Search results for "Peptide sequence"

showing 10 items of 330 documents

Isolation and characterization of a fish F-type lectin from gilt head bream (Sparus aurata) serum.

2007

A novel fucose-binding lectin, designated SauFBP32, was purified by affinity chromatography on fucose-agarose, from the serum of the gilt head bream Sparus aurata. Electrophoretic mobility of the subunit revealed apparent molecular weights of 35 and 30 kDa under reducing and non-reducing conditions, respectively. Size exclusion analysis suggests that the native lectin is a monomer under the selected experimental conditions. Agglutinating activity towards rabbit erythrocytes was not significantly modified by addition of calcium or EDTA; activity was optimal at 37 degrees C, retained partial activity by treatment at 70 degrees C, and was fully inactivated at 90 degrees C. On western blot anal…

Serum hemagglutininsTeleostMolecular Sequence DataBiophysicsBiochemistryAffinity chromatographyWestern blotSparus aurataLectinsmedicineAnimalsDicentrarchus labraxAmino Acid SequenceSea bassMolecular BiologyPeptide sequencePolyacrylamide gel electrophoresisbiologyMolecular massmedicine.diagnostic_testSequence Homology Amino AcidLectinF-type lectin; Sparus aurata; Dicentrarchus labrax; Teleost; Serum hemagglutininsbiology.organism_classificationSea BreamBiochemistrybiology.proteinChromatography GelDicentrarchusElectrophoresis Polyacrylamide GelF-type lectinBiochimica et biophysica acta
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The membrane anchor of microsomal epoxide hydrolase from human, rat, and rabbit displays an unexpected membrane topology.

1997

The microsomal epoxide hydrolase (mEH) and cytochrome P450s catalyze the sequential formation of carcinogenic metabolites. According to one algorithm for predicting the membrane topology of proteins, the human, the rabbit, and the rat mEH should adopt a type II topology. The type II topology is also predicted by a recently established neuronal network which is trained to recognize signal peptides with very high accuracy. In contrast to these predictions we find, based on N-glycosylation analysis in a cell-free and in a cellular system, that the membrane anchor of human, rat, and rabbit mEH displays a type I topology. This result is correctly predicted by the positive inside rule in which ne…

Signal peptide1303 BiochemistryGlycosylationGlycosylationCytochromeStereochemistryRecombinant Fusion ProteinsImmunoblottingMolecular Sequence DataBiophysics10050 Institute of Pharmacology and Toxicology610 Medicine & healthProtein Sorting SignalsTransfectionBiochemistry1307 Cell BiologyCell membranechemistry.chemical_compoundSpecies Specificity1312 Molecular BiologymedicineElectrochemistryAnimalsHumansAmino Acid SequenceMolecular BiologyPeptide sequenceEpoxide HydrolasesbiologyCell MembraneCell BiologyRatsmedicine.anatomical_structurechemistryMutagenesisMicrosomal epoxide hydrolaseMembrane topologyEpoxide HydrolasesCOS Cellsbiology.protein570 Life sciences; biologyRabbits1304 BiophysicsBiochemical and biophysical research communications
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Structure, organization and expression of two clustered cuticle protein genes during the metamorphosis of an insect, Tenebrio molitor.

1998

A 4-kb DNA segment of Tenebrio molitor (Insecta, Coleoptera) genomic DNA containing two larval-pupal cuticular genes has been cloned and sequenced. These genes, transcribed in opposite directions, are related in DNA sequence and the proteins encoded are very similar. Each of them contains a single intron located inside the sequence encoding the signal peptide, and a conserved sequence at -200 bp from the mRNA start position. These similarities in sequence suggest that these genes have evolved by duplication followed by diversification and that they are members of a family of genes with a common ancestry. They are the first example of clustered genes in Tenebrio molitor.

Signal peptideDNA ComplementaryMolecular Sequence DataGenes InsectBiologyBiochemistryDNA sequencingConserved sequenceEvolution MolecularGene duplicationAnimalsAmino Acid SequenceTenebrioPeptide sequenceGeneIn Situ HybridizationGeneticsBase SequenceSequence Homology Amino AcidfungiIntronMetamorphosis BiologicalGene Expression Regulation DevelopmentalIntronsgenomic DNAMultigene FamilyInsect ProteinsEuropean journal of biochemistry
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A novel cell wall protein specific to the mycelial form of Yarrowia lipolytica.

