Gene Details:
- Gene ID: AT2G26300
- Gene Symbol: ATGPA1, GP ALPHA 1, GPA1
- Gene Name: ARABIDOPSIS THALIANA G PROTEIN ALPHA SUBUNIT 1, G protein alpha subunit 1, G PROTEIN ALPHA SUBUNIT 1
- Description: G protein alpha subunit 1;(source:Araport11)
- TAIR Accession: locus:2005529
- Genome: Araport11_genome_release
- Species: Arabidopsis thaliana
Transcripts:
Plant Ontology Annotations:
- PO:0000293 — guard cell — célula guardiana (Spanish, exact), occlusive cell (exact), 孔辺細胞 (Japanese, exact)
- PO:0009005 — root — raíz (Spanish, exact), radices (exact, plural), radix (exact), 根 (Japanese, exact), aerial root (narrow), climbing root (narrow)
- PO:0009006 — shoot system — sistema de epiblasto (epiblastema) (Spanish, exact), シュート系、苗条系 (Japanese, exact), Poaceae crown (related), shoot (related), thalli (related), thallus (related), tree crown (narrow)
- PO:0009009 — plant embryo — embrión (Spanish, exact), 植物胚 (Japanese, exact), germ (related), embryo (broad)
- PO:0009029 — stamen — estambre (Spanish, exact), 雄蕊 (Japanese, exact), Poaceae stamen (narrow), Zea stamen (narrow)
- PO:0009052 — inflorescence flower pedicel — 小花柄 (Japanese, related), pedicelo (Spanish, broad)
- PO:0020030 — cotyledon — cotiledón (Spanish, exact), seed leaf (exact), 子葉 (Japanese, exact)
- PO:0020038 — petiole — pecíolo (Spanish, exact), 葉柄 (Japanese, exact)
- PO:0020100 — hypocotyl — hipocótile (Spanish, exact), 胚軸 (Japanese, exact)
- PO:0020137 — leaf apex — ápice de la hoja (Spanish, exact), 葉先 (Japanese, exact), leaf lamina apex (narrow), phyllid apex (narrow)
- PO:0025022 — collective leaf structure — estructura colectiva de hoja (Spanish, exact), leaf series (exact), 葉が集まった構造 (Japanese, exact), leaf whorl (narrow), rosette (narrow), cycle (broad), verticil (broad)
- PO:0025281 — pollen — polen (Spanish, exact), pollen grain (exact), 花粉 (Japanese, exact)
Gene Ontology:
- GO:0006499 — has protein modification of type — N-terminal protein myristoylation
- GO:0005515 — enables — protein binding
- GO:0009738 — involved in — abscisic acid-activated signaling pathway
- GO:0010027 — acts upstream of or within — thylakoid membrane organization
- GO:0009845 — acts upstream of or within — seed germination
- GO:0005834 — part of — heterotrimeric G-protein complex
- GO:0003924 — enables — GTPase activity
- GO:0010119 — acts upstream of or within — regulation of stomatal movement
- GO:0005525 — enables — GTP binding
- GO:0005737 — located in — cytoplasm
- GO:0009506 — located in — plasmodesma
- GO:0005886 — located in — plasma membrane
- GO:0009785 — involved in — blue light signaling pathway
- GO:0009740 — acts upstream of or within — gibberellic acid mediated signaling pathway
- GO:0003376 — acts upstream of or within — sphingosine-1-phosphate receptor signaling pathway
- GO:0006571 — acts upstream of or within — tyrosine biosynthetic process
- GO:0001664 — enables — G protein-coupled receptor binding
- GO:0005777 — located in — peroxisome
- GO:0005789 — located in — endoplasmic reticulum membrane
- GO:0031683 — enables — G-protein beta/gamma-subunit complex binding
- GO:0005095 — enables — GTPase inhibitor activity
- GO:0042127 — acts upstream of or within — regulation of cell population proliferation
- GO:0019236 — involved in — response to pheromone
- GO:0009789 — acts upstream of or within — positive regulation of abscisic acid-activated signaling pathway
- GO:0007186 — involved in — G protein-coupled receptor signaling pathway
- GO:0072593 — acts upstream of or within — reactive oxygen species metabolic process
- GO:0016247 — enables — channel regulator activity
- GO:0007188 — involved in — adenylate cyclase-modulating G protein-coupled receptor signaling pathway
- GO:0097468 — acts upstream of or within — programmed cell death in response to reactive oxygen species
- GO:0009738 — acts upstream of or within — abscisic acid-activated signaling pathway
