GG1_ARATH
ID GG1_ARATH Reviewed; 98 AA.
AC Q9FDX9; Q9LY73;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Guanine nucleotide-binding protein subunit gamma 1;
DE AltName: Full=Ggamma-subunit 1;
DE AltName: Full=Heterotrimeric G protein gamma-subunit 1;
DE Short=AtAGG1;
DE Flags: Precursor;
GN Name=GG1; Synonyms=AGG1; OrderedLocusNames=At3g63420; ORFNames=MAA21.50;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), INTERACTION WITH GB1,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11121078; DOI=10.1073/pnas.97.26.14784;
RA Mason M.G., Botella J.R.;
RT "Completing the heterotrimer: isolation and characterization of an
RT Arabidopsis thaliana G protein gamma-subunit cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14784-14788(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH GB1.
RX PubMed=17158913; DOI=10.1242/jcs.03284;
RA Adjobo-Hermans M.J.W., Goedhart J., Gadella T.W.J. Jr.;
RT "Plant G protein heterotrimers require dual lipidation motifs of Galpha and
RT Ggamma and do not dissociate upon activation.";
RL J. Cell Sci. 119:5087-5097(2006).
RN [7]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=17383830; DOI=10.1016/j.gene.2007.02.008;
RA Chakravorty D., Botella J.R.;
RT "Over-expression of a truncated Arabidopsis thaliana heterotrimeric G
RT protein gamma subunit results in a phenotype similar to alpha and beta
RT subunit knockouts.";
RL Gene 393:163-170(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION BY ALTERNARIA BRASSICICOLA AND FUSARIUM OXYSPORUM.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=17468261; DOI=10.1105/tpc.107.050096;
RA Trusov Y., Rookes J.E., Tilbrook K., Chakravorty D., Mason M.G.,
RA Anderson D., Chen J.-G., Jones A.M., Botella J.R.;
RT "Heterotrimeric G protein gamma subunits provide functional selectivity in
RT Gbetagamma dimer signaling in Arabidopsis.";
RL Plant Cell 19:1235-1250(2007).
RN [10]
RP SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-93, ISOPRENYLATION AT CYS-95,
RP AND MUTAGENESIS OF 88-ASN--ARG-94; CYS-93 AND CYS-95.
RX PubMed=17220359; DOI=10.1104/pp.106.093583;
RA Zeng Q., Wang X., Running M.P.;
RT "Dual lipid modification of Arabidopsis Ggamma-subunits is required for
RT efficient plasma membrane targeting.";
RL Plant Physiol. 143:1119-1131(2007).
RN [11]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=18441222; DOI=10.1104/pp.108.117655;
RA Trusov Y., Zhang W., Assmann S.M., Botella J.R.;
RT "Ggamma1 + Ggamma2 not equal to Gbeta: heterotrimeric G protein Ggamma-
RT deficient mutants do not recapitulate all phenotypes of Gbeta-deficient
RT mutants.";
RL Plant Physiol. 147:636-649(2008).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH NDL1; NDL2 AND NDL3.
RC STRAIN=cv. Columbia;
RX PubMed=19948787; DOI=10.1105/tpc.109.065557;
RA Mudgil Y., Uhrig J.F., Zhou J., Temple B., Jiang K., Jones A.M.;
RT "Arabidopsis N-MYC DOWNREGULATED-LIKE1, a positive regulator of auxin
RT transport in a G protein-mediated pathway.";
RL Plant Cell 21:3591-3609(2009).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20862254; DOI=10.1371/journal.pone.0012833;
RA Booker K.S., Schwarz J., Garrett M.B., Jones A.M.;
RT "Glucose attenuation of auxin-mediated bimodality in lateral root formation
RT is partly coupled by the heterotrimeric G protein complex.";
RL PLoS ONE 5:E12833-E12833(2010).
RN [14]
RP INTERACTION WITH NUDT7, AND SUBCELLULAR LOCATION.