1996

A cDNA clone specifying a cell wall protein was isolated from a Yarrowia lipolytica cDNA library. The cDNA library was constructed in the expression vector lambda gt 11, with the RNA isolated from actively growing mycelial cells. The deduced amino acid sequence shows that the encoded protein contains an N-terminal hydrophobic signal peptide. We have designated this protein YWP1 for Yarrowia lipolytica cell Wall Protein. Northern hybridization identified YWP1 transcript only when Y. lipolytica was growing in the mycelial form. The encoded protein seems to be covalently bound to the glucan cell wall since it is not released from the cell walls by sodium dodecyl sulphate extraction, but it is …

Signal peptideDNA ComplementaryTranscription GeneticHydrolasesBlotting WesternGenetic VectorsMolecular Sequence DataRestriction MappingBioengineeringApplied Microbiology and BiotechnologyBiochemistryCell wallFungal ProteinsOpen Reading FramesTransformation GeneticCell WallComplementary DNAGene Expression Regulation FungalYeastsGeneticsEscherichia coliAmino Acid SequenceCloning MolecularFluorescent Antibody Technique IndirectPeptide sequenceAntibodies FungalGene LibraryExpression vectorbiologyBase SequencecDNA libraryRNASodium Dodecyl SulfateYarrowiaRNA Fungalbiology.organism_classificationBlotting NorthernBlotting SouthernBiochemistrySaccharomycetalesElectrophoresis Polyacrylamide GelBiotechnologyYeast (Chichester, England)
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The Rare IL22RA2 Signal Peptide Coding Variant rs28385692 Decreases Secretion of IL-22BP Isoform-1, -2 and -3 and Is Associated with Risk for Multipl…

2020

The IL22RA2 locus is associated with risk for multiple sclerosis (MS) but causative variants are yet to be determined. In a single nucleotide polymorphism (SNP) screen of this locus in a Basque population, rs28385692, a rare coding variant substituting Leu for Pro at position 16 emerged significantly (p = 0.02). This variant is located in the signal peptide (SP) shared by the three secreted protein isoforms produced by IL22RA2 (IL-22 binding protein-1(IL-22BPi1), IL-22BPi2 and IL-22BPi3). Genotyping was extended to a Europe-wide case-control dataset and yielded high significance in the full dataset (p = 3.17 &times

Signal peptideGene isoformSignal peptidePopulationSingle-nucleotide polymorphismLocus (genetics)610 Medicine & healthBiologymultiple sclerosisMultiple sclerosis03 medical and health sciences0302 clinical medicineSNPIL-22 binding protein isoformsignal peptideddc:610Alleleeducation610 Medicine &amp; healthlcsh:QH301-705.5Peptide sequence030304 developmental biology0303 health scienceseducation.field_of_studyautoimmuneGeneral MedicineMolecular biologylcsh:Biology (General)<i>IL22RA2</i>IL22RA2Mutation[SDV.IMM]Life Sciences [q-bio]/Immunologymutation030217 neurology & neurosurgeryAutoimmune
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The nucleotide and deduced amino acid structures of sheep and pig fetuin. Common structural features of the mammalian fetuin family

1992

This study was initiated to gain further insight into the structural features of the mammalian fetuin family. The cDNA structures of sheep and pig fetuin were determined. The cDNA insert encoding sheep (pig) fetuin comprised 1550 (1470) nucleotides, including 54 (46) nucleotides encoding a signal peptide of 18 (15) residues and 1038 (1041) nucleotides encoding the 346 (347) amino acids of the mature plasma protein. The predicted amino-terminal sequence of the mature pig fetuin was confirmed by the amino-terminal sequence of the purified protein. However, two alternative sheep amino-terminal sequences were found in fetuin purified from the plasma of a single sheep fetus; the minor product wa…

Signal peptideGlycosylationSwineBlotting WesternMolecular Sequence DataSequence alignmentBiologyBiochemistrySequence Homology Nucleic AcidComplementary DNAEndopeptidasesAnimalsHumansAmino Acid SequenceCloning MolecularPeptide sequenceMammalschemistry.chemical_classificationSheepBase SequenceSerine EndopeptidasesStructural geneNucleic acid sequenceMembrane ProteinsDNAMolecular biologyFetuinAmino acidBiochemistrychemistryElectrophoresis Polyacrylamide Gelalpha-FetoproteinsEuropean Journal of Biochemistry
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Molecular characterization of hemoglobin from the honeybee Apis mellifera

2005

Due to the prevailing importance of the tracheal system for insect respiration, hemoglobins had been considered rare exceptions in this arthropod subphylum. Here we report the identification, cloning and expression analysis of a true hemoglobin gene in the honeybee Apis mellifera (Hymenoptera). The deduced amino acid sequence covers 171 residues (19.5 kDa) and harbors all globin-typical features, including the proximal and the distal histidines. The protein has no signal peptide for transmembrane transport and was predicted to localize in the cytoplasm. The honeybee hemoglobin gene shows an ancient structure, with introns in positions B12.2 and G7.0, while most other insect globins have div…

