-1) arising from the oxygenated intermediate at Deltat=0.4, 0.6 and 1.4ms.
    Title: Resonance Raman applications in investigations of cytochrome c oxidase.
  4. Studies indicate that mutational amino acid replacement in proton channels, at the negative (N) side of membrane-inserted prokaryotic aa(3) oxidases, as well as Zn(2+) binding at this site in the bovine oxidase, uncouples proton pumping.
    Title: Allosteric interactions and proton conducting pathways in proton pumping aa(3) oxidases: heme a as a key coupling element.
  5. Studies indicate that X-ray structure of heart cytochrome c oxidase (CcO) suggest that O(2) molecules are transiently trapped at the Cu(B) site before binding to Fe(a3)(2+) to provide O(2)(-).
    Title: Structural studies on bovine heart cytochrome c oxidase.
  6. Studies indicate that nitric oxide (NO) binding to reduced ba(3) and bovine cytochrome aa3.
    Title: Kinetic studies of the reactions of O(2) and NO with reduced Thermus thermophilus ba(3) and bovine aa(3) using photolabile carriers.
  7. Studies indicate that photoexcitation of Ru (II) to Ru(II*) leads to rapid electron transfer to the ferric heme group in cytochrome c (Cc), followed by electron transfer to Cu(A) in cytochrome c oxidase (CcO) with a rate constant of 60,000s(-1).
    Title: Design of photoactive ruthenium complexes to study electron transfer and proton pumping in cytochrome oxidase.
  8. Studies suggest that the master-equation models address the question of how pumping can be achieved in a system in which all reaction steps are reversible.
    Title: Proton-pumping mechanism of cytochrome c oxidase: a kinetic master-equation approach.
  9. Studies suggest for the His291 model of proton pumping in cytochrome c oxidase (CcO).
    Title: Coupled electron and proton transfer reactions during the O→E transition in bovine cytochrome c oxidase.
Submit: New GeneRIF Correction

Markers

Homology

Gene Ontology Provided by RefSeq

Process Evidence Code Pubs
involved_in mitochondrial electron transport, cytochrome c to oxygen IEA
Inferred from Electronic Annotation
more info
 PubMed 
Preferred Names
cytochrome c oxidase subunit 4 isoform 1, mitochondrial
Names
COX IV-1
cytochrome c oxidase polypeptide IV
cytochrome c oxydase subunit 4
NP_001001439.1
XP_005218495.1

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001001439.3 → NP_001001439.1  cytochrome c oxidase subunit 4 isoform 1, mitochondrial precursor

    See identical proteins and their annotated locations for NP_001001439.1

    Status: PROVISIONAL

    Source sequence(s)
    BC102733
    UniProtKB/Swiss-Prot
    P00423, Q3SZS0, Q5E991
    UniProtKB/TrEMBL
    A0AAF6Z2H9
    Conserved Domains (1) summary
    pfam02936
    Location:36 → 168
    COX4; Cytochrome c oxidase subunit IV

RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2024_12

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference ARS-UCD2.0 Primary Assembly

Genomic

  1. NC_037345.1 Reference ARS-UCD2.0 Primary Assembly

    Range
    11758912..11767079
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_005218438.2 → XP_005218495.1  cytochrome c oxidase subunit 4 isoform 1, mitochondrial isoform X1

    See identical proteins and their annotated locations for XP_005218495.1

    UniProtKB/Swiss-Prot
    P00423, Q3SZS0, Q5E991
    UniProtKB/TrEMBL
    A0AAF6Z2H9
    Related
    ENSBTAP00070043594.1, ENSBTAT00070071431.1
    Conserved Domains (1) summary
    pfam02936
    Location:36 → 168
    COX4; Cytochrome c oxidase subunit IV
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P00423.1 GenPept UniProtKB/Swiss-Prot:P00423

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.