RX PubMed=22068106;
RA Olejnik K., Bucholc M., Anielska-Mazur A., Lipko A., Kujawa M.,
RA Modzelan M., Augustyn A., Kraszewska E.;
RT "Arabidopsis thaliana Nudix hydrolase AtNUDT7 forms complexes with the
RT regulatory RACK1A protein and Ggamma subunits of the signal transducing
RT heterotrimeric G protein.";
RL Acta Biochim. Pol. 58:609-616(2011).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22209167; DOI=10.1016/j.jplph.2011.11.010;
RA Thung L., Trusov Y., Chakravorty D., Botella J.R.;
RT "Ggamma1+Ggamma2+Ggamma3=Gbeta: the search for heterotrimeric G-protein
RT gamma subunits in Arabidopsis is over.";
RL J. Plant Physiol. 169:542-545(2012).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21980142; DOI=10.1093/mp/ssr082;
RA Delgado-Cerezo M., Sanchez-Rodriguez C., Escudero V., Miedes E.,
RA Fernandez P.V., Jorda L., Hernandez-Blanco C., Sanchez-Vallet A.,
RA Bednarek P., Schulze-Lefert P., Somerville S., Estevez J.M., Persson S.,
RA Molina A.;
RT "Arabidopsis heterotrimeric G-protein regulates cell wall defense and
RT resistance to necrotrophic fungi.";
RL Mol. Plant 5:98-114(2012).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as a modulator or transducer in various transmembrane signaling
CC systems. The beta and gamma chains are required for the GTPase
CC activity, for replacement of GDP by GTP, and for G protein-effector
CC interaction. Involved in the abscisic acid (ABA) and ethylene signaling
CC pathways. Regulates acropetal transport of auxin (IAA) in roots and
CC hypocotyls, and thus modulates root architecture (e.g. lateral root
CC formation). The heterotrimeric G-protein controls defense responses to
CC necrotrophic and vascular fungi probably by modulating cell wall-
CC related genes expression; involved in resistance to fungal pathogens
CC such as Alternaria brassicicola, Plectosphaerella cucumerina and
CC Fusarium oxysporum. {ECO:0000269|PubMed:17383830,
CC ECO:0000269|PubMed:17468261, ECO:0000269|PubMed:19948787,
CC ECO:0000269|PubMed:20862254, ECO:0000269|PubMed:21980142,
CC ECO:0000269|PubMed:22209167}.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC Interacts with the beta subunit GB1. The dimer GB1-GG1 interacts with
CC NDL1, NDL2 and NDL3. Binds to NUDT7. {ECO:0000269|PubMed:11121078,
CC ECO:0000269|PubMed:17158913, ECO:0000269|PubMed:17468261,
CC ECO:0000269|PubMed:19948787, ECO:0000269|PubMed:22068106}.
CC -!- INTERACTION:
CC Q9FDX9; P49177: GB1; NbExp=8; IntAct=EBI-1750878, EBI-1632851;
CC Q9FDX9; P93397; Xeno; NbExp=4; IntAct=EBI-1750878, EBI-1750986;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17158913,
CC ECO:0000269|PubMed:17220359, ECO:0000269|PubMed:17644812}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:17158913,
CC ECO:0000269|PubMed:17220359}. Golgi apparatus, trans-Golgi network
CC membrane. Cytoplasm. Note=Localized to the cell membrane when attached
CC to beta subunit GB1 (Probable) (PubMed:17158913). Present in the
CC cytoplasm when associated with NUDT7 (PubMed:22068106).
CC {ECO:0000269|PubMed:17158913, ECO:0000269|PubMed:22068106,
CC ECO:0000305|PubMed:22068106}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FDX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FDX9-2; Sequence=VSP_044366;
CC -!- TISSUE SPECIFICITY: Mostly expressed in seedlings (especially at the
CC hypocotyl/root junction), young cauline leaves, open flowers, and
CC floral stems, and, to a lower extent, in roots (restricted to the
CC stele), rosette leaves (restricted to veins), siliques, and unopened
CC floral buds. Also present in hydathods. {ECO:0000269|PubMed:11121078,
CC ECO:0000269|PubMed:17468261, ECO:0000269|PubMed:18441222}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, first observed at the hypocotyl/root
CC junction but later confined to the hypocotyl. In flowers, restricted to
CC the stigma of mature flowers. In siliques, confined to the abscission
CC zone. {ECO:0000269|PubMed:17468261, ECO:0000269|PubMed:18441222}.
CC -!- INDUCTION: Induced locally by Alternaria brassicicola but systemically
CC by Fusarium oxysporum. {ECO:0000269|PubMed:17468261}.
CC -!- DISRUPTION PHENOTYPE: Enhanced susceptibility to Alternaria
CC brassicicola, Plectosphaerella cucumerina and Fusarium oxysporum
CC associated with a disturbed expression of genes involved in cell wall
CC metabolism (e.g. lower xylose content in cell walls). Reduced induction
CC of the plant defensin gene PDF1.2, and decreased sensitivity to methyl
CC jasmonate (MeJA). Hypersensitive to auxin-mediated induction of lateral
CC roots, within the central cylinder, attenuating acropetally transported
CC auxin signaling. Enhanced sensitivity to glucose and mannitol during
CC seed germination. Abnormal roots architecture.
CC {ECO:0000269|PubMed:17468261, ECO:0000269|PubMed:19948787,
CC ECO:0000269|PubMed:20862254, ECO:0000269|PubMed:21980142,
CC ECO:0000269|PubMed:22209167}.