- GO:0009094 — acts upstream of or within — L-phenylalanine biosynthetic process
- GO:0090333 — involved in — regulation of stomatal closure
- GO:0051020 — enables — GTPase binding
- GO:0009749 — acts upstream of or within — response to glucose
- GO:0010244 — acts upstream of or within — response to low fluence blue light stimulus by blue low-fluence system
Function-related keywords:
- guard cell , root , shoot system , plant embryo , stamen , inflorescence flower pedicel , cotyledon , petiole , hypocotyl , leaf apex , collective leaf structure , pollen
Literature:
- Genetic variation within and among populations of Arabidopsis thaliana. DOI: 10.1093/genetics/148.3.1311 ; PMID: 9539444
- The G protein alpha subunit (GP alpha1) is associated with the ER and the plasma membrane in meristematic cells of Arabidopsis and cauliflower. DOI: 10.1016/s0014-5793(97)00378-5 ; PMID: 9175885
- Molecular cloning and characterization of a cDNA for the alpha subunit of a G protein from rice. DOI: 10.1093/oxfordjournals.pcp.a078767 ; PMID: 7767602
- Molecular cloning and characterization of RGA1 encoding a G protein alpha subunit from rice (Oryza sativa L. IR-36). DOI: 10.1007/BF00020885 ; PMID: 7766894
- Immunolocalization of the G protein alpha subunit encoded by the GPA1 gene in Arabidopsis. DOI: 10.1105/tpc.5.11.1513 ; PMID: 8312737
- Isolation and sequence analysis of TGA1 cDNAs encoding a tomato G protein alpha subunit. DOI: 10.1016/0378-1119(91)90318-6 ; PMID: 1748292
- Molecular cloning and characterization of GPA1, a G protein alpha subunit gene from Arabidopsis thaliana. DOI: 10.1073/pnas.87.10.3821 ; PMID: 2111018
- Completing the heterotrimer: isolation and characterization of an Arabidopsis thaliana G protein gamma-subunit cDNA. DOI: 10.1073/pnas.97.26.14784 ; PMID: 11121078
- Plant G proteins: the different faces of GPA1. DOI: 10.1016/s0960-9822(01)00519-x ; PMID: 11696344
- Modulation of cell proliferation by heterotrimeric G protein in Arabidopsis. DOI: 10.1126/science.1059040 ; PMID: 11408654
- G protein regulation of ion channels and abscisic acid signaling in Arabidopsis guard cells. DOI: 10.1126/science.1059046 ; PMID: 11408655
- Role of a heterotrimeric G protein in regulation of Arabidopsis seed germination. DOI: 10.1104/pp.005017 ; PMID: 12068128
- Genomic structure and homoeologous relationship of the two alpha-subunit genes of a heterotrimeric GTP-binding protein in tobacco. DOI: 10.1139/g02-029 ; PMID: 12175065
- The beta-subunit of the Arabidopsis G protein negatively regulates auxin-induced cell division and affects multiple developmental processes. DOI: 10.1105/tpc.006148 ; PMID: 12566580
- A reevaluation of the role of the heterotrimeric G protein in coupling light responses in Arabidopsis. DOI: 10.1104/pp.102.017624 ; PMID: 12692321
- Sphingolipid signalling in Arabidopsis guard cells involves heterotrimeric G proteins. DOI: 10.1038/nature01643 ; PMID: 12789341
- The Arabidopsis cupin domain protein AtPirin1 interacts with the G protein alpha-subunit GPA1 and regulates seed germination and early seedling development. DOI: 10.1105/tpc.011890 ; PMID: 12837948
- Unexpected protein families including cell defense components feature in the N-myristoylome of a higher eukaryote. DOI: 10.1074/jbc.M307321200 ; PMID: 12912986
- A seven-transmembrane RGS protein that modulates plant cell proliferation. DOI: 10.1126/science.1087790 ; PMID: 14500984
- The G-protein-coupled receptor GCR1 regulates DNA synthesis through activation of phosphatidylinositol-specific phospholipase C. DOI: 10.1104/pp.103.026005 ; PMID: 12972659
- The Arabidopsis putative G protein-coupled receptor GCR1 interacts with the G protein alpha subunit GPA1 and regulates abscisic acid signaling. DOI: 10.1105/tpc.020321 ; PMID: 15155892
- GCR1 can act independently of heterotrimeric G-protein in response to brassinosteroids and gibberellins in Arabidopsis seed germination. DOI: 10.1104/pp.104.038992 ; PMID: 15181210
