SLC25A27: Difference between revisions

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{{Infobox_gene}}
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'''Mitochondrial uncoupling protein 4''' is a [[protein]] that in humans is encoded by the ''SLC25A27'' [[gene]].<ref name="pmid10025957">{{cite journal | vauthors = Mao W, Yu XX, Zhong A, Li W, Brush J, Sherwood SW, Adams SH, Pan G | title = UCP4, a novel brain-specific mitochondrial protein that reduces membrane potential in mammalian cells | journal = FEBS Lett | volume = 443 | issue = 3 | pages = 326–30 |date=Mar 1999 | pmid = 10025957 | pmc =  | doi =10.1016/S0014-5793(98)01713-X  }}</ref><ref name="pmid10772343">{{cite journal | vauthors = Jezek P, Urbankova E | title = Specific sequence of motifs of mitochondrial uncoupling proteins | journal = IUBMB Life | volume = 49 | issue = 1 | pages = 63–70 |date=Jun 2000 | pmid = 10772343 | pmc = | doi = 10.1080/713803586 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SLC25A27 solute carrier family 25, member 27| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9481| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Solute carrier family 25, member 27
| HGNCid = 21065
| Symbol = SLC25A27
| AltSymbols =; FLJ33552; UCP4
| OMIM = 
| ECnumber = 
| Homologene = 12523
| MGIid = 1921261
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005488 |text = binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006839 |text = mitochondrial transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9481
    | Hs_Ensembl = ENSG00000153291
    | Hs_RefseqProtein = NP_004268
    | Hs_RefseqmRNA = NM_004277
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 46728637
    | Hs_GenLoc_end = 46757267
    | Hs_Uniprot = O95847
    | Mm_EntrezGene = 74011
    | Mm_Ensembl = ENSMUSG00000023912
    | Mm_RefseqmRNA = NM_028711
    | Mm_RefseqProtein = NP_082987
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 43104955
    | Mm_GenLoc_end = 43130237
    | Mm_Uniprot = 
  }}
}}
'''Solute carrier family 25, member 27''', also known as '''SLC25A27''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC25A27 solute carrier family 25, member 27| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9481| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Mitochondrial uncoupling proteins (UCP) are members of the larger family of mitochondrial anion carrier proteins (MACP). UCPs separate oxidative phosphorylation from ATP synthesis with energy dissipated 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. Tissue specificity occurs for the different UCPs and the exact methods of how UCPs transfer H+/OH- are not known. UCPs contain the three homologous protein domains of MACPs. Transcripts of this gene are detected only in brain tissue and are specifically modulated by various environmental conditions.<ref name="entrez"/> Recently, the proton transport activity of UCP4 has also been shown to be activated by fatty acids and inhibited by purine nucleotides.<ref name="pmid22524567">{{cite journal | vauthors = Hoang T, Smith MD, Jelokhani-Niaraki M | title = Toward Understanding the Mechanism of Ion Transport Activity of Neuronal Uncoupling Proteins UCP2, UCP4, and UCP5 | journal = Biochemistry | volume = 51 | issue = 19 | pages = 4004–14 | year = 2012 | pmid = 22524567 | doi = 10.1021/bi3003378| url = http://pubs.acs.org/doi/abs/10.1021/bi3003378 }}</ref> In addition, reconstituted UCP4 exhibited a distinct conformation, compared to other UCPs in the family.<ref name="pmid20000716">{{cite journal | vauthors = Ivanova M, Hoang T, McSorly FR, Krnac G, Smith MD, Jelokhani-Niaraki M | title = A comparative study on conformation and ligand binding of the neuronal uncoupling proteins | journal = Biochemistry | volume = 49 | issue = 3 | pages = 512–21 | year = 2010 | pmid = 20000716 | doi = 10.1021/bi901742g| url = http://pubs.acs.org/doi/abs/10.1021/bi901742g }}</ref>
{{PBB_Summary
| section_title =
| summary_text = Mitochondrial uncoupling proteins (UCP) are members of the larger family of mitochondrial anion carrier proteins (MACP). UCPs separate oxidative phosphorylation from ATP synthesis with energy dissipated 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. Tissue specificity occurs for the different UCPs and the exact methods of how UCPs transfer H+/OH- are not known. UCPs contain the three homologous protein domains of MACPs. Transcripts of this gene are only detected in brain tissue and are specifically modulated by various environmental conditions.<ref name="entrez">{{cite web | title = Entrez Gene: SLC25A27 solute carrier family 25, member 27| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9481| accessdate = }}</ref>
}}


