##gff-version 3 P08539 UniProtKB Initiator methionine 1 1 . . . Note=Removed P08539 UniProtKB Chain 2 472 . . . ID=PRO_0000203616;Note=Guanine nucleotide-binding protein alpha-1 subunit P08539 UniProtKB Domain 40 472 . . . Note=G-alpha;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01230 P08539 UniProtKB Region 43 56 . . . Note=G1 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01230 P08539 UniProtKB Region 127 235 . . . Note=Insert%3B not present in other G-proteins P08539 UniProtKB Region 162 199 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P08539 UniProtKB Region 292 300 . . . Note=G2 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01230 P08539 UniProtKB Region 315 324 . . . Note=G3 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01230 P08539 UniProtKB Region 384 391 . . . Note=G4 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01230 P08539 UniProtKB Region 442 447 . . . Note=G5 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01230 P08539 UniProtKB Compositional bias 175 191 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P08539 UniProtKB Binding site 48 55 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P08539 UniProtKB Binding site 55 55 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P08539 UniProtKB Binding site 294 300 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P08539 UniProtKB Binding site 300 300 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P08539 UniProtKB Binding site 319 323 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P08539 UniProtKB Binding site 388 391 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P08539 UniProtKB Binding site 444 444 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P08539 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1936988,ECO:0000269|PubMed:8415763,ECO:0000269|PubMed:8702760;Dbxref=PMID:1936988,PMID:8415763,PMID:8702760 P08539 UniProtKB Lipidation 3 3 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10712512,ECO:0000269|PubMed:8942643;Dbxref=PMID:10712512,PMID:8942643 P08539 UniProtKB Cross-link 165 165 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11955054;Dbxref=PMID:11955054 P08539 UniProtKB Mutagenesis 2 2 . . . Note=Abolishes both palmitoylation and N-myristoylation. G->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10712512,ECO:0000269|PubMed:8702760,ECO:0000269|PubMed:8942643;Dbxref=PMID:10712512,PMID:8702760,PMID:8942643 P08539 UniProtKB Mutagenesis 3 3 . . . Note=Abolishes palmitoylation but not N-myristoylation. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10712512,ECO:0000269|PubMed:8942643;Dbxref=PMID:10712512,PMID:8942643 P08539 UniProtKB Mutagenesis 15 15 . . . Note=Slightly reduces ligand-dependent pheromone signaling. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14767760;Dbxref=PMID:14767760 P08539 UniProtKB Mutagenesis 17 17 . . . Note=Leads to a hypersensitive signaling phenotype resulting in greatly enhanced signal at low alpha-factor concentrations. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14767760;Dbxref=PMID:14767760 P08539 UniProtKB Mutagenesis 18 18 . . . Note=Reduces ligand-dependent pheromone signaling. L->P%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14767760;Dbxref=PMID:14767760 P08539 UniProtKB Mutagenesis 21 22 . . . Note=Impairs interaction with FUS3. KR->EE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12029138;Dbxref=PMID:12029138 P08539 UniProtKB Mutagenesis 50 50 . . . Note=Confers insensitivity to pheromone. G->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10705368,ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:2117698,ECO:0000269|PubMed:2548076;Dbxref=PMID:10705368,PMID:1900495,PMID:2117698,PMID:2548076 P08539 UniProtKB Mutagenesis 50 50 . . . Note=Has increased GTP occupancy and moderately reduces hydrolysis of GTP%2C resulting in a constitutively active form that down-regulates the pheromone response and causes hyperadaptation to pheromone. G->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10705368,ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:2117698,ECO:0000269|PubMed:2548076;Dbxref=PMID:10705368,PMID:1900495,PMID:2117698,PMID:2548076 P08539 UniProtKB Mutagenesis 54 54 . . . Note=Prevents GDP to GTP exchange%3B suppressor of L-323. K->E%2CI;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14767760,ECO:0000269|PubMed:9786851;Dbxref=PMID:14767760,PMID:9786851 P08539 UniProtKB Mutagenesis 165 165 . . . Note=Substantial decrease in ubiquitination. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11955054;Dbxref=PMID:11955054 P08539 UniProtKB Mutagenesis 297 297 . . . Note=Slows hydrolysis of GTP. R->H P08539 UniProtKB Mutagenesis 302 302 . . . Note=In GPA1(SST)%3B weakens interaction to SST2 and blocks its negative regulatory effect. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9488712;Dbxref=PMID:9488712 P08539 UniProtKB Mutagenesis 321 321 . . . Note=Causes a specific mating defect in alpha cells. G->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9604890;Dbxref=PMID:9604890 P08539 UniProtKB Mutagenesis 322 322 . . . Note=Confers insensitivity to pheromone. G->A%2CE%2CR;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:2117698,ECO:0000269|PubMed:8887662;Dbxref=PMID:1900495,PMID:2117698,PMID:8887662 P08539 UniProtKB Mutagenesis 323 323 . . . Note=Prevents hydrolysis of GTP%3B eliminates the interaction with STE4 and constitutively activates the pheromone response pathway. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9604890;Dbxref=PMID:9604890 P08539 UniProtKB Mutagenesis 327 327 . . . Note=Suppressor of L-323%3B does not prevent GTP binding to GPA1. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9786851;Dbxref=PMID:9786851 P08539 UniProtKB Mutagenesis 345 345 . . . Note=Suppressor of a STE2-L236H mutant. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866688;Dbxref=PMID:10866688 P08539 UniProtKB Mutagenesis 353 353 . . . Note=Suppressor of L-323. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9786851;Dbxref=PMID:9786851 P08539 UniProtKB Mutagenesis 355 355 . . . Note=Confers insensitivity to pheromone. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2117698;Dbxref=PMID:2117698 P08539 UniProtKB Mutagenesis 364 364 . . . Note=Enhances the rate of GDP for GTP exchange and slows hydrolysis of GTP%2C resulting in a constitutively active form that down-regulates the pheromone response independently of the pheromone receptor. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11394869,ECO:0000269|PubMed:2117698,ECO:0000269|PubMed:8887662;Dbxref=PMID:11394869,PMID:2117698,PMID:8887662 P08539 UniProtKB Mutagenesis 388 388 . . . Note=Forms a nondissociable complex with the pheromone receptor in response to receptor activation%2C resulting in reduced pheromone responsiveness. N->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11394869,ECO:0000269|PubMed:15197187,ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:8887662;Dbxref=PMID:11394869,PMID:15197187,PMID:1900495,PMID:8887662 P08539 UniProtKB Mutagenesis 388 388 . . . Note=Causes constitutive activation of the pheromone response pathway. N->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11394869,ECO:0000269|PubMed:15197187,ECO:0000269|PubMed:1900495,ECO:0000269|PubMed:8887662;Dbxref=PMID:11394869,PMID:15197187,PMID:1900495,PMID:8887662 P08539 UniProtKB Mutagenesis 391 391 . . . Note=Causes constitutive activation of the pheromone response pathway. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1900495;Dbxref=PMID:1900495 P08539 UniProtKB Mutagenesis 467 467 . . . Note=Impairs pheromone signaling in a and alpha cells. K->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1848203;Dbxref=PMID:1848203 P08539 UniProtKB Mutagenesis 468 468 . . . Note=Impairs pheromone signaling specifically in a cells. K->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1848203;Dbxref=PMID:1848203 P08539 UniProtKB Mutagenesis 470 470 . . . Note=Confers insensitivity to pheromone. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2117698;Dbxref=PMID:2117698 P08539 UniProtKB Sequence conflict 82 82 . . . Note=W->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P08539 UniProtKB Sequence conflict 194 194 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 P08539 UniProtKB Sequence conflict 226 226 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 P08539 UniProtKB Sequence conflict 246 246 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P08539 UniProtKB Sequence conflict 469 469 . . . Note=I->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P08539 UniProtKB Beta strand 303 309 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AD3 P08539 UniProtKB Beta strand 311 319 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AD3 P08539 UniProtKB Turn 325 329 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AD3 P08539 UniProtKB Helix 330 335 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AD3 P08539 UniProtKB Beta strand 338 344 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AD3 P08539 UniProtKB Helix 360 373 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AD3 P08539 UniProtKB Beta strand 379 381 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AD3 P08539 UniProtKB Beta strand 383 388 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AD3 P08539 UniProtKB Helix 390 396 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AD3 P08539 UniProtKB Beta strand 403 405 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AD3 P08539 UniProtKB Helix 417 428 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AD3 P08539 UniProtKB Beta strand 437 441 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AD3 P08539 UniProtKB Helix 450 465 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AD3 P08539 UniProtKB Turn 466 468 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7AD3