Signal peptideInsectaPhysiologymedia_common.quotation_subjectMolecular Sequence DataInsectBiologyHemoglobinsPhylogeneticsBotanyAnimalsAmino Acid SequenceRNA MessengerGlobinGenePeptide sequencemedia_commonGeneticsBase SequencefungiIntronSequence Analysis DNABeesBiological EvolutionInsect ScienceHemoglobinJournal of Insect Physiology
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Isolation of a novel LPS-induced component of the ML superfamily in Ciona intestinalis

2015

ML superfamily represents a group of proteins playing important roles in lipid metabolism and innate immune response. In this study, we report the identification of the first component of the ML superfamily in the invertebrate Ciona intestinalis by means of a subtractive hybridization strategy. Sequence homology and phylogenetic analysis showed that this protein forms a specific clade with vertebrate components of the Niemann-Pick type C2 protein and, for this reason, it has been named Ci-NPC2. The putative Ci-NPC2 is a 150 amino acids long protein with a short signal peptide, seven cysteine residues, three putative lipid binding site and a three-dimensional model showing a characteristic b…

Signal peptideLipopolysaccharidesHemocytesImmunologyMolecular Sequence DataSettore BIO/05 - ZoologiaSequence alignmentBiologyBioinformaticshemic and lymphatic diseasesGene expressionAnimalsCiona intestinalisAmino Acid SequencePeptide sequenceGenePhylogenychemistry.chemical_classificationBase SequenceSequence Homology Amino Acidnutritional and metabolic diseasesbiology.organism_classificationLipid MetabolismImmunity InnateAmino acidCiona intestinalisBiochemistrychemistryLPS NPC2 Ciona intestinalisSuppression subtractive hybridizationCarrier ProteinsSequence AlignmentDevelopmental Biology
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Candida albicans TDH3 gene promotes secretion of internal invertase when expressed in Saccharomyces cerevisiae as a glyceraldehyde-3-phosphate dehydr…

2003

We have checked the ability of the Candida albicans GAPDH polypeptide, which lacks a conventional N-terminal signal peptide, to reach the cell wall in Saccharomyces cerevisiae by using an intracellular form of the yeast invertase as a reporter protein. A hybrid TDH3-SUC2 gene containing the C. albicans TDH3 promoter sequences and a coding region encoding a fusion protein formed by the C. albicans GAPDH polypeptide, fused at its C-terminus with the yeast internal invertase, was constructed in a centromer derivative plasmid and transformed into a Suc(-) S. cerevisiae strain. Transformants displayed invertase activity measured in intact whole cells, and were able to grow on sucrose as the sole…

Signal peptideSaccharomyces cerevisiae ProteinsGlycoside HydrolasesSaccharomyces cerevisiaeMolecular Sequence DataBioengineeringSaccharomyces cerevisiaeBiologyApplied Microbiology and BiotechnologyBiochemistryGene productFungal ProteinsTransformation Geneticstomatognathic systemCell WallGene Expression Regulation FungalCandida albicansGeneticsAmino Acid SequenceCandida albicansDNA FungalPeptide sequenceGlyceraldehyde 3-phosphate dehydrogenaseBase Sequencebeta-FructofuranosidaseMembrane ProteinsRNA Fungalbiology.organism_classificationBlotting NorthernMolecular biologyFusion proteinRecombinant ProteinsInvertaseBiochemistrybiology.proteinGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)BiotechnologyPlasmidsYeast (Chichester, England)
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Characterization of a glycosylphosphatidylinositol-bound cell-wall protein (GPI-CWP) in Yarrowia lipolytica.

2004

The structure and composition of the cell wall of yeast has so far been studied mainly in Saccharomyces cerevisiae. It is basically made up of three components: beta-glucans, chitin and mannose-containing glycoproteins, also called mannoproteins. Most covalently bound cell-wall mannoproteins belong to the so-called glycosylphosphatidylinositol cell-wall protein (GPI-CWP) family, cell-wall proteins that are bound through the remnant of a GPI residue to 1,6-beta-glucan. The non-conventional yeast Yarrowia lipolytica shares Generally Regarded As Safe (GRAS) status with S. cerevisiae, has some industrial applications and is increasingly being proposed as a host for the production of recombinant…

Signal peptideSaccharomyces cerevisiae ProteinsGlycosylphosphatidylinositolsSaccharomyces cerevisiaeGenes FungalMolecular Sequence DataYarrowiaSaccharomyces cerevisiaeBiologyMicrobiologyGene productFungal ProteinsSpecies SpecificityCell WallAmino Acid SequenceDNA FungalPeptide sequencechemistry.chemical_classificationMembrane GlycoproteinsBase SequenceSequence Homology Amino AcidFungal geneticsMembrane ProteinsYarrowiabiology.organism_classificationYeastcarbohydrates (lipids)BiochemistrychemistryGlycoproteinMicrobiology (Reading, England)
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