Mitochondrial brown fat uncoupling protein 1

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• cardiolipin binding Source: UniProtKB
• GDP binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.10

    "Fatty acids change the conformation of uncoupling protein 1 (UCP1)."
    Divakaruni A.S., Humphrey D.M., Brand M.D.
    J. Biol. Chem. 287:36845-36853(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: ACTIVITY REGULATION, PURINE NUCLEOTIDE-BINDING.
• GTP binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "Substitutional mutations in the uncoupling protein-specific sequences of mitochondrial uncoupling protein UCP1 lead to the reduction of fatty acid-induced H+ uniport."
    Urbankova E., Hanak P., Skobisova E., Ruzicka M., Jezek P.
    Int. J. Biochem. Cell Biol. 35:212-220(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, GTP-BINDING, MUTAGENESIS OF CYS-25; ASP-28; THR-31; HIS-146; HIS-148 AND ARG-153.
• long-chain fatty acid binding Source: UniProtKB
• oxidative phosphorylation uncoupler activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "Fatty acids change the conformation of uncoupling protein 1 (UCP1)."
    Divakaruni A.S., Humphrey D.M., Brand M.D.
    J. Biol. Chem. 287:36845-36853(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: ACTIVITY REGULATION, PURINE NUCLEOTIDE-BINDING.
• purine ribonucleotide binding Source: RGDInferred from sequence orthologyⁱ
  • "Mechanism of fatty-acid-dependent UCP1 uncoupling in brown fat mitochondria."
    Fedorenko A., Lishko P.V., Kirichok Y.
    Cell 151:400-413(2012) [PubMed] [Europe PMC] [Abstract]
• transmembrane transporter activity Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.7

    "Substitutional mutations in the uncoupling protein-specific sequences of mitochondrial uncoupling protein UCP1 lead to the reduction of fatty acid-induced H+ uniport."
    Urbankova E., Hanak P., Skobisova E., Ruzicka M., Jezek P.
    Int. J. Biochem. Cell Biol. 35:212-220(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, GTP-BINDING, MUTAGENESIS OF CYS-25; ASP-28; THR-31; HIS-146; HIS-148 AND ARG-153.

GO - Biological processⁱ

• adaptive thermogenesis Source: UniProtKB
• brown fat cell differentiation Source: RGDInferred from sequence orthologyⁱ
  • "Cloning, expression, and differentiation-dependent regulation of SMAF1 in adipogenesis."
    Kim J.Y., Tillison K., Smas C.M.
    Biochem. Biophys. Res. Commun. 326:36-44(2005) [PubMed] [Europe PMC] [Abstract]
  • "Dynamic transcriptome changes during adipose tissue energy expenditure reveal critical roles for long noncoding RNA regulators."
    Bai Z., Chai X.R., Yoon M.J., Kim H.J., Lo K.A., Zhang Z.C., Xu D., Siang D.T.C., Walet A.C.E., Xu S.H., Chia S.Y., Chen P., Yang H., Ghosh S., Sun L.
    PLoS Biol. 15:e2002176-e2002176(2017) [PubMed] [Europe PMC] [Abstract]
• cellular response to cold Source: RGDInferred from sequence orthologyⁱ
  • "Dynamic transcriptome changes during adipose tissue energy expenditure reveal critical roles for long noncoding RNA regulators."
    Bai Z., Chai X.R., Yoon M.J., Kim H.J., Lo K.A., Zhang Z.C., Xu D., Siang D.T.C., Walet A.C.E., Xu S.H., Chia S.Y., Chen P., Yang H., Ghosh S., Sun L.
    PLoS Biol. 15:e2002176-e2002176(2017) [PubMed] [Europe PMC] [Abstract]
• cellular response to dehydroepiandrosterone Source: RGD <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "DHEA administration increases brown fat uncoupling protein 1 levels in obese OLETF rats."
    Ryu J.W., Kim M.S., Kim C.H., Song K.H., Park J.Y., Lee J.D., Kim J.B., Lee K.U.
    Biochem. Biophys. Res. Commun. 303:726-731(2003) [PubMed] [Europe PMC] [Abstract]
• cellular response to fatty acid Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "Fatty acids change the conformation of uncoupling protein 1 (UCP1)."
    Divakaruni A.S., Humphrey D.M., Brand M.D.
    J. Biol. Chem. 287:36845-36853(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: ACTIVITY REGULATION, PURINE NUCLEOTIDE-BINDING.
• cellular response to hormone stimulus Source: RGDInferred from expression patternⁱ
  • "Nutritional and hormonal regulation of uncoupling protein gene expression in rat adipocytes."
    Fukuda H., Hirakawa T., Iritani N.
    J. Nutr. Sci. Vitaminol. 53:426-431(2007) [PubMed] [Europe PMC] [Abstract]
• cellular response to reactive oxygen species Source: UniProtKB
• diet induced thermogenesis Source: RGDInferred from sequence orthologyⁱ
  • "UCP1 ablation induces obesity and abolishes diet-induced thermogenesis in mice exempt from thermal stress by living at thermoneutrality."
    Feldmann H.M., Golozoubova V., Cannon B., Nedergaard J.
    Cell Metab. 9:203-209(2009) [PubMed] [Europe PMC] [Abstract]
• generation of precursor metabolites and energy Source: RGD <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • "Growth factor regulation of uncoupling protein-1 mRNA expression in brown adipocytes."
    Garcia B., Obregon M.J.
    Am. J. Physiol., Cell Physiol. 282:C105-12(2002) [PubMed] [Europe PMC] [Abstract]
• mitochondrial transmembrane transport Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "Fatty acids change the conformation of uncoupling protein 1 (UCP1)."
    Divakaruni A.S., Humphrey D.M., Brand M.D.
    J. Biol. Chem. 287:36845-36853(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: ACTIVITY REGULATION, PURINE NUCLEOTIDE-BINDING.
• mitochondrial transport Source: RGDInferred from direct assayⁱ
  • Ref.8

