XLG2_ARATH
ID XLG2_ARATH Reviewed; 861 AA.
AC C6KIE6; Q9SZ04;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Extra-large guanine nucleotide-binding protein 2;
DE AltName: Full=Extra-large GTP-binding protein 2;
DE Short=Extra-large G-protein 2;
GN Name=XLG2; OrderedLocusNames=At4g34390; ORFNames=F10M10.160;
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 [MRNA], GENE FAMILY, NOMENCLATURE, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=17999646; DOI=10.1111/j.1365-313x.2007.03335.x;
RA Ding L., Pandey S., Assmann S.M.;
RT "Arabidopsis extra-large G proteins (XLGs) regulate root morphogenesis.";
RL Plant J. 53:248-263(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 INDUCTION, DISRUPTION PHENOTYPE, FUNCTION, AND INTERACTION WITH GB1.
RX PubMed=19825634; DOI=10.1093/mp/ssp001;
RA Zhu H., Li G.J., Ding L., Cui X., Berg H., Assmann S.M., Xia Y.;
RT "Arabidopsis extra large G-protein 2 (XLG2) interacts with the Gbeta
RT subunit of heterotrimeric G protein and functions in disease resistance.";
RL Mol. Plant 2:513-525(2009).
RN [5]
RP INTERACTION WITH RTV1, FUNCTION, COFACTOR, GTP-BINDING, AND MUTAGENESIS OF
RP THR-476.
RX PubMed=22232549; DOI=10.1074/jbc.m111.317412;
RA Heo J.B., Sung S., Assmann S.M.;
RT "Ca2+-dependent GTPase, extra-large G protein 2 (XLG2), promotes activation
RT of DNA-binding protein related to vernalization 1 (RTV1), leading to
RT activation of floral integrator genes and early flowering in Arabidopsis.";
RL J. Biol. Chem. 287:8242-8253(2012).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling systems
CC (By similarity). Binds GTP with specificity. Plays a role in the root
CC morphogenesis by regulation of the cell proliferation. Acts as a
CC positive regulator in resistance to pathogen that triggers the
CC salicylic acid (SA) pathway. Promotes the DNA binding activity of RTV1
CC specifically to promoter regions of FT and SOC1 in vivo leading to the
CC activation of floral integrator genes. {ECO:0000250,
CC ECO:0000269|PubMed:17999646, ECO:0000269|PubMed:19825634,
CC ECO:0000269|PubMed:22232549}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:22232549};
CC -!- SUBUNIT: Interacts with GB1. Component of a G-protein complex at least
CC composed of XLG2 and GB1. Interacts with RTV1.
CC {ECO:0000269|PubMed:19825634, ECO:0000269|PubMed:22232549}.
CC -!- INTERACTION:
CC C6KIE6; Q9XIB5: REM19; NbExp=4; IntAct=EBI-6868693, EBI-6869217;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17999646}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in vascular tissues,
CC root and shoot meristems and lateral root primordia.
CC {ECO:0000269|PubMed:17999646}.
CC -!- INDUCTION: By bacterial pathogen P.syringae.
CC {ECO:0000269|PubMed:19825634}.
CC -!- DOMAIN: The helical domain (492-627) is required for self-activation.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Enhanced susceptibility to
CC P.syringae. {ECO:0000269|PubMed:17999646, ECO:0000269|PubMed:19825634}.
CC -!- MISCELLANEOUS: Dark-grown xlg1-1 xlg2-1 xlg3-1 triple mutant plants
CC showed markedly increased primary root length compared with wild-type
CC plants. Dark-grown roots of the xlg triple mutants also showed altered
CC sensitivity to sugars, abscisic acid (ABA) hyposensitivity and ethylene
CC hypersensitivity, whereas seed germination in xlg triple mutants was
CC hypersensitive to osmotic stress and ABA (PubMed:17999646).
CC {ECO:0000305|PubMed:17999646}.
CC -!- SIMILARITY: Belongs to the G-alpha family. XLG subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36716.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80156.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GQ229389; ACT10804.1; -; mRNA.
DR EMBL; AL035521; CAB36716.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161585; CAB80156.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86367.1; -; Genomic_DNA.