- Arabidopsis sphingosine kinase and the effects of phytosphingosine-1-phosphate on stomatal aperture. DOI: 10.1104/pp.104.055806 ; PMID: 15665242
- Different signaling and cell death roles of heterotrimeric G protein alpha and beta subunits in the Arabidopsis oxidative stress response to ozone. DOI: 10.1105/tpc.104.029603 ; PMID: 15705948
- Extracellular calmodulin-induced stomatal closure is mediated by heterotrimeric G protein and H2O2. DOI: 10.1104/pp.104.047837 ; PMID: 15557100
- ERECTA receptor-like kinase and heterotrimeric G protein from Arabidopsis are required for resistance to the necrotrophic fungus Plectosphaerella cucumerina. DOI: 10.1111/j.1365-313X.2005.02440.x ; PMID: 15998304
- G-protein-coupled receptor 1, G-protein Galpha-subunit 1, and prephenate dehydratase 1 are required for blue light-induced production of phenylalanine in etiolated Arabidopsis. DOI: 10.1104/pp.105.071282 ; PMID: 16415218
- Mapping the Arabidopsis organelle proteome. DOI: 10.1073/pnas.0506958103 ; PMID: 16618929
- A bifurcating pathway directs abscisic acid effects on stomatal closure and opening in Arabidopsis. DOI: 10.1126/science.1123769 ; PMID: 16614222
- The plastid protein THYLAKOID FORMATION1 and the plasma membrane G-protein GPA1 interact in a novel sugar-signaling mechanism in Arabidopsis. DOI: 10.1105/tpc.105.037259 ; PMID: 16582010
- G-protein complex mutants are hypersensitive to abscisic acid regulation of germination and postgermination development. DOI: 10.1104/pp.106.079038 ; PMID: 16581874
- Differential roles of Arabidopsis heterotrimeric G-protein subunits in modulating cell division in roots. DOI: 10.1104/pp.106.079202 ; PMID: 16679415
- The GCR1, GPA1, PRN1, NF-Y signal chain mediates both blue light and abscisic acid responses in Arabidopsis. DOI: 10.1104/pp.106.089904 ; PMID: 17322342
- Heterotrimeric G protein signaling in the Arabidopsis unfolded protein response. DOI: 10.1073/pnas.0611735104 ; PMID: 17360436
- A G protein-coupled receptor is a plasma membrane receptor for the plant hormone abscisic acid. DOI: 10.1126/science.1135882 ; PMID: 17347412
- Genetic characterization reveals no role for the reported ABA receptor, GCR2, in ABA control of seed germination and early seedling development in Arabidopsis. DOI: 10.1111/j.1365-313X.2007.03291.x ; PMID: 17894782
- GTPase acceleration as the rate-limiting step in Arabidopsis G protein-coupled sugar signaling. DOI: 10.1073/pnas.0704751104 ; PMID: 17951432
- Arabidopsis extra-large G proteins (XLGs) regulate root morphogenesis. DOI: 10.1111/j.1365-313X.2007.03335.x ; PMID: 17999646
- Ggamma1 + Ggamma2 not equal to Gbeta: heterotrimeric G protein Ggamma-deficient mutants do not recapitulate all phenotypes of Gbeta-deficient mutants. DOI: 10.1104/pp.108.117655 ; PMID: 18441222
- Heterotrimeric G-proteins in plant development. DOI: 10.2741/2928 ; PMID: 18508435
- Loss-of-function mutations in the Arabidopsis heterotrimeric G-protein alpha subunit enhance the developmental defects of brassinosteroid signaling and biosynthesis mutants. DOI: 10.1093/pcp/pcn078 ; PMID: 18499742
- and RGS-deficient Arabidopsis lines. DOI: 10.1073/pnas.0800980105 ; PMID: 18541915
- Whole proteome identification of plant candidate G-protein coupled receptors in Arabidopsis, rice, and poplar: computational prediction and in-vivo protein coupling. DOI: 10.1186/gb-2008-9-7-r120 ; PMID: 18671868
- Global analysis of Arabidopsis gene expression uncovers a complex array of changes impacting pathogen response and cell cycle during geminivirus infection. DOI: 10.1104/pp.108.121038 ; PMID: 18650403
- The plant innate immunity response in stomatal guard cells invokes G-protein-dependent ion channel regulation. DOI: 10.1111/j.1365-313X.2008.03657.x ; PMID: 18702674
- D-Glucose sensing by a plasma membrane regulator of G signaling protein, AtRGS1. DOI: 10.1016/j.febslet.2008.08.038 ; PMID: 18817773