    "Fatty acid activation of the uncoupling proteins requires the presence of the central matrix loop from UCP1."
    Jimenez-Jimenez J., Ledesma A., Zaragoza P., Gonzalez-Barroso M.M., Rial E.
    Biochim. Biophys. Acta 1757:1292-1296(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• positive regulation of cold-induced thermogenesis Source: YuBioLab <p>Inferred from Sequence or Structural Similarity<br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iss">GO evidence code guide</a></p> Inferred from sequence or structural similarityⁱ
  • "UCP1 deficiency causes brown fat respiratory chain depletion and sensitizes mitochondria to calcium overload-induced dysfunction."
    Kazak L., Chouchani E.T., Stavrovskaya I.G., Lu G.Z., Jedrychowski M.P., Egan D.F., Kumari M., Kong X., Erickson B.K., Szpyt J., Rosen E.D., Murphy M.P., Kristal B.S., Gygi S.P., Spiegelman B.M.
    Proc. Natl. Acad. Sci. U.S.A. 114:7981-7986(2017) [PubMed] [Europe PMC] [Abstract]
• positive regulation of metabolic process Source: RGDTraceable author statementⁱ
  • "Synergy of fatty acid and reactive alkenal activation of proton conductance through uncoupling protein 1 in mitochondria."
    Esteves T.C., Parker N., Brand M.D.
    Biochem. J. 395:619-628(2006) [PubMed] [Europe PMC] [Abstract]
• proton transmembrane transport Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "Fatty acids change the conformation of uncoupling protein 1 (UCP1)."
    Divakaruni A.S., Humphrey D.M., Brand M.D.
    J. Biol. Chem. 287:36845-36853(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: ACTIVITY REGULATION, PURINE NUCLEOTIDE-BINDING.
• regulation of reactive oxygen species biosynthetic process Source: RGDInferred from sequence orthologyⁱ
  • "The role of UCP 1 in production of reactive oxygen species by mitochondria isolated from brown adipose tissue."
    Dlaskova A., Clarke K.J., Porter R.K.
    Biochim. Biophys. Acta 1797:1470-1476(2010) [PubMed] [Europe PMC] [Abstract]
• regulation of transcription by RNA polymerase II Source: RGDInferred from sequence orthologyⁱ
  • "High glucose increases angiopoietin-2 transcription in microvascular endothelial cells through methylglyoxal modification of mSin3A."
    Yao D., Taguchi T., Matsumura T., Pestell R., Edelstein D., Giardino I., Suske G., Rabbani N., Thornalley P.J., Sarthy V.P., Hammes H.P., Brownlee M.
    J. Biol. Chem. 282:31038-31045(2007) [PubMed] [Europe PMC] [Abstract]
• response to cold Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• response to nutrient levels Source: UniProtKB
• response to temperature stimulus Source: UniProtKB

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Topology

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

Protein-protein interaction databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MVSSTTSEVQ PTMGVKIFSA GVSACLADII TFPLDTAKVR LQIQGEGQAS 
        60         70         80         90        100
STIRYKGVLG TITTLAKTEG LPKLYSGLPA GIQRQISFAS LRIGLYDTVQ 
       110        120        130        140        150
EYFSSGRETP ASLGSKISAG LMTGGVAVFI GQPTEVVKVR MQAQSHLHGI 
       160        170        180        190        200
KPRYTGTYNA YRVIATTESL STLWKGTTPN LMRNVIINCT ELVTYDLMKG 
       210        220        230        240        250
ALVNHHILAD DVPCHLLSAL VAGFCTTLLA SPVDVVKTRF INSLPGQYPS 
       260        270        280        290        300
VPSCAMTMYT KEGPAAFFKG FAPSFLRLGS WNVIMFVCFE QLKKELMKSR 

QTVDCTT                                                

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. SIMILARITY comments
   Index of protein domains and families