3A8D7BEB494B0C737204BEF1C542F3A8B7B7D70BFAE0E32AEC270C83DBBCF8783237D9E400583A1E21562D31B2492998

Glycoprotein G1 is a homotrimer; disulfide-linked. Glycoprotein G2 is a homotrimer. GP2 homotrimers bind with GP1 homotrimers to form, with the stable signal peptide, the GP-complex. Interacts with host DAG1. In infected cell, this interaction reduces the expression of functional host DAG1. GP-complex interacts with protein Z, which interacts with ribonucleocapsid; these interactions supposely induce virion budding.

Source:http://purl.uniprot.org/SHA-384/3A8D7BEB494B0C737204BEF1C542F3A8B7B7D70BFAE0E32AEC270C83DBBCF8783237D9E400583A1E21562D31B2492998

Download in:

Named Graph Language Inference

Statements in which the resource exists as a subject.
Predicate	Object
rdf:type	uniprot:Subunit_Annotation
rdfs:comment	Glycoprotein G1 is a homotrimer; disulfide-linked. Glycoprotein G2 is a homotrimer. GP2 homotrimers bind with GP1 homotrimers to form, with the stable signal peptide, the GP-complex. Interacts with host DAG1. In infected cell, this interaction reduces the expression of functional host DAG1. GP-complex interacts with protein Z, which interacts with ribonucleocapsid; these interactions supposely induce virion budding.