
uncoupling protein 1
Sign in to saveAlso known as mitochondrial brown fat uncoupling protein 1, uncoupling protein 1 (mitochondrial, proton carrier), solute carrier family 25 member 7, thermogenin, UCP1
Thermogenin (called uncoupling protein by its discoverers and now known as uncoupling protein 1, or UCP1) is a mitochondrial carrier protein found in brown adipose tissue (BAT). It is used to generate heat by non-shivering thermogenesis, and makes a quantitatively important contribution to countering heat loss in babies which would otherwise occur due to their high surface area-volume ratio. Recent findings indicate that the UCP1 protein plays a crucial role in thermogenesis by catalyzing the dissipative production of heat through protons derived from NADH and FADH2. These electron carriers ar
Protein · UniProt
Mitochondrial brown fat uncoupling protein 1
- Gene
- UCP1
- Organism
- Homo sapiens (Human)
- Length
- 307 aa
- Molecular mass
- 33,005 Da
- Evidence
- 1: Evidence at protein level
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 (By similarity). Functions as a long-chain fatty acid/LCFA and proton symporter, simultaneously transporting one LCFA and one proton through the inner mitochondrial membrane (PubMed:24196960, PubMed:28781081). However, LCFAs remaining associated with the transporter via their hydrophobic tails, it results in an apparent tra…
Swiss-Prot (reviewed) · via UniProt
Research
4,988 papers- Uncoupling Protein 1 Does Not Produce Heat without Activation.International journal of molecular sciences · 2022
- Structural mechanisms of mitochondrial uncoupling protein 1 regulation in thermogenesis.Trends in biochemical sciences · 2024
- Uncoupling Protein-1 Modulates Anxiety-Like Behavior in a Temperature-Dependent Manner.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
- Transcriptional regulation of the uncoupling protein-1 gene.Biochimie · 2017
- The cellular and functional complexity of thermogenic fat.Nature reviews. Molecular cell biology · 2021
via PubMed
Clinical Trials
5 registered- NACOMPLETEDThe Effects of Chronic Exercise on UCP1 Gene in Human White Adipose TissuePetros Dinas · NCT04039685
- NACOMPLETEDCold Induced Activation of Brown Adipose Tissue in HumansSusanna Søberg · NCT03096535
- NACOMPLETEDCold Induced Activation of Brown Adipose Tissue in Winter SwimmersRigshospitalet, Denmark · NCT03095846
- NAACTIVE_NOT_RECRUITINGWinter-Swimming and Brown Adipose Tissue Activity in Middel-aged Obese Subjects (WinterBAT).Kristian Karstoft · NCT03541096
- UNKNOWNChanges in Mitochondrial Uncoupling Protein 2 (UCP2) Messenger RNA(mRNA) in Type 2 Diabetes (T2DM) PatientsTel-Aviv Sourasky Medical Center · NCT01781754
~11 min read
Encyclopedic overview
10 sectionsContents
- Structure
- Mechanism
- HEAT cycle
- Evolution
- History
- Clinical relevance
- See also
- References
- Further reading
- External links
Thermogenin (called uncoupling protein by its discoverers and now known as uncoupling protein 1, or UCP1) is a mitochondrial carrier protein found in brown adipose tissue (BAT). It is used to generate heat by non-shivering thermogenesis, and makes a quantitatively important contribution to countering heat loss in babies which would otherwise occur due to their high surface area-volume ratio. Recent findings indicate that the UCP1 protein plays a crucial role in thermogenesis by catalyzing the dissipative production of heat through protons derived from NADH and FADH2. These electron carriers are produced in the TCA cycle from the oxidation of acetyl-CoA, which comes from the breakdown of free fatty acids. Intriguingly, the acetyl-CoA products undergo a recycling process that facilitates their re-utilization, thereby sustaining the cycle known as the HEAT cycle.
==Structure== thumb|left|Structure of the human uncoupling protein The atomic structure of human uncoupling protein 1 UCP1 has been solved by cryogenic-electron microscopy. The structure has the typical fold of a member of the SLC25 family. UCP1 is locked in a cytoplasmic-open state by guanosine triphosphate in a pH-dependent manner, preventing proton leak.
Excerpted from Wikipedia’s “uncoupling protein 1” article, available under the CC BY-SA 4.0 licence.