STE2_YEASX
ID STE2_YEASX Reviewed; 431 AA.
AC P0CI39; P06842; Q70D63; Q70D65; Q70D69; Q70D73; Q70D74;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Pheromone alpha factor receptor;
GN Name=STE2;
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-34; THR-176; GLY-201;
RP ILE-294; GLU-337; ASN-370 AND LEU-394.
RC STRAIN=CBS 5287 / CLIB 219, CLIB 388, CLIB 410, CLIB 413, CLIB 556,
RC CLIB 630, CLIB 95,
RC Diastaticus / ATCC 13007 / CBS 1782 / CLIB 382 / NBRC 1046 / NRRL Y-2416,
RC K1, R12, R13, Sigma 1278B, YIIc12, and YIIc17;
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).
CC -!- FUNCTION: Receptor for the peptide pheromone alpha factor, the mating
CC factor of yeast. {ECO:0000250}.
CC -!- INTERACTION:
CC P0CI39; P11972: SST2; Xeno; NbExp=4; IntAct=EBI-18360, EBI-18232;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: N-glycosylation may be involved in the sorting process
CC for misfolded STE2 protein. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 4 family.
CC {ECO:0000305}.
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DR EMBL; AJ585737; CAE52257.1; -; Genomic_DNA.
DR EMBL; AJ585738; CAE52258.1; -; Genomic_DNA.
DR EMBL; AJ585739; CAE52259.1; -; Genomic_DNA.
DR EMBL; AJ585740; CAE52260.1; -; Genomic_DNA.
DR EMBL; AJ585741; CAE52261.1; -; Genomic_DNA.
DR EMBL; AJ585742; CAE52262.1; -; Genomic_DNA.
DR EMBL; AJ585743; CAE52263.1; -; Genomic_DNA.
DR EMBL; AJ585744; CAE52264.1; -; Genomic_DNA.
DR EMBL; AJ585745; CAE52265.1; -; Genomic_DNA.
DR EMBL; AJ585746; CAE52266.1; -; Genomic_DNA.
DR EMBL; AJ585747; CAE52267.1; -; Genomic_DNA.
DR EMBL; AJ585748; CAE52268.1; -; Genomic_DNA.
DR EMBL; AJ585749; CAE52269.1; -; Genomic_DNA.
DR EMBL; AJ585750; CAE52270.1; -; Genomic_DNA.
DR EMBL; AJ585751; CAE52271.1; -; Genomic_DNA.
DR EMBL; AJ585752; CAE52272.1; -; Genomic_DNA.
DR EMBL; AJ585753; CAE52273.1; -; Genomic_DNA.
DR EMBL; AJ585754; CAE52274.1; -; Genomic_DNA.
DR AlphaFoldDB; P0CI39; -.
DR BMRB; P0CI39; -.
DR SMR; P0CI39; -.
DR IntAct; P0CI39; 23.
DR MINT; P0CI39; -.
DR VEuPathDB; FungiDB:YFL026W; -.
DR PhylomeDB; P0CI39; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004932; F:mating-type factor pheromone receptor activity; IEA:InterPro.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
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 G-protein coupled receptor; Glycoprotein; Isopeptide bond; Membrane;
KW Pheromone response; Phosphoprotein; Receptor; Transducer; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..431
FT /note="Pheromone alpha factor receptor"
FT /id="PRO_0000402383"
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:0000250|UniProtKB:D6VTK4"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D6VTK4"
FT MOD_RES 329
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D6VTK4"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D6VTK4"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D6VTK4"
FT MOD_RES 363
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D6VTK4"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D6VTK4"
FT MOD_RES 382
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D6VTK4"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D6VTK4"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D6VTK4"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D6VTK4"
FT MOD_RES 414
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D6VTK4"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CROSSLNK 374
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:D6VTK4"
FT CROSSLNK 400
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:D6VTK4"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:D6VTK4"
FT VARIANT 34
FT /note="S -> T (in strain: CLIB 95, CLIB 219, CLIB 382, CLIB
FT 388, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 176
FT /note="A -> T (in strain: CLIB 95, CLIB 382, CLIB 388, CLIB
FT 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 201
FT /note="D -> G (in strain: CLIB 95, CLIB 219, CLIB 382, CLIB
FT 388, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 294
FT /note="M -> I (in strain: CLIB 630 haplotype Ha2)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 337
FT /note="K -> E (in strain: CLIB 388, YIIc12 haplotype Ha2
FT and YIIc17 haplotype Ha2)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 370
FT /note="D -> N (in strain: CLIB 95, CLIB 219, CLIB 382, CLIB
FT 388, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 394
FT /note="F -> L (in strain: R12 haplotype Ha2)"
FT /evidence="ECO:0000269|PubMed:15087486"
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