==See also==
==See also==
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==References==
==References==
{{reflist|2}}
{{reflist}}


==Further reading==
==Further reading==
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{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Ricquier D, Bouillaud F |title=The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP. |journal=Biochem. J. |volume=345 Pt 2 |issue=  |pages= 161-79 |year= 2000 |pmid= 10620491 |doi=  }}
*{{cite journal  | vauthors=Ricquier D, Bouillaud F |title=The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP. |journal=Biochem. J. |volume=345 |issue=  2|pages= 161–79 |year= 2000 |pmid= 10620491 |doi=10.1042/0264-6021:3450161  | pmc=1220743 }}
*{{cite journal  | author=Muzzin P |title=The uncoupling proteins. |journal=Ann. Endocrinol. (Paris) |volume=63 |issue= 2 Pt 1 |pages= 106-10 |year= 2002 |pmid= 11994670 |doi=  }}
*{{cite journal  | author=Muzzin P |title=The uncoupling proteins. |journal=Ann. Endocrinol. |location = Paris |volume=63 |issue= 2 Pt 1 |pages= 106–10 |year= 2002 |pmid= 11994670 |doi=  }}
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal  | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
*{{cite journal  | author=Mao W, Yu XX, Zhong A, ''et al.'' |title=UCP4, a novel brain-specific mitochondrial protein that reduces membrane potential in mammalian cells. |journal=FEBS Lett. |volume=443 |issue= 3 |pages= 326-30 |year= 1999 |pmid= 10025957 |doi=  }}
*{{cite journal   |vauthors=Yu XX, Mao W, Zhong A, etal |title=Characterization of novel UCP5/BMCP1 isoforms and differential regulation of UCP4 and UCP5 expression through dietary or temperature manipulation. |journal=FASEB J. |volume=14 |issue= 11 |pages= 1611–8 |year= 2000 |pmid= 10928996 |doi=10.1096/fj.14.11.1611 }}
*{{cite journal  | author=Jezek P, Urbánková E |title=Specific sequence of motifs of mitochondrial uncoupling proteins. |journal=IUBMB Life |volume=49 |issue= 1 |pages= 63-70 |year= 2000 |pmid= 10772343 |doi= }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Yu XX, Mao W, Zhong A, ''et al.'' |title=Characterization of novel UCP5/BMCP1 isoforms and differential regulation of UCP4 and UCP5 expression through dietary or temperature manipulation. |journal=FASEB J. |volume=14 |issue= 11 |pages= 1611-8 |year= 2000 |pmid= 10928996 |doi=  }}
*{{cite journal   |vauthors=Clark HF, Gurney AL, Abaya E, etal |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265–70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 | pmc=403697 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal   |vauthors=Liu D, Chan SL, de Souza-Pinto NC, etal |title=Mitochondrial UCP4 mediates an adaptive shift in energy metabolism and increases the resistance of neurons to metabolic and oxidative stress. |journal=Neuromolecular Med. |volume=8 |issue= 3 |pages= 389–414 |year= 2007 |pmid= 16775390 |doi=10.1385/NMM:8:3:389 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal   |vauthors=Chan SL, Liu D, Kyriazis GA, etal |title=Mitochondrial uncoupling protein-4 regulates calcium homeostasis and sensitivity to store depletion-induced apoptosis in neural cells. |journal=J. Biol. Chem. |volume=281 |issue= 49 |pages= 37391–403 |year= 2007 |pmid= 17035241 |doi= 10.1074/jbc.M605552200 }}
*{{cite journal | author=Liu D, Chan SL, de Souza-Pinto NC, ''et al.'' |title=Mitochondrial UCP4 mediates an adaptive shift in energy metabolism and increases the resistance of neurons to metabolic and oxidative stress. |journal=Neuromolecular Med. |volume=8 |issue= 3 |pages= 389-414 |year= 2007 |pmid= 16775390 |doi=  }}
*{{cite journal   |vauthors=Yasuno K, Ando S, Misumi S, etal |title=Synergistic association of mitochondrial uncoupling protein (UCP) genes with schizophrenia. |journal=Am. J. Med. Genet. B Neuropsychiatr. Genet. |volume=144 |issue= 2 |pages= 250–3 |year= 2007 |pmid= 17066476 |doi= 10.1002/ajmg.b.30443 }}
*{{cite journal | author=Chan SL, Liu D, Kyriazis GA, ''et al.'' |title=Mitochondrial uncoupling protein-4 regulates calcium homeostasis and sensitivity to store depletion-induced apoptosis in neural cells. |journal=J. Biol. Chem. |volume=281 |issue= 49 |pages= 37391-403 |year= 2007 |pmid= 17035241 |doi= 10.1074/jbc.M605552200 }}
*{{cite journal  |vauthors=Ho PW, Ho JW, Tse HM, etal |title=Uncoupling protein-4 (UCP4) increases ATP supply by interacting with mitochondrial Complex II in neuroblastoma cells. |journal=PLOS ONE |volume=7 |issue= 2 |pages= e32810 |year= 2012 |pmid= 22427795 |doi= 10.1371/journal.pone.0032810 |pmc=3303587}}
*{{cite journal | author=Yasuno K, Ando S, Misumi S, ''et al.'' |title=Synergistic association of mitochondrial uncoupling protein (UCP) genes with schizophrenia. |journal=Am. J. Med. Genet. B Neuropsychiatr. Genet. |volume=144 |issue= 2 |pages= 250-3 |year= 2007 |pmid= 17066476 |doi= 10.1002/ajmg.b.30443 }}
*{{cite journal  |vauthors=Ho JW, Ho PW, Liu HF, etal |title=UCP4 is a target effector of the NF-κB c-Rel prosurvival pathway against oxidative stress. |journal=Free Radic Biol Med |volume=53 |issue= 2 |pages= 383–394 |year= 2012 |pmid= 22580300 |doi= 10.1016/j.freeradbiomed.2012.05.002 }}
}}
}}
{{refend}}
{{refend}}


