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Proteinase-activated receptor 2

Gene

F2RL1

OrganismHomo sapiens (Human)Status Reviewed - Annotation score: Annotation score: 5 out of 5

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<p><a href='/help/annotation_score' target='_top'>More...</a></p> - Experimental evidence at protein level i <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p> Select a section on the left to see content.

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

Receptor for trypsin and trypsin-like enzymes coupled to G proteins. Its function is mediated through the activation of several signaling pathways including phospholipase C (PLC), intracellular calcium, mitogen-activated protein kinase (MAPK), I-kappaB kinase/NF-kappaB and Rho. Can also be transactivated by cleaved F2R/PAR1. Involved in modulation of inflammatory responses and regulation of innate and adaptive immunity, and acts as a sensor for proteolytic enzymes generated during infection. Generally is promoting inflammation. Can signal synergistically with TLR4 and probably TLR2 in inflammatory responses and modulates TLR3 signaling. Has a protective role in establishing the endothelial barrier; the activity involves coagulation factor X. Proposed to have a bronchoprotective role in airway epithelium, but also shown to compromise the airway epithelial barrier by interrupting E-cadherin adhesion. Involved in the regulation of vascular tone; activation results in hypotension presumably mediated by vasodilation. Associates with a subset of G proteins alpha subunits such as G alpha-q, G alpha-11, G alpha-14, G alpha-12 and G alpha-13, but probably not with G(o) alpha, G(i) subunit alpha-1 and G(i) subunit alpha-2. However, according to PubMed:21627585 can signal through G(i) subunit alpha. Believed to be a class B receptor which internalizes as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptor, for extended periods of time. Mediates inhibition of TNF-alpha stimulated JNK phosphorylation via coupling to G alpha-q/11; the function involves dissociation of RIPK1 and TRADD from TNFR1. Mediates phosphorylation of nuclear factor NF-kappa-B RELA subunit at 'Ser-536'; the function involves IKBKB and is predominantly independent of G proteins. Involved in cellular migration. Involved in cytoskeletal rearrangement and chemotaxis through beta-arrestin-promoted scaffolds; the function is independent of G alpha-q/11 and involves promotion of cofilin dephosphoryltaion and actin filament severing. Induces redistribution of COPS5 from the plasma membrane to the cytosol and activation of the JNK cascade is mediated by COPS5. Involved in the recruitment of leukocytes to the sites of inflammation and is the major PAR receptor capable of modulating eosinophil function such as proinflammatory cytokine secretion, superoxide production and degranulation. During inflammation promotes dendritic cell maturation, trafficking to the lymph nodes and subsequent T-cell activation. Involved in antimicrobial response of innate immnune cells; activation enhances phagocytosis of Gram-positive and killing of Gram-negative bacteria. Acts synergistically with interferon-gamma in enhancing antiviral responses. Implicated in a number of acute and chronic inflammatory diseases such as of the joints, lungs, brain, gastrointestinal tract, periodontium, skin, and vascular systems, and in autoimmune disorders. 24 Publications

<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="http://www.uniprot.org/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment in i

Miscellaneous Synthetic PAR agonist peptides (APs) that mimic the first six amino acids of the newly formed N-terminus activate the native, uncleaved receptor nonenzymatically by binding directly to the corresponding second extracellular loop to mediate signaling. <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 function i Complete GO annotation... <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 - Biological process i Complete GO annotation... <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> Keywords i Molecular function G-protein coupled receptor, Receptor, Transducer Biological process Immunity, Inflammatory response, Innate immunity Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More... Reactome i R-HSA-375276. Peptide ligand-binding receptors. R-HSA-416476. G alpha (q) signalling events.

SIGNOR Signaling Network Open Resource

More... SIGNOR i P55085. Protein family/group databases

Transport Classification Database

More... TCDB i 9.A.14.13.12. the g-protein-coupled receptor (gpcr) family.

