STE2_YEAST
ID STE2_YEAST Reviewed; 431 AA.
AC D6VTK4; P06842; Q70D63; Q70D65; Q70D69; Q70D73; Q70D74;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Pheromone alpha factor receptor;
GN Name=STE2; OrderedLocusNames=YFL026W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204660 / DBY746;
RX PubMed=16453635; DOI=10.1002/j.1460-2075.1985.tb03982.x;
RA Nakayama N., Miyajima A., Arai K.;
RT "Nucleotide sequences of STE2 and STE3, cell type-specific sterile genes
RT from Saccharomyces cerevisiae.";
RL EMBO J. 4:2643-2648(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3001640; DOI=10.1093/nar/13.23.8463;
RA Burkholder A.C., Hartwell L.H.;
RT "The yeast alpha-factor receptor: structural properties deduced from the
RT sequence of the STE2 gene.";
RL Nucleic Acids Res. 13:8463-8475(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=15087486; DOI=10.1093/nar/gkh529;
RA Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S.,
RA Souciet J.-L.;
RT "Differential evolution of the Saccharomyces cerevisiae DUP240 paralogs and
RT implication of recombination in phylogeny.";
RL Nucleic Acids Res. 32:2069-2078(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [5]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 269.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP GLYCOSYLATION AT ASN-25 AND ASN-32.
RX PubMed=11583169; DOI=10.1021/bi0108507;
RA Mentesana P.E., Konopka J.B.;
RT "Mutational analysis of the role of N-glycosylation in alpha-factor
RT receptor function.";
RL Biochemistry 40:9685-9694(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310; THR-329; SER-331;
RP SER-360; THR-363; SER-366; THR-382; SER-385; SER-386; THR-411 AND THR-414,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; THR-329; SER-331;
RP SER-366; THR-382 AND SER-386, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-374; LYS-400 AND LYS-422, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Receptor for the peptide pheromone alpha factor, the mating
CC factor of yeast.
CC -!- INTERACTION:
CC D6VTK4; P06783: STE3; NbExp=2; IntAct=EBI-6323511, EBI-18366;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: N-glycosylation may be involved in the sorting process
CC for misfolded STE2 protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 4 family.
CC {ECO:0000305}.
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DR EMBL; X03010; CAA26794.1; -; Genomic_DNA.
DR EMBL; M24335; AAA35112.1; -; Genomic_DNA.
DR EMBL; AJ585736; CAE52256.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09212.1; -; Genomic_DNA.
DR EMBL; AY693134; AAT93153.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12414.2; -; Genomic_DNA.
DR PIR; S56228; S56228.
DR RefSeq; NP_116627.2; NM_001179940.2.
DR PDB; 1PJD; NMR; -; A=253-269.
DR PDB; 2K9P; NMR; -; A=31-110.
DR PDBsum; 1PJD; -.
DR PDBsum; 2K9P; -.
DR AlphaFoldDB; D6VTK4; -.
DR BMRB; D6VTK4; -.
DR SMR; D6VTK4; -.
DR BioGRID; 31120; 46.
DR IntAct; D6VTK4; 2.
DR MINT; D6VTK4; -.
DR STRING; 4932.YFL026W; -.
DR TCDB; 9.B.45.1.1; the fungal mating-type pheromone receptor (mat-pr) family.
DR iPTMnet; D6VTK4; -.
DR MaxQB; D6VTK4; -.
DR PaxDb; D6VTK4; -.
DR PRIDE; D6VTK4; -.
DR EnsemblFungi; YFL026W_mRNA; YFL026W; YFL026W.
DR GeneID; 850518; -.
DR KEGG; sce:YFL026W; -.
DR SGD; S000001868; STE2.
DR VEuPathDB; FungiDB:YFL026W; -.
DR eggNOG; ENOG502QTV4; Eukaryota.
DR HOGENOM; CLU_038593_1_0_1; -.
DR InParanoid; D6VTK4; -.
DR OMA; FIMGCQT; -.
DR BioCyc; YEAST:G3O-30434-MON; -.
DR EvolutionaryTrace; D6VTK4; -.
DR PRO; PR:D6VTK4; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; D6VTK4; protein.
DR GO; GO:0038038; C:G protein-coupled receptor homodimeric complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:SGD.
DR GO; GO:0004934; F:mating-type alpha-factor pheromone receptor activity; IDA:SGD.
DR GO; GO:0004932; F:mating-type factor pheromone receptor activity; IBA:GO_Central.
DR GO; GO:0005550; F:pheromone binding; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IMP:SGD.
DR GO; GO:0000755; P:cytogamy; IDA:SGD.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:SGD.
DR Gene3D; 1.10.287.920; -; 1.
DR InterPro; IPR000366; GPCR_STE2.
DR InterPro; IPR027458; STE2_TM1-TM2_sf.
DR PANTHER; PTHR28009; PTHR28009; 1.
DR Pfam; PF02116; STE2; 1.
DR PRINTS; PR00250; GPCRSTE2.
PE 1: Evidence at protein level;
KW 3D-structure; G-protein coupled receptor; Glycoprotein; Isopeptide bond;
KW Membrane; Pheromone response; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..431
FT /note="Pheromone alpha factor receptor"
FT /id="PRO_0000195068"
FT TRANSMEM 51..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 379..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 329
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 363
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 382
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 414
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11583169"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11583169"
FT CROSSLNK 374
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 269
FT /note="K -> E (in Ref. 4; BAA09212)"
FT /evidence="ECO:0000305"
FT HELIX 39..72
FT /evidence="ECO:0007829|PDB:2K9P"
FT HELIX 80..106
FT /evidence="ECO:0007829|PDB:2K9P"
FT HELIX 256..264
FT /evidence="ECO:0007829|PDB:1PJD"
SQ SEQUENCE 431 AA; 47849 MW; 011F604DC2A6907E CRC64;
MSDAAPSLSN LFYDPTYNPG QSTINYTSIY GNGSTITFDE LQGLVNSTVT QAIMFGVRCG
AAALTLIVMW MTSRSRKTPI FIINQVSLFL IILHSALYFK YLLSNYSSVT YALTGFPQFI
SRGDVHVYGA TNIIQVLLVA SIETSLVFQI KVIFTGDNFK RIGLMLTSIS FTLGIATVTM
YFVSAVKGMI VTYNDVSATQ DKYFNASTIL LASSINFMSF VLVVKLILAI RSRRFLGLKQ
FDSFHILLIM SCQSLLVPSI IFILAYSLKP NQGTDVLTTV ATLLAVLSLP LSSMWATAAN
NASKTNTITS DFTTSTDRFY PGTLSSFQTD SINNDAKSSL RSRLYDLYPR RKETTSDKHS
ERTFVSETAD DIEKNQFYQL PTPTSSKNTR IGPFADASYK EGEVEPVDMY TPDTAADEEA
RKFWTEDNNN L