- Heterotrimeric G-protein is involved in phytochrome A-mediated cell death of Arabidopsis hypocotyls. DOI: 10.1038/cr.2008.271 ; PMID: 19160542
- Activation of the heterotrimeric G protein alpha-subunit GPA1 suppresses the ftsh-mediated inhibition of chloroplast development in Arabidopsis. DOI: 10.1111/j.1365-313X.2009.03843.x ; PMID: 19228339
- The heterotrimeric G-protein complex modulates light sensitivity in Arabidopsis thaliana seed germination. DOI: 10.1111/j.1751-1097.2008.00505.x ; PMID: 19192205
- A signaling pathway linking nitric oxide production to heterotrimeric G protein and hydrogen peroxide regulates extracellular calmodulin induction of stomatal closure in Arabidopsis. DOI: 10.1104/pp.109.137067 ; PMID: 19321706
- Two novel GPCR-type G proteins are abscisic acid receptors in Arabidopsis. DOI: 10.1016/j.cell.2008.12.026 ; PMID: 19135895
- Arabidopsis nucleoside diphosphate kinase-2 as a plant GTPase activating protein. DOI: 10.5483/bmbrep.2008.41.9.645 ; PMID: 18823588
- The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits. DOI: 10.7150/ijbs.1.51 ; PMID: 15951850
- Heterotrimeric G-protein signaling in Arabidopsis: Puzzling G-protein-coupled receptor. DOI: 10.4161/psb.3.12.6064 ; PMID: 19513236
- Dissection of the relationship between RACK1 and heterotrimeric G-proteins in Arabidopsis. DOI: 10.1093/pcp/pcp113 ; PMID: 19651700
- Opposite ends of the spectrum: plant and animal g-protein signaling. DOI: 10.4161/psb.2.6.4497 ; PMID: 19704591
- Arabidopsis MPK3, a Key Signalling Intermediate in Stomatal Function. DOI: 10.4161/psb.2.4.3896 ; PMID: 19704678
- Arabidopsis extra large G-protein 2 (XLG2) interacts with the Gbeta subunit of heterotrimeric G protein and functions in disease resistance. DOI: 10.1093/mp/ssp001 ; PMID: 19825634
- ABA-regulated G protein signaling in Arabidopsis guard cells: a proteomic perspective. DOI: 10.1021/pr901011h ; PMID: 20166762
- The alpha-subunit of the Arabidopsis heterotrimeric G protein, GPA1, is a regulator of transpiration efficiency. DOI: 10.1104/pp.109.148262 ; PMID: 20200073
- Identification of novel proteins involved in plant cell-wall synthesis based on protein-protein interaction data. DOI: 10.1021/pr100249c ; PMID: 20687615
- Glucose attenuation of auxin-mediated bimodality in lateral root formation is partly coupled by the heterotrimeric G protein complex. DOI: 10.1371/journal.pone.0012833 ; PMID: 20862254
- Heterotrimeric G-protein regulation of ROS signalling and calcium currents in Arabidopsis guard cells. DOI: 10.1093/jxb/erq424 ; PMID: 21262908
- The crystal structure of a self-activating G protein alpha subunit reveals its distinct mechanism of signal initiation. DOI: 10.1126/scisignal.2001446 ; PMID: 21304159
- ABA-dependent and -independent G-protein signaling in Arabidopsis roots revealed through an iTRAQ proteomics approach. DOI: 10.1021/pr2001786 ; PMID: 21545083
- Minimal influence of G-protein null mutations on ozone-induced changes in gene expression, foliar injury, gas exchange and peroxidase activity in Arabidopsis thaliana L. DOI: 10.1111/j.1365-3040.2011.02443.x ; PMID: 21988569
- The GCR1 and GPA1 participate in promotion of Arabidopsis primary root elongation induced by N-acyl-homoserine lactones, the bacterial quorum-sensing signals. DOI: 10.1094/MPMI-10-11-0274 ; PMID: 22250582
- Ca2+-dependent GTPase, extra-large G protein 2 (XLG2), promotes activation of DNA-binding protein related to vernalization 1 (RTV1), leading to activation of floral integrator genes and early flowering in Arabidopsis. DOI: 10.1074/jbc.M111.317412 ; PMID: 22232549
- Gγ1+Gγ2+Gγ3=Gβ: the search for heterotrimeric G-protein γ subunits in Arabidopsis is over. DOI: 10.1016/j.jplph.2011.11.010 ; PMID: 22209167
- The plant-specific G protein γ subunit AGG3 influences organ size and shape in Arabidopsis thaliana. DOI: 10.1111/j.1469-8137.2012.04083.x ; PMID: 22380792