<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 & Taxonomy i

<p>This subsection of the ‘Names and Taxonomy’ section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p> Protein names i Recommended name: Proteinase-activated receptor 2 Short name: PAR-2 Alternative name(s): Coagulation factor II receptor-like 1G-protein coupled receptor 11Thrombin receptor-like 1Cleaved into the following 2 chains: Proteinase-activated receptor 2, alternate cleaved 1 Proteinase-activated receptor 2, alternate cleaved 2 <p>This subsection of the ‘Names and taxonomy’ section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p> Gene names i Name:F2RL1 Synonyms: GPR11 , PAR2 <p>This subsection of the ‘Names and taxonomy’ section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p> Organism i Homo sapiens (Human) <p>This subsection of the ‘Names and taxonomy’ section shows the unique identifier assigned by the <span class="caps">NCBI</span> to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p> Taxonomic identifier i 9606 [NCBI] <p>This subsection of the ‘Names and taxonomy’ section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p> Taxonomic lineage i cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo <p>This subsection of the “Names and Taxonomy” section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p> Proteomes i Organism-specific databases

Eukaryotic Pathogen Database Resources

More... EuPathDB i HostDB:ENSG00000164251.4.

Human Gene Nomenclature Database

More... HGNC i HGNC:3538. F2RL1.

<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 location i

#subcell-image-P55085 .uniprot .Plasma_Membrane { fill:#FBEFB6; fill-opacity:1; cursor: pointer;} #subcell-image-P55085 .uniprot .Plasma_Membrane:hover { fill:#E2D69D; } #subcell-image-P55085 .uniprot .Plasma_Membrane_Label {; fill-opacity:1;} #subcell-image-P55085 .goimage .Endosome { fill:#FBEFB6; fill-opacity:1; cursor: pointer;} #subcell-image-P55085 .goimage .Endosome:hover { fill:#E2D69D; } #subcell-image-P55085 .goimage .Golgi_Apparatus { fill:#FBEFB6; fill-opacity:1; cursor: pointer;} #subcell-image-P55085 .goimage .Golgi_Apparatus:hover { fill:#E2D69D; } #subcell-image-P55085 .goimage .Plasma_Membrane { fill:#FBEFB6; fill-opacity:1; cursor: pointer;} #subcell-image-P55085 .goimage .Plasma_Membrane:hover { fill:#E2D69D; } #subcell-image-P55085 .goimage .Endosome_Label {; fill-opacity:1;} #subcell-image-P55085 .goimage .Golgi_Apparatus_Label {; fill-opacity:1;} #subcell-image-P55085 .goimage .Plasma_Membrane_Label {; fill-opacity:1;} Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS Topology Feature key Position(s) Description Actions Graphical view Length <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p> Topological domain i 37 – 75 Extracellular Sequence analysis Add BLAST 39 <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p> Transmembrane i 76 – 101 Helical; Name=1 Sequence analysis Add BLAST 26 <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p> Topological domain i 102 – 110 Cytoplasmic Sequence analysis 9 <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p> Transmembrane i 111 – 130 Helical; Name=2 Sequence analysis Add BLAST 20 <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p> Topological domain i 131 – 149 Extracellular Sequence analysis Add BLAST 19 <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p> Transmembrane i 150 – 171 Helical; Name=3 Sequence analysis Add BLAST 22 <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p> Topological domain i 172 – 190 Cytoplasmic Sequence analysis Add BLAST 19 <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p> Transmembrane i 191 – 211 Helical; Name=4 Sequence analysis Add BLAST 21 <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p> Topological domain i 212 – 241 Extracellular Sequence analysis Add BLAST 30 <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p> Transmembrane i 242 – 260 Helical; Name=5 Sequence analysis Add BLAST 19 <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p> Topological domain i 261 – 285 Cytoplasmic Sequence analysis Add BLAST 25 <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p> Transmembrane i 286 – 308 Helical; Name=6 Sequence analysis Add BLAST 23 <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p> Topological domain i 309 – 323 Extracellular Sequence analysis Add BLAST 15 <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p> Transmembrane i 324 – 347 Helical; Name=7 Sequence analysis Add BLAST 24 <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">‘Subcellular location’</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p> Topological domain i 348 – 397 Cytoplasmic Sequence analysis Add BLAST 50 <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> Keywords - Cellular component i Cell membrane, Membrane

<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 & Biotech i

Mutagenesis Feature key Position(s) Description Actions Graphical view Length <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p> Mutagenesis i 30 N → A: Decreases cell surface expression; when associate with A-222. 1 Publication

<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="http://www.uniprot.org/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment in i

1 <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p> Mutagenesis i 30 N → A: Increase of sensitivity towards tryptase. 1 Publication

<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="http://www.uniprot.org/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment in i

1 <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p> Mutagenesis i 222 N → A: Decreases cell surface expression; when associate with A-30. 1 Publication

<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="http://www.uniprot.org/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment in i

