P10861 · UCP1_BOVIN
- ProteinMitochondrial brown fat uncoupling protein 1
- GeneUCP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids309 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates in non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance. Functions as a long-chain fatty acid/LCFA and proton symporter, simultaneously transporting one LCFA and one proton through the inner mitochondrial membrane. However, LCFAs remaining associated with the transporter via their hydrophobic tails, it results in an apparent transport of protons activated by LCFAs. Thereby, dissipates the mitochondrial proton gradient and converts the energy of substrate oxydation into heat instead of ATP. Regulates the production of reactive oxygen species/ROS by mitochondria.
Catalytic activity
- H+(in) = H+(out)
Activity regulation
Has no constitutive proton transporter activity and has to be activated by long-chain fatty acids/LCFAs. Inhibited by purine nucleotides. Both purine nucleotides and LCFAs bind the cytosolic side of the transporter and directly compete to activate or inhibit it. Activated by noradrenaline and reactive oxygen species. Despite lacking canonical translational encoding for selenocysteine, a small pool of the protein has been observed to selectively incorporate selenocysteine at 'Cys-256'. Selenocysteine-modified protein is highly sensitive to redox modification and may constitute a pool of protein highly sensitive to activation by elevated levels of reactive oxygen species (ROS).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 60 | fatty acid 16:0 (UniProtKB | ChEBI) | |||
Binding site | 271 | fatty acid 16:0 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Molecular Function | cardiolipin binding | |
Molecular Function | long-chain fatty acid binding | |
Molecular Function | oxidative phosphorylation uncoupler activity | |
Molecular Function | purine ribonucleotide binding | |
Biological Process | adaptive thermogenesis | |
Biological Process | cellular response to fatty acid | |
Biological Process | cellular response to hormone stimulus | |
Biological Process | cellular response to reactive oxygen species | |
Biological Process | mitochondrial transmembrane transport | |
Biological Process | proton transmembrane transport | |
Biological Process | regulation of reactive oxygen species biosynthetic process | |
Biological Process | response to cold | |
Biological Process | response to nutrient levels | |
Biological Process | response to temperature stimulus |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMitochondrial brown fat uncoupling protein 1
- Short namesUCP 1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP10861
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Topological domain | 2-10 | Mitochondrial intermembrane | |||
Transmembrane | 11-32 | Helical; Name=1 | |||
Topological domain | 33-77 | Mitochondrial matrix | |||
Transmembrane | 78-100 | Helical; Name=2 | |||
Topological domain | 101-118 | Mitochondrial intermembrane | |||
Transmembrane | 119-135 | Helical; Name=3 | |||
Topological domain | 136-180 | Mitochondrial matrix | |||
Transmembrane | 181-197 | Helical; Name=4 | |||
Topological domain | 198-214 | Mitochondrial intermembrane | |||
Transmembrane | 215-234 | Helical; Name=5 | |||
Topological domain | 235-268 | Mitochondrial matrix | |||
Transmembrane | 269-291 | Helical; Name=6 | |||
Topological domain | 292-309 | Mitochondrial intermembrane | |||
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000090654 | 1-309 | Mitochondrial brown fat uncoupling protein 1 | ||
Modified residue | 256 | Cysteine sulfenic acid (-SOH) | |||
Post-translational modification
May undergo sulfenylation upon cold exposure. May increase the sensitivity of UCP1 thermogenic function to the activation by noradrenaline probably through structural effects.
May undergo ubiquitin-mediated proteasomal degradation.
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Most probably functions as a monomer. Binds one purine nucleotide per monomer. However, has also been suggested to function as a homodimer or a homotetramer. Tightly associates with cardiolipin in the mitochondrion inner membrane; may stabilize and regulate its activity.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for repeat.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Repeat | 11-106 | Solcar 1 | |||
Repeat | 113-203 | Solcar 2 | |||
Repeat | 212-297 | Solcar 3 | |||
Sequence similarities
Belongs to the mitochondrial carrier (TC 2.A.29) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length309
- Mass (Da)33,360
- Last updated2016-11-02 v3
- MD5 ChecksumBAB4BE70A5D7067EB374A3D95B6AE9E4
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 43-46 | in Ref. 2; CAA32227 | |||
Sequence conflict | 92 | in Ref. 2; CAA32227 | |||
Sequence conflict | 180 | in Ref. 2; CAA32227 | |||
Sequence conflict | 185 | in Ref. 2; CAA32227 | |||
Sequence conflict | 250 | in Ref. 2; CAA32227 | |||
Sequence conflict | 285 | in Ref. 2; CAA32227 | |||
Sequence conflict | 293 | in Ref. 2; CAA32227 | |||
Sequence conflict | 301 | in Ref. 2; CAA32227 | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DAAA02044420 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
DAAA02044421 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
X14064 EMBL· GenBank· DDBJ | CAA32227.1 EMBL· GenBank· DDBJ | mRNA |