The domain within your query sequence starts at position 709 and ends at position 750; the E-value for the GPS domain shown below is 1.1e-7.



PFAM accession number:PF01825
Interpro abstract (IPR000203):

GPS (for GPCR proteolytic site) motif is found in a number of G-protein-coupled receptors (GPCRs) including CIRLs/latrophilins and in other membrane-associated proteins like the sea urchin receptor for egg jelly protein (REJ) [ (PUBMED:10469603) ].

For the CIRL-1, CIRL-2, CIRL-3 and CD-97 proteins, it has been shown that they are each made of two non-covalently bound subunits resulting from the endogenous proteolytic cleavage of a precursor protein. Because the cysteine-rich domain of CIRL-1 and possibly other receptors is involved in the endogenous proteolytic processing of CIRL-1 and possibly other receptors, it has been named GPS for GPCR proteolytic site. As the amino acids surrounding the putative cleavage site are the most conserved residues in the GPS domain, it has been suggested that all proteins containing it may be cleaved at this position [ (PUBMED:10026162) (PUBMED:9830014) (PUBMED:10469603) ].

GPS motifs are about 50 residues long and contain either 2 or 4 cysteine residues that are likely to form disulphide bridges. Based on conservation of these cysteines the following pairing can be predicted.

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+-----------------+---------------+ |
| | | |
cleavage site

The GPS motif is an integral part of a much larger (320-residue approximately) domain that has been termed GPCR-Autoproteolysis INducing (GAIN) domain. The GAIN domain represents an autoproteolytic fold whose function is likely relevant for GPCR signalling [ (PUBMED:22333914) ].

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