1 <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p> Mutagenesis i 222 N → A: Loss of sensitivity towards all tested proteases. 1 Publication

<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="http://www.uniprot.org/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment in i

1 <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p> Mutagenesis i 355 – 363 Missing : Abolishes signaling through accumulation of intracellular calcium and phosphoinositide; no effect in signaling through MAPK. 1 Publication

<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="http://www.uniprot.org/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment in i

9 <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p> Mutagenesis i 361 C → A: Loss of palmitoylation; increases surface expression and internalization following trypsin activation, decreases sensitivity and intracellular calcium signaling, increases ERK activation through G(i) subunit alpha. 1 <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p> Mutagenesis i 363 S → A: Reduces receptor desensitization and internalization, activates ERK1/2; when associated with A-366. 1 Publication

<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="http://www.uniprot.org/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment in i

1 <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p> Mutagenesis i 366 T → A: Reduces receptor desensitization and internalization, activates ERK1/2; when associated with A-363. 1 Publication

<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="http://www.uniprot.org/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment in i

1 Organism-specific databases

DisGeNET

More... DisGeNET i 2150.

MalaCards human disease database

More... MalaCards i F2RL1.

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More... PharmGKB i PA27947. Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More... ChEMBL i CHEMBL5963.

IUPHAR/BPS Guide to PHARMACOLOGY

More... GuidetoPHARMACOLOGY i 348. Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More... BioMuta i F2RL1.

Domain mapping of disease mutations (DMDM)

More... DMDM i 1709580.

<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 / Processing i

Molecule processing Feature key Position(s) Description Actions Graphical view Length <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p> Signal peptide i 1 – 25 Sequence analysis Add BLAST 25 <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p>

Swiss made

Un article de Wikipédia, l'encyclopédie libre.
Aller à : navigation, rechercher
Pour les articles homonymes, voir Swiss.

Swiss made est un label qui indique qu'un produit a été fabriqué en Suisse. Ce label est utilisé spécialement pour les montres, avec une ordonnance de la Confédération suisse qui en spécifie les conditions d'utilisation.

Sommaire

  • 1 Histoire
  • 2 Aspect légal
  • 3 Notes et références
  • 4 Liens externes

Histoire[modifier | modifier le code]

Le Swiss made trouve son origine au XVIIe siècle quand la corporation des horlogers de Genève décida de l'apposition d'un poinçon sur ses montres, pour en certifier la qualité. Le label se formalise à la fin du XIXe siècle. Dans les années 1880, les horlogers suisses se trouvent confrontés à la concurrence américaine. Ils décident donc de créer leur propre certification, qu'ils appellent Swiss made.

En 1971, cette certification est protégée légalement par la Suisse, au moyen de l'Ordonnance réglant l'utilisation du nom « Suisse » pour les montres[1].

Aujourd'hui le label Swiss Made pour les montres reste particulièrement controversé. Car pour être qualifié de Swiss Made, il suffit que 50 % de la valeur constituant le mouvement soit fabriquée en Suisse ; et que la montre et son mouvement soient assemblés et contrôlés en Suisse.

Certaines montres peuvent donc être majoritairement composées de pièces venant de Chine ou d'ailleurs, et arborer légalement le label Swiss Made. La Fédération Horlogère Suisse souhaite d'ailleurs renforcer le label afin d'éviter ces dérives.

Aspect légal[modifier | modifier le code]

La loi suisse définit d'abord la montre. Elle définit ensuite la montre suisse et le mouvement suisse. Pour être considérée comme suisse, la montre doit avoir un mouvement suisse emboîté en Suisse et être contrôlée en Suisse. Le mouvement suisse doit être assemblé et contrôlé en Suisse[2].

Notes et références[modifier | modifier le code]

  1. « http://www.swissinfo.ch/fre/aux-origines-du-swiss-made-horloger/5989116 »(Archive • Wikiwix • Archive.is • Google • Que faire ?)
  2. http://www.admin.ch/ch/f/rs/2/232.119.fr.pdf

Liens externes[modifier | modifier le code]

  • Swiss Madesur le site de la Fédération horlogère suisse
  • Swissness FAQ sur la nouvelle réglementation sur le site de l'Institut Fédéral de la Proriété Intellectuelle
  • Swiss Label pour promotion des produits et des services suisses
  • Portail de la Suisse
  • Portail de l’horlogerie
Ce document provient de « https://fr.wikipedia.org/w/index.php?title=Swiss_made&oldid=139342526 ».