PTHR35496

2S SEED STORAGE PROTEIN 1-RELATED

PANTHER entry
Member databasePANTHER
PANTHER typefamily

Description
Imported from IPR000617

This entry represents a group of plant seed storage proteins, including Napin, 2S seed storage protein and Conglutin.

Napins are low-molecular weight, basic storage proteins synthesised in rape-seed embryos during seed maturation
[1, 2]
. Sequence comparisons have revealed that Napin belongs to a diverse protein family, which includes major allergens, trypsin inhibitors and natural anti-fungal proteins. Napin comprises 2 polypeptide chains (MW 9000 and 4000) held together by disulphide bonds. The protein is initially synthesised as a precursor of 178 residues, which is proteolytically cleaved to generate mature Napin chains, with 86 and 29 residues respectively
[1]
.

Some of the proteins in this family are allergens, with cores that are very resistant to proteolytic digestion and to elevated temperatures of up to 100 degrees C
[6, 5, 3, 4]
. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee King T.P., Hoffmann D., Loewenstein H., Marsh D.G., Platts-Mills T.A.E., Thomas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed of the first three letters of the genus; a space; the first letter of the species name; a space and an arabic number. In the event that two species names have identical designations, they are discriminated from one another by adding one or more letters (as necessary) to each species designation.

References
Imported from IPR000617

1.Structure of the rapeseed 1.7 S storage protein, napin, and its precursor. Ericson ML, Rodin J, Lenman M, Glimelius K, Josefsson LG, Rask L. J. Biol. Chem. 261, 14576-81, (1986). View articlePMID: 3771543

2.cDNA clones for Brassica napus seed storage proteins: evidence from nucleotide sequence analysis that both subunits of napin are cleaved from a precursor polypeptide. Crouch ML, Tenbarge KM, Simon AE, Ferl R. J. Mol. Appl. Genet. 2, 273-83, (1983). PMID: 6689334

3.Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. Prodic I, Stanic-Vucinic D, Apostolovic D, Mihailovic J, Radibratovic M, Radosavljevic J, Burazer L, Milcic M, Smiljanic K, van Hage M, Cirkovic Velickovic T. Clin Exp Allergy 48, 731-740, (2018). PMID: 29412488

4.Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis. Pantoja-Uceda D, Bruix M, Gimenez-Gallego G, Rico M, Santoro J. Biochemistry 42, 13839-47, (2003). View articlePMID: 14636051

5.Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions. Lehmann K, Schweimer K, Reese G, Randow S, Suhr M, Becker WM, Vieths S, Rosch P. Biochem. J. 395, 463-72, (2006). View articlePMID: 16372900

6.Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing: seed storage proteins as common food allergens. Beyer K, Bardina L, Grishina G, Sampson HA. J Allergy Clin Immunol 110, 154-9, (2002). PMID: 12110835

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