- Systematic identification of functional plant modules through the integration of complementary data sources. DOI: 10.1104/pp.112.196725 ; PMID: 22589469
- cry1 and GPA1 signaling genetically interact in hook opening and anthocyanin synthesis in Arabidopsis. DOI: 10.1007/s11103-012-9950-x ; PMID: 22855128
- Role and interrelationship of Gα protein, hydrogen peroxide, and nitric oxide in ultraviolet B-induced stomatal closure in Arabidopsis leaves. DOI: 10.1104/pp.112.211623 ; PMID: 23341360
- Heterotrimeric G proteins serve as a converging point in plant defense signaling activated by multiple receptor-like kinases. DOI: 10.1104/pp.112.212431 ; PMID: 23424249
- Abscisic acid-responsive guard cell metabolomes of Arabidopsis wild-type and gpa1 G-protein mutants. DOI: 10.1105/tpc.113.119800 ; PMID: 24368793
- Arabidopsis heterotrimeric G-proteins play a critical role in host and nonhost resistance against Pseudomonas syringae pathogens. DOI: 10.1371/journal.pone.0082445 ; PMID: 24349286
- Abscisic acid signalling determines susceptibility of bundle sheath cells to photoinhibition in high light-exposed Arabidopsis leaves. DOI: 10.1098/rstb.2013.0234 ; PMID: 24591719
- Significant reduction of BiFC non-specific assembly facilitates in planta assessment of heterotrimeric G-protein interactors. DOI: 10.1111/tpj.12639 ; PMID: 25187041
- Adaptive evolution of signaling partners. DOI: 10.1093/molbev/msu404 ; PMID: 25568345
- Heterotrimeric G protein mediates ethylene-induced stomatal closure via hydrogen peroxide synthesis in Arabidopsis. DOI: 10.1111/tpj.12799 ; PMID: 25704455
- Ethylene mediates brassinosteroid-induced stomatal closure via Gα protein-activated hydrogen peroxide and nitric oxide production in Arabidopsis. DOI: 10.1111/tpj.12815 ; PMID: 25754244
- Extra-Large G Proteins Expand the Repertoire of Subunits in Arabidopsis Heterotrimeric G Protein Signaling. DOI: 10.1104/pp.15.00251 ; PMID: 26157115
- Heterotrimeric G protein subunits differentially respond to endoplasmic reticulum stress in Arabidopsis. DOI: 10.1080/15592324.2015.1061162 ; PMID: 26237103
- Endogenous Arabidopsis messenger RNAs transported to distant tissues. DOI: 10.1038/nplants.2015.25 ; PMID: 27247031
- G-protein α-subunit (GPA1) regulates stress, nitrate and phosphate response, flavonoid biosynthesis, fruit/seed development and substantially shares GCR1 regulation in A. thaliana. DOI: 10.1007/s11103-015-0374-2 ; PMID: 26346778
- G-protein Signaling Components GCR1 and GPA1 Mediate Responses to Multiple Abiotic Stresses in Arabidopsis. DOI: 10.3389/fpls.2015.01000 ; PMID: 26635828
- Cell-free translation and purification of Arabidopsis thaliana regulator of G signaling 1 protein. DOI: 10.1016/j.pep.2016.04.016 ; PMID: 27164033
- Heterotrimeric G-proteins facilitate resistance to plant pathogenic viruses in Arabidopsis thaliana (L.) Heynh. DOI: 10.1080/15592324.2016.1212798 ; PMID: 27454415
- Growth attenuation under saline stress is mediated by the heterotrimeric G protein complex. DOI: 10.1186/1471-2229-14-129 ; PMID: 24884438
- EXTRA-LARGE G PROTEINs Interact with E3 Ligases PUB4 and PUB2 and Function in Cytokinin and Developmental Processes. DOI: 10.1104/pp.16.00816 ; PMID: 27986866
- Ligand-induced dynamics of heterotrimeric G protein-coupled receptor-like kinase complexes. DOI: 10.1371/journal.pone.0171854 ; PMID: 28187200
- Heterotrimeric G-protein regulatory circuits in plants: Conserved and novel mechanisms. DOI: 10.1080/15592324.2017.1325983 ; PMID: 28532301
- Dynamic G protein alpha signaling in Arabidopsis innate immunity. DOI: 10.1016/j.bbrc.2017.07.040 ; PMID: 28698136
- Endocytosis of AtRGS1 Is Regulated by the Autophagy Pathway after D-Glucose Stimulation. DOI: 10.3389/fpls.2017.01229 ; PMID: 28747924
- Tyrosine phosphorylation switching of a G protein. DOI: 10.1074/jbc.RA117.000163 ; PMID: 29382719
