GG2_ARATH
ID GG2_ARATH Reviewed; 100 AA.
AC Q93V47;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Guanine nucleotide-binding protein subunit gamma 2;
DE AltName: Full=Ggamma-subunit 2;
DE AltName: Full=Heterotrimeric G protein gamma-subunit 2;
DE Short=AtAGG2;
DE Flags: Precursor;
GN Name=GG2; Synonyms=AGG2; OrderedLocusNames=At3g22942; ORFNames=F5N5;
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], INTERACTION WITH GB1, TISSUE
RP SPECIFICITY, AND ALTERNATIVE SPLICING.
RC STRAIN=cv. Columbia;
RX PubMed=11513956; DOI=10.1016/s0167-4781(01)00262-7;
RA Mason M.G., Botella J.R.;
RT "Isolation of a novel G-protein gamma-subunit from Arabidopsis thaliana and
RT its interaction with Gbeta.";
RL Biochim. Biophys. Acta 1520:147-153(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBUNIT, PALMITOYLATION AT CYS-95, SUBCELLULAR LOCATION, INTERACTION WITH
RP GB1, AND MUTAGENESIS OF CYS-95 AND LEU-100.
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 FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
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 [9]
RP SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-95, ISOPRENYLATION AT CYS-97,
RP AND MUTAGENESIS OF 90-LYS--GLY-96; CYS-95 AND CYS-97.
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(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 basipetal 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 Plectosphaerella
CC cucumerina. {ECO:0000269|PubMed:17383830, ECO:0000269|PubMed:17468261,
CC ECO:0000269|PubMed:19948787, ECO:0000269|PubMed:20862254,
CC ECO:0000269|PubMed:21980142, ECO:0000269|PubMed:22209167}.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC GPG1 interacts with the beta subunit GB1. The dimer GB1-GG2 interacts
CC with NDL1, NDL2 and NDL3. Binds to NUDT7. {ECO:0000269|PubMed:11513956,
CC ECO:0000269|PubMed:17158913, ECO:0000269|PubMed:17468261,
CC ECO:0000269|PubMed:19948787, ECO:0000269|PubMed:22068106}.
CC -!- INTERACTION:
CC Q93V47; P49177: GB1; NbExp=2; IntAct=EBI-1751115, EBI-1632851;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17158913,
CC ECO:0000269|PubMed:17220359, ECO:0000269|PubMed:22068106}.
CC Note=Localized to the cell membrane when attached to beta subunit GB1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q93V47-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots (excluded from the
CC stele), seedlings (especially at the hypocotyl/root junction), floral
CC stems, floral buds, flowers and siliques, and, to a lower extent, in
CC leaves (restricted to guard cells). Also present in hydathods.
CC {ECO:0000269|PubMed:11513956, ECO:0000269|PubMed:17468261,
CC ECO:0000269|PubMed:18441222}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, first observed at the hypocotyl/root
CC junction but later confined to the root, including root hairs. In
CC flowers, expressed in the apex of stamen filaments at a very early
CC developmental stage and disappeared before the flower opened. Not
CC present in siliques. {ECO:0000269|PubMed:17468261,
CC ECO:0000269|PubMed:18441222}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitive to auxin-mediated induction of
CC lateral roots, within the epidermis and/or cortex, attenuating
CC basipetally transported auxin and graviresponsiveness. Enhanced
CC sensitivity to glucose. Abnormal roots architecture. Enhanced
CC susceptibility to necrotrophic and vascular pathogenic fungi, such as
CC Plectosphaerella cucumerina associated with a disturbed expression of
CC genes involved in cell wall metabolism (e.g. lower xylose content in
CC cell walls). {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; AF347077; AAK71536.1; -; mRNA.
DR EMBL; AF347078; AAK71537.1; -; Genomic_DNA.
DR EMBL; AP001300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE76694.1; -; Genomic_DNA.
DR EMBL; BT024657; ABD57482.1; -; mRNA.
DR EMBL; AK228306; BAF00249.1; -; mRNA.
DR RefSeq; NP_850746.1; NM_180415.3. [Q93V47-1]
DR AlphaFoldDB; Q93V47; -.
DR SMR; Q93V47; -.
DR BioGRID; 10846; 9.
DR IntAct; Q93V47; 2.
DR STRING; 3702.AT3G22942.1; -.
DR TCDB; 8.A.92.1.2; the g-protein AlphaBetaGama complex (gpc) family.
DR iPTMnet; Q93V47; -.
DR SwissPalm; Q93V47; -.
DR PaxDb; Q93V47; -.
DR PRIDE; Q93V47; -.
DR ProteomicsDB; 221832; -. [Q93V47-1]
DR EnsemblPlants; AT3G22942.1; AT3G22942.1; AT3G22942. [Q93V47-1]
DR GeneID; 825532; -.
DR Gramene; AT3G22942.1; AT3G22942.1; AT3G22942. [Q93V47-1]
DR KEGG; ath:AT3G22942; -.
DR Araport; AT3G22942; -.
DR TAIR; locus:1005471648; AT3G22942.
DR eggNOG; ENOG502S439; Eukaryota.
DR HOGENOM; CLU_105699_2_0_1; -.
DR InParanoid; Q93V47; -.
DR OMA; DASGCRC; -.
DR PhylomeDB; Q93V47; -.
DR PRO; PR:Q93V47; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93V47; baseline and differential.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0010540; P:basipetal auxin transport; 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; IMP:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; IMP:UniProtKB.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR Pfam; PF00631; G-gamma; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Coiled coil; Lipoprotein;
KW Membrane; Methylation; Palmitate; Prenylation; Reference proteome;
KW Transducer.
FT CHAIN 1..97
FT /note="Guanine nucleotide-binding protein subunit gamma 2"
FT /id="PRO_0000419815"
FT PROPEP 98..100
FT /note="Removed in mature form"
FT /id="PRO_0000419816"
FT DOMAIN 21..100
FT /note="G protein gamma"
FT REGION 90..96
FT /note="Regulates lipidation and cell membrane subcellular
FT localization"
FT COILED 19..55
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 97
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 95
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:17158913,
FT ECO:0000269|PubMed:17220359"
FT LIPID 97
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:17220359"
FT MUTAGEN 90..96
FT /note="KEAKRCG->NGGEGCR: Golgi and other internal membranes
FT subcellular localization, probably by reduced lipidation."
FT /evidence="ECO:0000269|PubMed:17220359"
FT MUTAGEN 95
FT /note="C->S: Loss of cell membrane attachment leading to
FT Golgi and other internal membranes subcellular
FT localization."
FT /evidence="ECO:0000269|PubMed:17158913,
FT ECO:0000269|PubMed:17220359"
FT MUTAGEN 97
FT /note="C->S: No prenylation and loss of cell membrane
FT attachment leading to cytoplasmic subcellular
FT localization."
FT /evidence="ECO:0000269|PubMed:17220359"
FT MUTAGEN 100
FT /note="L->LTEFNH: Loss of cell membrane attachment leading
FT to cytoplasmic subcellular localization."
FT /evidence="ECO:0000269|PubMed:17158913"
SQ SEQUENCE 100 AA; 11139 MW; F7CA80881064D4BB CRC64;
MEAGSSNSSG QLSGRVVDTR GKHRIQAELK RLEQEARFLE EELEQLEKMD NASASCKEFL
DSVDSKPDPL LPETTGPVNA TWDQWFEGPK EAKRCGCSIL
