##gff-version 3
P10823	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
P10823	UniProtKB	Chain	2	449	.	.	.	ID=PRO_0000203617;Note=Guanine nucleotide-binding protein alpha-2 subunit	
P10823	UniProtKB	Domain	122	448	.	.	.	Note=G-alpha;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01230	
P10823	UniProtKB	Region	1	91	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P10823	UniProtKB	Region	125	138	.	.	.	Note=G1 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01230	
P10823	UniProtKB	Region	268	276	.	.	.	Note=G2 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01230	
P10823	UniProtKB	Region	292	301	.	.	.	Note=G3 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01230	
P10823	UniProtKB	Region	361	368	.	.	.	Note=G4 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01230	
P10823	UniProtKB	Region	418	423	.	.	.	Note=G5 motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01230	
P10823	UniProtKB	Compositional bias	1	24	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P10823	UniProtKB	Compositional bias	38	61	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P10823	UniProtKB	Compositional bias	71	91	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P10823	UniProtKB	Binding site	130	137	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P10823	UniProtKB	Binding site	137	137	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P10823	UniProtKB	Binding site	270	276	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P10823	UniProtKB	Binding site	276	276	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P10823	UniProtKB	Binding site	296	300	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P10823	UniProtKB	Binding site	365	368	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P10823	UniProtKB	Binding site	420	420	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P10823	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250	
P10823	UniProtKB	Lipidation	4	4	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250	
P10823	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Abolishes both palmitoylation and N-myristoylation. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250	
P10823	UniProtKB	Mutagenesis	4	4	.	.	.	Note=Abolishes palmitoylation but not N-myristoylation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250	
P10823	UniProtKB	Mutagenesis	6	6	.	.	.	Note=Abolishes both palmitoylation and N-myristoylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030250;Dbxref=PMID:16030250	
P10823	UniProtKB	Mutagenesis	132	132	.	.	.	Note=Locks GPA2 in its activated GTP-bound form and abrogates the negative control by RGS2. G->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10523302,ECO:0000269|PubMed:12150916;Dbxref=PMID:10523302,PMID:12150916	
P10823	UniProtKB	Mutagenesis	299	299	.	.	.	Note=Dominant negative allele unable to undergo the GTP-induced conformational change. G->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12150916,ECO:0000269|PubMed:16030250;Dbxref=PMID:12150916,PMID:16030250	
P10823	UniProtKB	Mutagenesis	300	300	.	.	.	Note=Dominant active allele that abolishes intrinsic GTPase activity. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12150916;Dbxref=PMID:12150916	
P10823	UniProtKB	Sequence conflict	375	375	.	.	.	Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305