- Phytomelatonin receptor PMTR1-mediated signaling regulates stomatal closure in Arabidopsis thaliana. DOI: 10.1111/jpi.12500 ; PMID: 29702752
- The Arabidopsis heterotrimeric G-protein β subunit, AGB1, is required for guard cell calcium sensing and calcium-induced calcium release. DOI: 10.1111/tpj.14318 ; PMID: 30882980
- GCR1 and GPA1 coupling regulates nitrate, cell wall, immunity and light responses in Arabidopsis. DOI: 10.1038/s41598-019-42084-2 ; PMID: 30967583
- BAK1-mediated phosphorylation of canonical G protein alpha during flagellin signaling in Arabidopsis. DOI: 10.1111/jipb.12824 ; PMID: 31087771
- JA-Induced Endocytosis of AtRGS1 Is Involved in G-Protein Mediated JA Responses. DOI: 10.3390/ijms20153779 ; PMID: 31382426
- Receptor-Like Kinase Phosphorylation of Arabidopsis Heterotrimeric G-Protein Gα -Subunit AtGPA1. DOI: 10.1002/pmic.201900265 ; PMID: 31693794
- Nucleotide exchange-dependent and nucleotide exchange-independent functions of plant heterotrimeric GTP-binding proteins. DOI: 10.1126/scisignal.aav9526 ; PMID: 31690635
- An atypical heterotrimeric Gα protein has substantially reduced nucleotide binding but retains nucleotide-independent interactions with its cognate RGS protein and Gβγ dimer. DOI: 10.1080/07391102.2019.1704879 ; PMID: 31838952
- Crosstalk between heterotrimeric G protein-coupled signaling pathways and WRKY transcription factors modulating plant responses to suboptimal micronutrient conditions. DOI: 10.1093/jxb/eraa108 ; PMID: 32107545
- GTP binding by Arabidopsis extra-large G protein 2 is not essential for its functions. DOI: 10.1093/plphys/kiab119 ; PMID: 33729516
- A G protein-coupled receptor-like module regulates cellulose synthase secretion from the endomembrane system in Arabidopsis. DOI: 10.1016/j.devcel.2021.03.031 ; PMID: 33878345
- Differential responses of G-protein Arabidopsis thaliana mutants to ozone. DOI: 10.1111/j.1469-8137.2004.01081.x ; PMID: 33873772
- Cantil: a previously unreported organ in wild-type Arabidopsis regulated by FT, ERECTA and heterotrimeric G proteins. DOI: 10.1242/dev.195545 ; PMID: 34129030
- The stress induced caleosin, RD20/CLO3, acts as a negative regulator of GPA1 in Arabidopsis. DOI: 10.1007/s11103-021-01189-x ; PMID: 34599731
- The Melatonin Receptor CAND2/PMTR1 Is Involved in the Regulation of Mitochondrial Gene Expression under Photooxidative Stress. DOI: 10.1134/S1607672922010021 ; PMID: 35275300
- Evolutionarily Conserved and Non-Conserved Roles of Heterotrimeric Gα Proteins of Plants. DOI: 10.1093/pcp/pcac045 ; PMID: 35388418
- Dark secrets of phytomelatonin. DOI: 10.1093/jxb/erac168 ; PMID: 35522068
- and Ethylene-Induced Stomatal Closure via Activating GPA1-Dependent ROS and NO Production. DOI: 10.3390/ijms23105512 ; PMID: 35628324
- The caleosin CLO7 and its role in the heterotrimeric G-protein signalling network. DOI: 10.1016/j.jplph.2022.153841 ; PMID: 36334585
- The G protein alpha subunit (GP alpha1) is associated with the ER and the plasma membrane in meristematic cells of Arabidopsis and cauliflower. DOI: 10.1016/s0014-5793(97)00378-5 ; PMID: 9175885
- Isolation of a putative receptor from Zea mays microsomal membranes that interacts with the G-protein, GP alpha 1. DOI: 10.1016/s0014-5793(94)80076-6 ; PMID: 7805845
- Isolation and sequence analysis of TGA1 cDNAs encoding a tomato G protein alpha subunit. DOI: 10.1016/0378-1119(91)90318-6 ; PMID: 1748292
- Molecular cloning and characterization of GPA1, a G protein alpha subunit gene from Arabidopsis thaliana. DOI: 10.1073/pnas.87.10.3821 ; PMID: 2111018
- G protein regulation of ion channels and abscisic acid signaling in Arabidopsis guard cells. DOI: 10.1126/science.1059046 ; PMID: 11408655
- Unexpected protein families including cell defense components feature in the N-myristoylome of a higher eukaryote. DOI: 10.1074/jbc.M307321200 ; PMID: 12912986
