Specific sequence of motifs of mitochondrial uncoupling proteins
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
10772343
DOI
10.1080/713803586
Knihovny.cz E-resources
- MeSH
- Amino Acid Motifs MeSH
- Fungal Proteins chemistry MeSH
- Ion Channels MeSH
- Conserved Sequence MeSH
- Cricetinae MeSH
- Rats MeSH
- Humans MeSH
- Membrane Proteins chemistry metabolism MeSH
- Membrane Transport Proteins * MeSH
- Mitochondrial Uncoupling Proteins MeSH
- Mitochondrial Proteins * MeSH
- Molecular Sequence Data MeSH
- Mice MeSH
- Nerve Tissue Proteins chemistry MeSH
- Proteins chemistry MeSH
- Plant Proteins chemistry MeSH
- Protein Folding MeSH
- Protein Structure, Secondary MeSH
- Amino Acid Sequence MeSH
- Sequence Homology, Amino Acid MeSH
- Cattle MeSH
- Protein Structure, Tertiary MeSH
- Mitochondrial Membrane Transport Proteins MeSH
- Carrier Proteins chemistry metabolism MeSH
- Uncoupling Protein 1 MeSH
- Uncoupling Protein 2 MeSH
- Binding Sites MeSH
- Animals MeSH
- Check Tag
- Cricetinae MeSH
- Rats MeSH
- Humans MeSH
- Mice MeSH
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Fungal Proteins MeSH
- Ion Channels MeSH
- Membrane Proteins MeSH
- Membrane Transport Proteins * MeSH
- Mitochondrial Uncoupling Proteins MeSH
- Mitochondrial Proteins * MeSH
- Nerve Tissue Proteins MeSH
- Proteins MeSH
- Plant Proteins MeSH
- SLC25A14 protein, human MeSH Browser
- Slc25a14 protein, mouse MeSH Browser
- Slc25a14 protein, rat MeSH Browser
- Mitochondrial Membrane Transport Proteins MeSH
- Carrier Proteins MeSH
- UCP1 protein, human MeSH Browser
- Ucp1 protein, mouse MeSH Browser
- Ucp1 protein, rat MeSH Browser
- UCP2 protein, human MeSH Browser
- Ucp2 protein, mouse MeSH Browser
- Ucp2 protein, rat MeSH Browser
- Uncoupling Protein 1 MeSH
- Uncoupling Protein 2 MeSH
We have searched for the exclusivity of common sequence motifs of the mitochondrial uncoupling proteins (UCP1, UCP2, UCP3, UCP4, BMCP1, and plant UCP [PUMP]) within the gene family of mitochondrial anion carrier proteins. The UCP-specific sequences, "UCP signatures", were found in the first, second, and fourth alpha-helices. First: Ala/Ser-Cys/Thr/n-n/Phe-Ala/Gly-[negatively charged residue]-n/Phe-n/Cys-Thr-Phe/n; second: Gly/Ala-Ile/Leu-Gln/X-[positively charged residue]-NH-n/Cys-Ser/nphi/X-n/Ser-OH/Gly-n-[positively charged residue]-Ile/Met-Gly/Val-n/Thr; fourth: Pro-Asn/ Thr-n-X-[positively charged residue]-Asn/Ser/Ala-n-n-Ile/Leu-n-Asn/Val-Cys/n-n/Thr-[negatively charged residue]-n-n/Thr/Pro-OH/Val (n, nonpolar; phi, aromatic; (positively charged residue/negatively charged residue, charged residue). The second and part of the third signature are also present in the yeast dicarboxylate transporter. The UCP signature excluding BMCP1 was also found in the second matrix segment: [positively charged residue]-(Pro/ del-Leu/del)-[positively charged residue]-phi-X-Gly/Ser-Thr/n-X-NH/[negatively charged residue]-Ala-phi. These UCP signatures are thought to be involved in fatty acid anion binding and translocation.
References provided by Crossref.org
Mitochondrial Uncoupling Proteins: Subtle Regulators of Cellular Redox Signaling
