The domain within your query sequence starts at position 168 and ends at position 331; the E-value for the IFNGR1 domain shown below is 1.6e-53.



PFAM accession number:PF07140
Interpro abstract (IPR021126):

Interferon (INF)-gamma is a dimeric glycoprotein produced by activated T cells and natural killer cells. Although originally isolated based on its antiviral activity, INF-gamma also displays powerful anti-proliferative and immuno-modulatory activities, which are essential for developing appropriate cellular defences against a variety of infectious agents. The first step in eliciting these responses is the specific high affinity interaction of INF- gamma with its cell-surface receptor (INF-gammaRalpha); the complex then interacts with at least one of a family of additional species-specific accessory factors (AF-1 or INF-gammabeta), which convey different cellular responses. One such response is the association and phosphorylation of two protein tyrosine kinases (Jak-1 and Jak-2), which in turn stimulate nuclear transcription activators [ (PUBMED:7617032) ].

  • The human INF-gammaR, is a member of the hematopoietic cytokine receptor superfamily. It is expressed in a membrane-bound form in many cell types, and is over-expressed in tumour cells. It comprises an extracellular portion of 229 residues, a single transmembrane region, and a cytoplasmic domain of 221 residues. As with other members of its superfamily, the cytokine-binding sites are formed by a small set of closely-spaced surface loops that extend from a beta-sheet core, much like antigen-binding sites on antibodies. The extracellular INF-gammaR monomer comprises two domains (domain D1 from residue 14-102, and domain D2 from residue 114-221), each resembling an Ig fold with fibronectin type III topology [ (PUBMED:9367779) ].
  • The vaccinia virus interferon (IFN)-gamma receptor (IFN-gammaR) is a 43kDa soluble glycoprotein that is secreted from infected cells early during infection. IFN-gammaR from vaccinia virus, cowpox virus and camelpox virus exist naturally as homodimers, whereas the cellular IFN-gammaR dimerizes only upon binding the homodimeric IFN-gamma. The existence of the virus protein as a dimer in the absence of ligand may provide an advantage to the virus in efficient binding and inhibition of IFN-gamma in solution [ (PUBMED:11842249) ].
GO component:membrane (GO:0016020)
GO function:cytokine binding (GO:0019955)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry IFNGR1