UCP2

Protein-coding gene in the species Homo sapiens
UCP2
Identifiers
AliasesUCP2, BMIQ4, SLC25A8, UCPH, uncoupling protein 2
External IDsOMIM: 601693; MGI: 109354; HomoloGene: 2516; GeneCards: UCP2; OMA:UCP2 - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for UCP2
Genomic location for UCP2
Band11q13.4Start73,974,672 bp[1]
End73,983,246 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for UCP2
Genomic location for UCP2
Band7 E2|7 54.36 cMStart100,142,544 bp[2]
End100,151,227 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • granulocyte

  • bronchial epithelial cell

  • right uterine tube

  • spleen

  • epithelium of nasopharynx

  • appendix

  • blood

  • trabecular bone

  • nasal epithelium

  • palpebral conjunctiva
Top expressed in
  • blood

  • epithelium of stomach

  • granulocyte

  • lip

  • pyloric antrum

  • fetal liver hematopoietic progenitor cell

  • mucous cell of stomach

  • tibiofemoral joint

  • molar

  • mesenteric lymph nodes
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • protein binding
  • oxidative phosphorylation uncoupler activity
  • transmembrane transporter activity
Cellular component
  • cytoplasm
  • membrane
  • mitochondrial membranes
  • mitochondrial inner membrane
  • integral component of membrane
  • mitochondrion
Biological process
  • positive regulation of cell death
  • response to hypoxia
  • response to superoxide
  • response to fatty acid
  • female pregnancy
  • cellular response to amino acid starvation
  • negative regulation of insulin secretion involved in cellular response to glucose stimulus
  • human ageing
  • negative regulation of apoptotic process
  • response to glucose
  • regulation of mitochondrial membrane potential
  • liver regeneration
  • cellular response to hormone stimulus
  • cellular response to insulin stimulus
  • cellular response to glucose stimulus
  • response to cold
  • mitochondrial transmembrane transport
  • adaptive thermogenesis
  • mitochondrial transport
  • proton transmembrane transport
  • positive regulation of cold-induced thermogenesis
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7351

22228

Ensembl

ENSG00000175567

ENSMUSG00000033685

UniProt

P55851

P70406

RefSeq (mRNA)

NM_003355

NM_011671

RefSeq (protein)
NP_003346
NP_001368872
NP_001368873
NP_001368874
NP_001368876

NP_001368877
NP_001368878
NP_001368879

NP_035801

Location (UCSC)Chr 11: 73.97 – 73.98 MbChr 7: 100.14 – 100.15 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Mitochondrial uncoupling protein 2 is a protein that in humans is encoded by the UCP2 gene.[5]

Mitochondrial uncoupling proteins (UCP) are members of the larger family of mitochondrial anion carrier proteins (MACP). UCPs separate, or uncouple, oxidative phosphorylation from ATP synthesis by dissipating the mitochondrial membrane potential as heat, also referred to as the mitochondrial proton leak. UCPs facilitate the transfer of anions from the inner to the outer mitochondrial membrane and the return transfer of protons from the outer to the inner mitochondrial membrane. They also reduce the mitochondrial membrane potential in mammalian cells, which reduces production of reactive oxygen species (ROS).

In contrast to UCP1 and UCP3, which are primarily expressed in adipose and smooth muscle, UCP2 is expressed on many different tissues[6] including the kidney, liver, GI tract, brain, and skeletal muscle.

The exact mechanisms of anion transfer by UCPs are not known.[7] UCPs contain the three homologous protein domains of MACPs. Although it was originally thought to play a role in non-shivering thermogenesis, obesity, diabetes and atherosclerosis, it now appears that the main function of UCP2 is the control of mitochondria-derived reactive oxygen species.[8]

Chromosomal order is 5'-UCP3-UCP2-3'.[9]

Mitochondrial Uncoupling Protein 2

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000175567 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033685 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Vidal-Puig A, Solanes G, Grujic D, Flier JS, Lowell BB (Jul 1997). "UCP3: an uncoupling protein homologue expressed preferentially and abundantly in skeletal muscle and brown adipose tissue". Biochem Biophys Res Commun. 235 (1): 79–82. doi:10.1006/bbrc.1997.6740. PMID 9196039.
  6. ^ "Tissue expression of UCP2 - Summary - The Human Protein Atlas". www.proteinatlas.org. Retrieved 2020-08-20.
  7. ^ Garlid, Keith D.; Jabůrek, Martin; Ježek, Petr; Vařecha, Miroslav (2000-08-15). "How do uncoupling proteins uncouple?". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1459 (2–3): 383–389. doi:10.1016/S0005-2728(00)00175-4. ISSN 0005-2728. PMID 11004454.
  8. ^ Arsenijevic D, Onuma H, Pecqueur C, et al. (December 2000). "Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production". Nat. Genet. 26 (4): 435–9. doi:10.1038/82565. PMID 11101840. S2CID 29831657.
  9. ^ "Entrez Gene: UCP2 uncoupling protein 2 (mitochondrial, proton carrier)".