- Mapping the Arabidopsis organelle proteome. DOI: 10.1073/pnas.0506958103 ; PMID: 16618929
- Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis. DOI: 10.1074/mcp.M600429-MCP200 ; PMID: 17317660
- A high content in lipid-modified peripheral proteins and integral receptor kinases features in the arabidopsis plasma membrane proteome. DOI: 10.1074/mcp.M700099-MCP200 ; PMID: 17644812
- Regulation of root-wave response by extra large and conventional G proteins in Arabidopsis thaliana. DOI: 10.1111/j.1365-313X.2008.03506.x ; PMID: 18397373
Sequences:
cDNA Sequence
- >AT2G26300.1
GTTAACTTAATAGTATATAAAATAAAAATGCATATAGGTTCCGTAATTAATCTTCTTTATCGTCACGAGAGGCACATCTTTTTTCAACATTTGACCACTCTCTCTCTCTCTCTCTCAGGACCTTTCGGCGTAATTTCGTCTTCCCCTTTGCTTAACATTTTCTTTCTTTCTTTTTGACCAAATATTAAAAATATATCCATTTTTATTTTATTTTTAATTAAATTCATAATTTGCATTTTATGTATTTATAATAAAAAGGAGAGAATAAATCCAAAAGAGTGAAGCAAAAACATTAAAGCGGAAAGAAAGTGGTAAAACAATAATAGAAACAGGAGAAGCAGAAGTACTACTTCTTCTTCTTCTGCTCTCTTCTCAGACCTTGTTTTGTACTTTCTTCTTCTTCTTCTTCTTCTTGTTTGCGAACTCCGATATCTTCTTCACTACCTTTGACTCCATTTCTTTTTCTTCTTCAGGTGTAGGCATTGTCTTGTTATGAGAAGCAACTGTAGCTGGAAGCTCAAGTATTTGTTTTTAGCTGTGGAGCTTGAATCTTGATAGTTTTCGACTTCTATGTTATTACCTGTGGGGATATAGAAACAATCATGGGCTTACTCTGCAGTAGAAGTCGACATCATACTGAAGATACTGATGAGAATACACAGGCTGCTGAAATCGAAAGACGGATAGAGCAAGAAGCAAAGGCTGAAAAGCATATTCGGAAGCTTTTGCTACTTGGTGCTGGGGAATCTGGAAAATCTACAATTTTTAAGCAGATAAAACTTCTATTCCAAACGGGATTTGATGAAGGAGAACTAAAGAGCTATGTTCCAGTCATTCATGCCAATGTCTATCAGACTATAAAATTATTGCATGATGGAACAAAGGAGTTTGCTCAAAATGAAACAGATTCTGCTAAATATATGTTATCTTCTGAAAGTATTGCAATTGGGGAGAAACTATCTGAGATTGGTGGTAGGTTAGACTATCCACGTCTTACCAAGGACATCGCTGAGGGAATAGAAACACTATGGAAGGATCCTGCAATTCAGGAAACTTGTGCTCGTGGTAATGAGCTTCAGGTTCCTGATTGTACGAAATATCTGATGGAGAACTTGAAGAGACTATCAGATATAAATTATATTCCAACTAAGGAGGATGTACTTTATGCAAGAGTTCGCACAACTGGTGTCGTGGAAATACAGTTCAGCCCTGTGGGAGAGAATAAAAAAAGTGGTGAAGTGTACCGATTGTTTGACGTGGGTGGACAGAGAAATGAGAGGAGGAAATGGATTCATCTGTTTGAAGGTGTAACAGCTGTGATATTTTGTGCTGCCATCAGCGAGTACGACCAAACGCTCTTTGAGGACGAGCAGAAAAACAGGATGATGGAGACCAAGGAATTATTCGACTGGGTCCTGAAACAACCCTGTTTTGAGAAAACATCCTTCATGCTGTTCTTGAACAAGTTCGACATATTTGAGAAGAAAGTTCTTGACGTTCCGTTGAACGTTTGCGAGTGGTTCAGAGATTACCAACCAGTTTCAAGTGGGAAACAAGAGATTGAGCATGCATACGAGTTTGTGAAGAAGAAGTTTGAGGAGTTATATTACCAGAACACGGCGCCGGATAGAGTGGACAGGGTATTCAAAATCTACAGGACGACGGCTTTGGACCAGAAGCTTGTAAAGAAAACGTTCAAGCTCGTAGATGAGACACTAAGAAGGAGAAATTTACTGGAGGCTGGCCTTTTATGACCTTATTATTACATATCTCTAGTAAATTACCTCTCCTTATTATTATAAGAAAAACTCGAAAACTGAATGACCGTGTAATTTATCTTTCGGGACAAAAGACTTAGCGATTCAAAATCTAATGTGTCTCGATGGCTACGACTAGTTTCTATTTTATCATTGTTTTTGTTAACATTCCTCTGTCTTTGACTTCTTATTTTTTTTTCTCATCAAAAACATCTCATTTTGATCTTGTTTTTGGGGTTATATTATTATTAAAATGAGGCATCCACATCCCGAAATC - >AT2G26300.2
GTTAACTTAATAGTATATAAAATAAAAATGCATATAGGTTCCGTAATTAATCTTCTTTATCGTCACGAGAGGCACATCTTTTTTCAACATTTGACCACTCTCTCTCTCTCTCTCTCAGGACCTTTCGGCGTAATTTCGTCTTCCCCTTTGCTTAACATTTTCTTTCTTTCTTTTTGACCAAATATTAAAAATATATCCATTTTTATTTTATTTTTAATTAAATTCATAATTTGCATTTTATGTATTTATAATAAAAAGGAGAGAATAAATCCAAAAGAGTGAAGCAAAAACATTAAAGCGGAAAGAAAGTGGTAAAACAATAATAGAAACAGGAGAAGCAGAAGTACTACTTCTTCTTCTTCTGCTCTCTTCTCAGACCTTGTTTTGTACTTTCTTCTTCTTCTTCTTCTTCTTGTTTGCGAACTCCGATATCTTCTTCACTACCTTTGACTCCATTTCTTTTTCTTCTTCAGGTGTAGGCATTGTCTTGTTATGAGAAGCAACTGTAGCTGGAAGCTCAAGTATTTGTTTTTAGCTGTGGAGCTTGAATCTTGATAGTTTTCGACTTCTATGTTATTACCTGTGGGGATATAGAAACAATCATGGGCTTACTCTGCAGTAGAAGTCGACATCATACTGAAGATACTGATGAGAATACACAGGCTGCTGAAATCGAAAGACGGATAGAGCAAGAAGCAAAGGCTGAAAAGCATATTCGGAAGCTTTTGCTACTTGGTGCTGGGGAATCTGGAAAATCTACAATTTTTAAGCAGATAAAACTTCTATTCCAAACGGGATTTGATGAAGGAGAACTAAAGAGCTATGTTCCAGTCATTCATGCCAATGTCTATCAGACTATAAAATTATTGCATGATGGAACAAAGGAGTTTGCTCAAAATGAAACAGATTCTGCTAAATATATGTTATCTTCTGAAAGTATTGCAATTGGGGAGAAACTATCTGAGATTGGTGGTAGGTTAGACTATCCACGTCTTACCAAGGACATCGCTGAGGGAATAGAAACACTATGGAAGGATCCTGCAATTCAGGAAACTTGTGCTCGTGGTAATGAGCTTCAGGTTCCTGATTGTACGAAATATCTGATGGAGAACTTGAAGAGACTATCAGATATAAATTATATTCCAACTAAGGAGGATGTACTTTATGCAAGAGTTCGCACAACTGGTGTCGTGGAAATACAGTTCAGCCCTGTGGGAGAGAATAAAAAAAGTGGTGAAGTGTACCGATTGTTTGACGTGGGTGGACAGAGAAATGAGAGGAGGAAATGGATTCATCTGTTTGAAGGTGTAACAGCTGTGATATTTTGTGCTGCCATCAGCGAGTACGACCAAACGCTCTTTGAGGACGAGCAGAAAAACAGGATGATGGAGACCAAGGAATTATTCGACTGGGTCCTGAAACAACCCTGTTTTGAGAAAACATCCTTCATGCTGTTCTTGAACAAGTTCGACATATTTGAGAAGAAAGTTCTTGACGTTCCGTTGAACGTTTGCGAGTGGTTCAGAGATTACCAACCAGTTTCAAGTGGGAAACAAGAGATTGAGCATGCATACGAGTTTGTGAAGAAGAAGTTTGAGGAGTTATATTACCAGAACACGGCGCCGGATAGAGTGGACAGGGTATTCAAAATCTACAGGACGACGGCTTTGGACCAGAAGCTTGTAAAGAAAACGTTCAAGCTCGTAGATGAGACACTAAGAAGGAGAAATTTACTGGAGGCTGGCCTTTTATGACCTTATTATTACATATCTCTAGTAAATTACCTCTCCTTATTATTATAAGAAAAACTCGAAAACTGAATGACCGTGTAATTTATCTTTCGGGACAAAAGACTTAGCGATTCAAAATCTAATGTGTCTCGATGGCTACGACTAGTTTCTATTTTATCATTGTTTTTGTTAACATTCCTCTGTCTTTGACTTCTTATTTTTTTTTCTCATCAAAAACATCTCATTTTGATCTTGTTTTTGGGGTTATATTATTATTAAAATGAGGCATCCACATCCCGAAATC
CDS Sequence
- >AT2G26300.1
ATGGGCTTACTCTGCAGTAGAAGTCGACATCATACTGAAGATACTGATGAGAATACACAGGCTGCTGAAATCGAAAGACGGATAGAGCAAGAAGCAAAGGCTGAAAAGCATATTCGGAAGCTTTTGCTACTTGGTGCTGGGGAATCTGGAAAATCTACAATTTTTAAGCAGATAAAACTTCTATTCCAAACGGGATTTGATGAAGGAGAACTAAAGAGCTATGTTCCAGTCATTCATGCCAATGTCTATCAGACTATAAAATTATTGCATGATGGAACAAAGGAGTTTGCTCAAAATGAAACAGATTCTGCTAAATATATGTTATCTTCTGAAAGTATTGCAATTGGGGAGAAACTATCTGAGATTGGTGGTAGGTTAGACTATCCACGTCTTACCAAGGACATCGCTGAGGGAATAGAAACACTATGGAAGGATCCTGCAATTCAGGAAACTTGTGCTCGTGGTAATGAGCTTCAGGTTCCTGATTGTACGAAATATCTGATGGAGAACTTGAAGAGACTATCAGATATAAATTATATTCCAACTAAGGAGGATGTACTTTATGCAAGAGTTCGCACAACTGGTGTCGTGGAAATACAGTTCAGCCCTGTGGGAGAGAATAAAAAAAGTGGTGAAGTGTACCGATTGTTTGACGTGGGTGGACAGAGAAATGAGAGGAGGAAATGGATTCATCTGTTTGAAGGTGTAACAGCTGTGATATTTTGTGCTGCCATCAGCGAGTACGACCAAACGCTCTTTGAGGACGAGCAGAAAAACAGGATGATGGAGACCAAGGAATTATTCGACTGGGTCCTGAAACAACCCTGTTTTGAGAAAACATCCTTCATGCTGTTCTTGAACAAGTTCGACATATTTGAGAAGAAAGTTCTTGACGTTCCGTTGAACGTTTGCGAGTGGTTCAGAGATTACCAACCAGTTTCAAGTGGGAAACAAGAGATTGAGCATGCATACGAGTTTGTGAAGAAGAAGTTTGAGGAGTTATATTACCAGAACACGGCGCCGGATAGAGTGGACAGGGTATTCAAAATCTACAGGACGACGGCTTTGGACCAGAAGCTTGTAAAGAAAACGTTCAAGCTCGTAGATGAGACACTAAGAAGGAGAAATTTACTGGAGGCTGGCCTTTTATGA - >AT2G26300.2
ATGGGCTTACTCTGCAGTAGAAGTCGACATCATACTGAAGATACTGATGAGAATACACAGGCTGCTGAAATCGAAAGACGGATAGAGCAAGAAGCAAAGGCTGAAAAGCATATTCGGAAGCTTTTGCTACTTGGTGCTGGGGAATCTGGAAAATCTACAATTTTTAAGCAGATAAAACTTCTATTCCAAACGGGATTTGATGAAGGAGAACTAAAGAGCTATGTTCCAGTCATTCATGCCAATGTCTATCAGACTATAAAATTATTGCATGATGGAACAAAGGAGTTTGCTCAAAATGAAACAGATTCTGCTAAATATATGTTATCTTCTGAAAGTATTGCAATTGGGGAGAAACTATCTGAGATTGGTGGTAGGTTAGACTATCCACGTCTTACCAAGGACATCGCTGAGGGAATAGAAACACTATGGAAGGATCCTGCAATTCAGGAAACTTGTGCTCGTGGTAATGAGCTTCAGGTTCCTGATTGTACGAAATATCTGATGGAGAACTTGAAGAGACTATCAGATATAAATTATATTCCAACTAAGGAGGATGTACTTTATGCAAGAGTTCGCACAACTGGTGTCGTGGAAATACAGTTCAGCCCTGTGGGAGAGAATAAAAAAAGTGGTGAAGTGTACCGATTGTTTGACGTGGGTGGACAGAGAAATGAGAGGAGGAAATGGATTCATCTGTTTGAAGGTGTAACAGCTGTGATATTTTGTGCTGCCATCAGCGAGTACGACCAAACGCTCTTTGAGGACGAGCAGAAAAACAGGATGATGGAGACCAAGGAATTATTCGACTGGGTCCTGAAACAACCCTGTTTTGAGAAAACATCCTTCATGCTGTTCTTGAACAAGTTCGACATATTTGAGAAGAAAGTTCTTGACGTTCCGTTGAACGTTTGCGAGTGGTTCAGAGATTACCAACCAGTTTCAAGTGGGAAACAAGAGATTGAGCATGCATACGAGTTTGTGAAGAAGAAGTTTGAGGAGTTATATTACCAGAACACGGCGCCGGATAGAGTGGACAGGGTATTCAAAATCTACAGGACGACGGCTTTGGACCAGAAGCTTGTAAAGAAAACGTTCAAGCTCGTAGATGAGACACTAAGAAGGAGAAATTTACTGGAGGCTGGCCTTTTATGA
Protein Sequence
- >AT2G26300.1
MGLLCSRSRHHTEDTDENTQAAEIERRIEQEAKAEKHIRKLLLLGAGESGKSTIFKQIKLLFQTGFDEGELKSYVPVIHANVYQTIKLLHDGTKEFAQNETDSAKYMLSSESIAIGEKLSEIGGRLDYPRLTKDIAEGIETLWKDPAIQETCARGNELQVPDCTKYLMENLKRLSDINYIPTKEDVLYARVRTTGVVEIQFSPVGENKKSGEVYRLFDVGGQRNERRKWIHLFEGVTAVIFCAAISEYDQTLFEDEQKNRMMETKELFDWVLKQPCFEKTSFMLFLNKFDIFEKKVLDVPLNVCEWFRDYQPVSSGKQEIEHAYEFVKKKFEELYYQNTAPDRVDRVFKIYRTTALDQKLVKKTFKLVDETLRRRNLLEAGLL - >AT2G26300.2
MGLLCSRSRHHTEDTDENTQAAEIERRIEQEAKAEKHIRKLLLLGAGESGKSTIFKQIKLLFQTGFDEGELKSYVPVIHANVYQTIKLLHDGTKEFAQNETDSAKYMLSSESIAIGEKLSEIGGRLDYPRLTKDIAEGIETLWKDPAIQETCARGNELQVPDCTKYLMENLKRLSDINYIPTKEDVLYARVRTTGVVEIQFSPVGENKKSGEVYRLFDVGGQRNERRKWIHLFEGVTAVIFCAAISEYDQTLFEDEQKNRMMETKELFDWVLKQPCFEKTSFMLFLNKFDIFEKKVLDVPLNVCEWFRDYQPVSSGKQEIEHAYEFVKKKFEELYYQNTAPDRVDRVFKIYRTTALDQKLVKKTFKLVDETLRRRNLLEAGLL