{{membrane-protein-stub}}
{{NLM content}}
{{NLM content}}
{{Membrane transport proteins}}
{{Membrane transport proteins}}
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[[Category:Solute carrier family]]
[[Category:Solute carrier family]]


[[ca:UCP4]]
 
{{WikiDoc Sources}}
{{membrane-protein-stub}}

Latest revision as of 20:58, 27 March 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Mitochondrial uncoupling protein 4 is a protein that in humans is encoded by the SLC25A27 gene.[1][2][3]


Mitochondrial uncoupling proteins (UCP) are members of the larger family of mitochondrial anion carrier proteins (MACP). UCPs separate oxidative phosphorylation from ATP synthesis with energy dissipated 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. Tissue specificity occurs for the different UCPs and the exact methods of how UCPs transfer H+/OH- are not known. UCPs contain the three homologous protein domains of MACPs. Transcripts of this gene are detected only in brain tissue and are specifically modulated by various environmental conditions.[3] Recently, the proton transport activity of UCP4 has also been shown to be activated by fatty acids and inhibited by purine nucleotides.[4] In addition, reconstituted UCP4 exhibited a distinct conformation, compared to other UCPs in the family.[5]

See also

References

  1. Mao W, Yu XX, Zhong A, Li W, Brush J, Sherwood SW, Adams SH, Pan G (Mar 1999). "UCP4, a novel brain-specific mitochondrial protein that reduces membrane potential in mammalian cells". FEBS Lett. 443 (3): 326–30. doi:10.1016/S0014-5793(98)01713-X. PMID 10025957.
  2. Jezek P, Urbankova E (Jun 2000). "Specific sequence of motifs of mitochondrial uncoupling proteins". IUBMB Life. 49 (1): 63–70. doi:10.1080/713803586. PMID 10772343.
  3. 3.0 3.1 "Entrez Gene: SLC25A27 solute carrier family 25, member 27".
  4. Hoang T, Smith MD, Jelokhani-Niaraki M (2012). "Toward Understanding the Mechanism of Ion Transport Activity of Neuronal Uncoupling Proteins UCP2, UCP4, and UCP5". Biochemistry. 51 (19): 4004–14. doi:10.1021/bi3003378. PMID 22524567.
  5. Ivanova M, Hoang T, McSorly FR, Krnac G, Smith MD, Jelokhani-Niaraki M (2010). "A comparative study on conformation and ligand binding of the neuronal uncoupling proteins". Biochemistry. 49 (3): 512–21. doi:10.1021/bi901742g. PMID 20000716.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.