Further reading

  • Ricquier D, Bouillaud F (2000). "The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP". Biochem. J. 345 (2): 161–79. doi:10.1042/0264-6021:3450161. PMC 1220743. PMID 10620491.
  • Saleh MC, Wheeler MB, Chan CB (2002). "Uncoupling protein-2: evidence for its function as a metabolic regulator". Diabetologia. 45 (2): 174–87. doi:10.1007/s00125-001-0737-x. PMID 11935148.
  • Muzzin P (2002). "The uncoupling proteins". Ann. Endocrinol. 63 (2 Pt 1): 106–10. PMID 11994670.
  • Horvath TL, Diano S, Barnstable C (2003). "Mitochondrial uncoupling protein 2 in the central nervous system: neuromodulator and neuroprotector". Biochem. Pharmacol. 65 (12): 1917–21. doi:10.1016/S0006-2952(03)00143-6. PMID 12787871.
  • Paradis E, Clavel S, Bouillaud F, et al. (2004). "Uncoupling protein 2: a novel player in neuroprotection". Trends in Molecular Medicine. 9 (12): 522–5. doi:10.1016/j.molmed.2003.10.009. PMID 14659466.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Fleury C, Neverova M, Collins S, et al. (1997). "Uncoupling protein-2: a novel gene linked to obesity and hyperinsulinemia". Nat. Genet. 15 (3): 269–72. doi:10.1038/ng0397-269. PMID 9054939. S2CID 13421247.
  • Gimeno RE, Dembski M, Weng X, et al. (1997). "Cloning and characterization of an uncoupling protein homolog: a potential molecular mediator of human thermogenesis". Diabetes. 46 (5): 900–6. doi:10.2337/diabetes.46.5.900. PMID 9133562.
  • Boss O, Samec S, Paoloni-Giacobino A, et al. (1997). "Uncoupling protein-3: a new member of the mitochondrial carrier family with tissue-specific expression". FEBS Lett. 408 (1): 39–42. doi:10.1016/S0014-5793(97)00384-0. PMID 9180264. S2CID 33808140.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Hodný Z, Kolárová P, Rossmeisl M, et al. (1998). "High expression of uncoupling protein 2 in foetal liver". FEBS Lett. 425 (2): 185–90. doi:10.1016/S0014-5793(98)00230-0. PMID 9559644. S2CID 35050170.
  • Argyropoulos G, Brown AM, Peterson R, et al. (1998). "Structure and organization of the human uncoupling protein 2 gene and identification of a common biallelic variant in Caucasian and African-American subjects". Diabetes. 47 (4): 685–7. doi:10.2337/diabetes.47.4.685. PMID 9568704. S2CID 38803735.
  • Tu N, Chen H, Winnikes U, et al. (1999). "Structural organization and mutational analysis of the human uncoupling protein-2 (hUCP2) gene". Life Sci. 64 (3): PL41–50. doi:10.1016/S0024-3205(98)00555-4. PMID 10027754.
  • Pecqueur C, Cassard-Doulcier AM, Raimbault S, et al. (1999). "Functional organization of the human uncoupling protein-2 gene, and juxtaposition to the uncoupling protein-3 gene". Biochem. Biophys. Res. Commun. 255 (1): 40–6. doi:10.1006/bbrc.1998.0146. PMID 10082652.
  • Jezek P, Urbánková E (2000). "Specific sequence of motifs of mitochondrial uncoupling proteins". IUBMB Life. 49 (1): 63–70. doi:10.1080/713803586. PMID 10772343. S2CID 8541209.
  • Pierrat B, Ito M, Hinz W, et al. (2000). "Uncoupling proteins 2 and 3 interact with members of the 14.3.3 family". Eur. J. Biochem. 267 (9): 2680–7. doi:10.1046/j.1432-1327.2000.01285.x. PMID 10785390.
  • Esterbauer H, Schneitler C, Oberkofler H, et al. (2001). "A common polymorphism in the promoter of UCP2 is associated with decreased risk of obesity in middle-aged humans". Nat. Genet. 28 (2): 178–83. doi:10.1038/88911. PMID 11381268. S2CID 29550924.
  • Echtay KS, Roussel D, St-Pierre J, et al. (2002). "Superoxide activates mitochondrial uncoupling proteins". Nature. 415 (6867): 96–9. Bibcode:2002Natur.415...96E. doi:10.1038/415096a. PMID 11780125. S2CID 4349744.
  • Rupprecht A, Sittner D, Smorodchenko A, Hilse KE, Goyn J, Moldzio R, Seiler AE, Bräuer AU, Pohl EE (2014). "Uncoupling protein 2 and 4 expression pattern during stem cell differentiation provides new insight into their putative function". PLOS ONE. 9 (2): e88474. Bibcode:2014PLoSO...988474R. doi:10.1371/journal.pone.0088474. PMC 3921169. PMID 24523901.
  • Rupprecht A, Bräuer AU, Smorodchenko A, Goyn J, Hilse KE, Shabalina IG, Infante-Duarte C, Pohl EE (2012). "Quantification of uncoupling protein 2 reveals its main expression in immune cells and selective up-regulation during T-cell proliferation". PLOS ONE. 7 (8): e41406. Bibcode:2012PLoSO...741406R. doi:10.1371/journal.pone.0041406. PMC 3411681. PMID 22870219.
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By group
SLC1–10
(1):
(2):
(3):
(4):
(5):
(6):
(7):
(8):
  • Na+/Ca2+ exchanger
(9):
(10):
SLC11–20
(11):
(12):
(13):
(14):
(15):
(16):
(17):
(18):
(19):
(20):
SLC21–30
(21):
(22):
(23):
  • Na+-dependent ascorbic acid transporter
(24):
  • Na+/(Ca2+-K+) exchanger
(25):
(26):
(27):
(28):
(29):
(30):
SLC31–40
(31):
(32):
(33):
(34):
(35):
(36):
(37):
(38):
(39):
(40):
  • basolateral iron transporter
SLC41–48
(41):
(42):
(43):
  • Na+-independent, system-L like amino-acid transporter
(44):
(45):
(46):
(47):
(48):
SLCO1–4
Symporter, Cotransporter
  • Na+/K+,Cl−
  • Na+/Pi3
  • Na+/Cl−
  • Na+/glucose
  • Na+/I−
  • Cl−/K+
Antiporter (exchanger)
  • Na+/H+
  • Na+/Ca2+
    • Na+/(Ca2+-K+) - Cl−/HCO−
      3       (Band 3)
  • Cl−-formate
  • Cl−-oxalate
see also solute carrier disorders


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