DR PIR; T04785; T04785.
DR RefSeq; NP_195165.2; NM_119604.4.
DR AlphaFoldDB; C6KIE6; -.
DR SMR; C6KIE6; -.
DR BioGRID; 14871; 5.
DR IntAct; C6KIE6; 2.
DR STRING; 3702.AT4G34390.1; -.
DR iPTMnet; C6KIE6; -.
DR PaxDb; C6KIE6; -.
DR PRIDE; C6KIE6; -.
DR ProteomicsDB; 234371; -.
DR EnsemblPlants; AT4G34390.1; AT4G34390.1; AT4G34390.
DR GeneID; 829589; -.
DR Gramene; AT4G34390.1; AT4G34390.1; AT4G34390.
DR KEGG; ath:AT4G34390; -.
DR Araport; AT4G34390; -.
DR TAIR; locus:2116204; AT4G34390.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_006703_0_1_1; -.
DR InParanoid; C6KIE6; -.
DR OMA; CTNKMME; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; C6KIE6; -.
DR PRO; PR:C6KIE6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; C6KIE6; baseline and differential.
DR Genevisible; C6KIE6; AT.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW Calcium; GTP-binding; Metal-binding; Nucleotide-binding; Nucleus;
KW Plant defense; Reference proteome; Transducer; Zinc; Zinc-finger.
FT CHAIN 1..861
FT /note="Extra-large guanine nucleotide-binding protein 2"
FT /id="PRO_0000423398"
FT DOMAIN 461..853
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT ZN_FING 214..257
FT /note="RING-type; degenerate"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..477
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 523..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..632
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 665..674
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 737..744
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 818..823
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT MOTIF 204..211
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 17..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 469..477
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 624..632
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 632
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 741..744
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MUTAGEN 476
FT /note="T->A: Strongly reduces GTP-binding and GTPase
FT activity."
FT /evidence="ECO:0000269|PubMed:22232549"
SQ SEQUENCE 861 AA; 97183 MW; E1D9D723224166CF CRC64;
MAAVIRKLLP FPSPNPKRDN RESDDDDETS SGYRIEYSFA SEYKGPLIAN VPRALPVEVD
QIPTALPVSF SSLRSGISYP VAPLVMTKDT KRPPDSGIEK KNGFVDSAAG SSVVLIGRDV
VSGSSSSSSS KRLDVPEEVK SPADFRLSPS SPLSASAREE DHLDDDRVSD VGPRAVRFVE
PFQSSECDES SYVSDGESIA ATHRAERKGK RGSCYRCQLG NRFTEKEVCI VCDAKYCFNC
VRRAMGAMPE GRKCQACIGY RIDESKRASL GKCSRMLKRH LTDSELRQVM NAEITCKANQ
LPSRLIIVND KPLSEDELYT LQTCPNPPKK LKPGHYWYDK VAGYWGKIGE KPSQIISPNN
SIGGYISEKV SNGDTEIYIN GREITKPELT MLKWAGVQCE GKPHFWVDSD GSYREEGQKH
PIGNIWSKKR AKIACAVFSL PVPPASSAVE PYDVPLYEQK MLNKLLLIGS EKGGATTIYK
QARSLYNVSF SLEDRERIKF IIQTNLYTYL AMVLEAHERF EKEMSNDQSS GNVGDETSAK
PGNSINPRLK HFSDWVLKEK EDGNLKIFPP SSRENAQTVA DLWRVPAIQA TYKRLRDTLP
RNAVYFLERI LEISRSEYDP SDMDILQAEG LSSMEGLSCV DFSFPSTSQE ESLESDYQHD
TDMKYQLIRL NPRSLGENWK LLEMFEDADL VIFCVSLTDY AENIEDGEGN IVNKMLATKQ
LFENMVTHPS LANKRFLLVL TKFDLLEEKI EEVPLRTCEW FEDFNPLISQ NQTSRHNPPM
AQRAFHYIGY KFKRLYDSIL EPVNMRGRSF KPKLFVCQVS LESDTVDNAL RYAREILKWH
VEETSMFQEM STTSIEASSS S