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DR EMBL; AF283673; AAG45959.1; -; mRNA.
DR EMBL; AF283674; AAG45960.1; -; Genomic_DNA.
DR EMBL; AL163818; CAB87795.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80479.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80480.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63533.1; -; Genomic_DNA.
DR EMBL; AK175815; BAD43578.1; -; mRNA.
DR EMBL; BT024540; ABD38879.1; -; mRNA.
DR PIR; T49183; T49183.
DR RefSeq; NP_001325615.1; NM_001340213.1. [Q9FDX9-2]
DR RefSeq; NP_567147.1; NM_116207.3. [Q9FDX9-1]
DR RefSeq; NP_850741.1; NM_180410.1. [Q9FDX9-1]
DR AlphaFoldDB; Q9FDX9; -.
DR SMR; Q9FDX9; -.
DR BioGRID; 10831; 12.
DR IntAct; Q9FDX9; 5.
DR STRING; 3702.AT3G63420.1; -.
DR TCDB; 8.A.92.1.2; the g-protein AlphaBetaGama complex (gpc) family.
DR SwissPalm; Q9FDX9; -.
DR PaxDb; Q9FDX9; -.
DR PRIDE; Q9FDX9; -.
DR ProteomicsDB; 221831; -. [Q9FDX9-1]
DR EnsemblPlants; AT3G63420.1; AT3G63420.1; AT3G63420. [Q9FDX9-1]
DR EnsemblPlants; AT3G63420.2; AT3G63420.2; AT3G63420. [Q9FDX9-1]
DR EnsemblPlants; AT3G63420.3; AT3G63420.3; AT3G63420. [Q9FDX9-2]
DR GeneID; 825517; -.
DR Gramene; AT3G63420.1; AT3G63420.1; AT3G63420. [Q9FDX9-1]
DR Gramene; AT3G63420.2; AT3G63420.2; AT3G63420. [Q9FDX9-1]
DR Gramene; AT3G63420.3; AT3G63420.3; AT3G63420. [Q9FDX9-2]
DR KEGG; ath:AT3G63420; -.
DR Araport; AT3G63420; -.
DR TAIR; locus:2087398; AT3G63420.
DR eggNOG; ENOG502S439; Eukaryota.
DR HOGENOM; CLU_105699_2_0_1; -.
DR InParanoid; Q9FDX9; -.
DR OrthoDB; 1597898at2759; -.
DR PRO; PR:Q9FDX9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9FDX9; baseline and differential.
DR Genevisible; Q9FDX9; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:TAIR.
DR GO; GO:0010541; P:acropetal auxin transport; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; ISS:UniProtKB.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR045878; GG1/2.
DR PANTHER; PTHR35129; PTHR35129; 1.
DR Pfam; PF00631; G-gamma; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Cell membrane; Coiled coil; Cytoplasm;
KW Golgi apparatus; Lipoprotein; Membrane; Methylation; Palmitate;
KW Plant defense; Prenylation; Reference proteome; Transducer.
FT CHAIN 1..95
FT /note="Guanine nucleotide-binding protein subunit gamma 1"
FT /id="PRO_0000419813"
FT PROPEP 96..98
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000419814"
FT DOMAIN 19..98
FT /note="G protein gamma"
FT REGION 88..94
FT /note="Regulates lipidation and cell membrane subcellular
FT localization"
FT COILED 20..50
FT /evidence="ECO:0000255"
FT MOD_RES 95
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 93
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:17220359"
FT LIPID 95
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:17220359"
FT VAR_SEQ 1
FT /note="M -> MEGKSRFESERERLRRQFKLVRTKTRLSLTLSDLRPASERM (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044366"
FT MUTAGEN 88..94
FT /note="NGGEGCR->KEAKRCG: Plasma membrane only localization,
FT probably by increased lipidation."
FT /evidence="ECO:0000269|PubMed:17220359"
FT MUTAGEN 93
FT /note="C->S: Normal subcellular localization."
FT /evidence="ECO:0000269|PubMed:17220359"
FT MUTAGEN 95
FT /note="C->S: No prenylation and loss of cell membrane and
FT Golgi apparatus attachment leading to cytoplasmic
FT subcellular localization."
FT /evidence="ECO:0000269|PubMed:17220359"
SQ SEQUENCE 98 AA; 10947 MW; F032D1883E59538B CRC64;
MREETVVYEQ EESVSHGGGK HRILAELARV EQEVAFLEKE LKEVENTDIV STVCEELLSV
IEKGPDPLLP LTNGPLNLGW DRWFEGPNGG EGCRCLIL
