fungal mating pheromone receptors
{{Short description|Family of G-protein-coupled receptors}}
{{Pfam_box
| Symbol = STE2
| Name = Fungal pheromone mating factor STE2 GPCR
| image = PDB_1pjd_EBI.jpg
| width =
| caption = Structure of a Peptide Segment of the 6th Transmembrane Domain of the Saccharomyces cerevisiae alpha-Factor Receptor.{{cite journal |vauthors=Valentine KG, Liu SF, Marassi FM |title=Structure and topology of a peptide segment of the 6th transmembrane domain of the Saccharomyces cerevisiae alpha-factor receptor in phospholipid bilayers |journal=Biopolymers |volume=59 |issue=4 |pages=243–56 |date=October 2001 |pmid=11473349 |doi=10.1002/1097-0282(20011005)59:4<243::AID-BIP1021>3.0.CO;2-H |pmc=3282060|display-authors=etal}}
| Pfam= PF02116
| InterPro= IPR000366
| SMART=
| Prosite =
| SCOP = 1pjd
| TCDB =
| OPM family= 6
| OPM protein= 2k9p
| CDD = cd14939
| PDB=
{{PDB3|1pjd}}A:253-269
}}
Fungal pheromone mating factor receptors form a distinct family of G-protein-coupled receptors.
Function
Mating factor receptors STE2 and STE3 are integral membrane proteins that may be involved in the response to mating factors on the cell membrane.{{cite journal |vauthors=Nakayama N, Miyajima A, Arai K |title=Nucleotide sequences of STE2 and STE3, cell type-specific sterile genes from Saccharomyces cerevisiae |journal=EMBO J. |volume=4 |issue=10|pages=2643–2648 |year=1985 |doi=10.1002/j.1460-2075.1985.tb03982.x |pmid=16453635 |pmc=554555}}{{cite journal |vauthors=Burkholder AC, Hartwell LH |title=The yeast alpha-factor receptor: structural properties deduced from the sequence of the STE2 gene |journal=Nucleic Acids Res. |volume=13 |issue=23 |pages=8463–8475 |year=1985 |pmid=3001640 |doi=10.1093/nar/13.23.8463 |pmc=322145}}{{cite journal |vauthors=Herskowitz I, Marsh L |title=STE2 protein of Saccharomyces kluyveri is a member of the rhodopsin/beta-adrenergic receptor family and is responsible for recognition of the peptide ligand alpha factor |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue=11 |pages=3855–3859 |year=1988 |pmid=2836861 |doi=10.1073/pnas.85.11.3855 |pmc=280318|bibcode=1988PNAS...85.3855M |doi-access=free }} The amino acid sequences of both receptors contain high proportions of hydrophobic residues grouped into 7 domains, in a manner reminiscent of the rhodopsins and other receptors believed to interact with G-proteins.