G protein-coupled receptor 127; EGF-like module containing mucin-like hormone receptor-like 4 (GPR127, EMR4, EMR4P)

Function: - may play role in cellular interaction between myeloid cells & B-cells (putative) - forms a heterodimer, consisting of a large extracellular region (alpha subunit) non-covalently linked to a seven- transmembrane moiety (beta subunit) (putative) - proteolytically cleaved into 2 subunits, an extracellular alpha subunit non-covalently linked to a 7- transmembrane beta subunit Structure: - belongs to the G-protein coupled receptor 2 family LN-TM7 subfamily - contains 2 EGF-like domains - contains 1 GPS domain Compartment: cell membrane; multi-pass membrane protein Alternative splicing: named isoforms=2 Pathology: - mutation in exon 8 would result in a truncated soluble form Note: - could be the product of a pseudogene - seems to have became non-functional after human-chimpanzee speciation, about 5 million years ago

General

evolutionary divergent human protein glycoprotein G-protein coupled receptor; serpentine receptor

Properties

SIZE: MW = 51 kD entity length = 457 aa COMPARTMENT: cellular membrane MOTIF: exoplasmic domain {15-191} MOTIF: EGF domain {15-53} MOTIF: cysteine residue {C15} MODIFICATION: cysteine residue {C24} cysteine residue {C18} MODIFICATION: cysteine residue {C30} cysteine residue {C24} MODIFICATION: cysteine residue {C15} N-glycosylation site {N26} cysteine residue {C30} MODIFICATION: cysteine residue {C18} cysteine residue {C32} MODIFICATION: cysteine residue {C52} cysteine residue {C52} MODIFICATION: cysteine residue {C32} EGF domain {54-104} MOTIF: cysteine residue {C58} MODIFICATION: cysteine residue {C71} cysteine residue {C65} MODIFICATION: cysteine residue {C80} cysteine residue {C71} MODIFICATION: cysteine residue {C58} cysteine residue {C80} MODIFICATION: cysteine residue {C65} cysteine residue {C82} MODIFICATION: cysteine residue {C103} cysteine residue {C103} MODIFICATION: cysteine residue {C82} N-glycosylation site {N106} N-glycosylation site {N162} proteolytic site {173-174} transmembrane domain {192-212} cytoplasmic loop {213-223} transmembrane domain {224-244} exoplasmic loop {245-250} MOTIF: N-glycosylation site {N245} transmembrane domain {251-271} cytoplasmic loop {272-299} transmembrane domain {300-320} exoplasmic loop {321-336} transmembrane domain {337-357} cytoplasmic loop {358-384} transmembrane domain {385-405} exoplasmic loop {406-413} transmembrane domain {414-434} cytoplasmic domain {435-457}

Database Correlations

UniProt Q86SQ3 PFAM correlations

References

UniProt :accession Q86SQ3