glycoprotein 3 GP3 [Equine arteritis virus]

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Signal peptide cleavage from GP3 enabled by removal of adjacent glycosylation sites does not impair replication of equine arteritis virus in cell culture, but the hydrophobic C-terminus is essential. [Virus Res. 2014]
Signal peptide cleavage from GP3 enabled by removal of adjacent glycosylation sites does not impair replication of equine arteritis virus in cell culture, but the hydrophobic C-terminus is essential.
Matczuk AK, Veit M. Virus Res. 2014 Apr; 183:107-11. Epub 2014 Feb 17.
Co-translational processing of glycoprotein 3 from equine arteritis virus: N-glycosylation adjacent to the signal peptide prevents cleavage. [J Biol Chem. 2013]
Co-translational processing of glycoprotein 3 from equine arteritis virus: N-glycosylation adjacent to the signal peptide prevents cleavage.
Matczuk AK, Kunec D, Veit M. J Biol Chem. 2013 Dec 6; 288(49):35396-405. Epub 2013 Oct 18.
Identification of a novel structural protein of arteriviruses. [J Virol. 1999]
Identification of a novel structural protein of arteriviruses.
Snijder EJ, van Tol H, Pedersen KW, Raamsman MJ, de Vries AA. J Virol. 1999 Aug; 73(8):6335-45.

RefSeq protein
See the reference protein sequence for glycoprotein 3 (GP3) (NP_065657.1).

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Protein