| IED ID | IndEnz0018001436 |
| Enzyme Type ID | peroxidase001436 |
| Protein Name |
Regulator of G-protein signaling 1 AtRGS1 |
| Gene Name | RGS1 At3g26090 MPE11.27 MPE11.28 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MASGCALHGGCPSDYVAVAISVICFFVLLSRSVLPCLIHKAPRTNSSSFWIPVIQVISSFNLLFSIMMSVNLLRFRTKHWWRYCYLWAVWIEGPLGFGLLMSCRITQAFQLYFIFVKKRLPPVKSYIFLPLVLLPWIFGAAIIHATKPLNDKCHMGLQWTFPVAGLHALYVLALIAFTRAVRHVEFRFDELRDLWKGILVSATSIVIWVTAFVLNEIHEEISWLQVASRFVLLVTGGILVVVFFSISSNQPLLSQISLKKRQNFEFQRMGQALGIPDSGLLFRKEEFRPVDPNEPLDKLLLNKRFRHSFMEFADSCYAGETLHFFEEVYEHGKIPEDDSIRRIYMARHIMEKFIVAGAEMELNLSHKTRQEILTTQDLTHTDLFKNALNEVMQLIKMNLVRDYWSSIYFIKFKEEESCHEAMHKEGYSFSSPRLSSVQGSDDPFYQEHMSKSSRCSSPG |
| Enzyme Length | 459 |
| Uniprot Accession Number | Q8H1F2 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Glucose-regulated GTPase-accelerating protein (GAP) for the GTP-bound self-activating heterotrimeric G alpha protein GPA1. Cooperates with G beta-gamma dimers to maintain an unactivated but fully functional pool of GPA1. Phosphorylation-dependent endocytosis of RGS1 physically uncouples the two proteins, resulting in signal activation. Free AGB1 is essential, but not sufficient, for RGS1 endocytosis. Modulates cell proliferation, abscisic acid (ABA) and drought stress signal transduction by acting in a hexokinase-independent glucose-signaling pathway (PubMed:26528314). Involved in the shapes of leaves, the development of floral buds, the elongation of stems, siliques, and hypocotyls, the time of flowering and the regulation of guard-cell K(+) and anion channels. Important for the kinetics of voltage activation of inward K(+) current but not for the current amplitude. {ECO:0000269|PubMed:14500984, ECO:0000269|PubMed:15313575, ECO:0000269|PubMed:16361523, ECO:0000269|PubMed:16714312, ECO:0000269|PubMed:17951432, ECO:0000269|PubMed:18541915, ECO:0000269|PubMed:18817773, ECO:0000269|PubMed:21325279, ECO:0000269|PubMed:22940907, ECO:0000269|PubMed:26528314}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Erroneous gene model prediction (2); Modified residue (1); Mutagenesis (4); Region (1); Sequence conflict (1); Transmembrane (7) |
| Keywords | Cell membrane;Endosome;Membrane;Phosphoprotein;Reference proteome;Signal transduction inhibitor;Transmembrane;Transmembrane helix |
| Interact With | P18064 |
| Induction | INDUCTION: Up-regulated by ozone. {ECO:0000269|PubMed:21988569}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endosome membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=accumulates at the nascent cell plate during cytokinesis. {ECO:0000269|PubMed:14500984, ECO:0000269|PubMed:17951432, ECO:0000269|PubMed:22940907}. |
| Modified Residue | MOD_RES 428; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:22940907 |
| Post Translational Modification | PTM: Phosphorylated by WNK8 and WNK10, and in vitro by WNK1. Also phosphorylated at Ser-435 or Ser-436. {ECO:0000269|PubMed:22940907}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15313574; 15951850; 17317660; 18650403; 20862254; 22310500; 23329848; 23793400; 24151308; 24884438; 25568345; 25917395; 26935351; 27164033; 27235398; 27252940; 27923735; 28161903; 28187200; 28532301; 28545052; 28698136; 28747924; 28890722; 29287086; 29382719; 29545645; 30481338; 31055999; 31087771; 31245704; 31382426; 31461856; 31838952; 32290990; 33522388; 34376571; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,947 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |