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Extra-large guanine nucleotide-binding protein 2 (Extra-large GTP-binding protein 2) (Extra-large G-protein 2)

 XLG2_ARATH              Reviewed;         861 AA.
C6KIE6; Q9SZ04;
18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
01-SEP-2009, sequence version 1.
25-APR-2018, entry version 73.
RecName: Full=Extra-large guanine nucleotide-binding protein 2;
AltName: Full=Extra-large GTP-binding protein 2;
Short=Extra-large G-protein 2;
Name=XLG2; OrderedLocusNames=At4g34390; ORFNames=F10M10.160;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
STRAIN=cv. Columbia;
PubMed=17999646; DOI=10.1111/j.1365-313X.2007.03335.x;
Ding L., Pandey S., Assmann S.M.;
"Arabidopsis extra-large G proteins (XLGs) regulate root
morphogenesis.";
Plant J. 53:248-263(2008).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
INDUCTION, DISRUPTION PHENOTYPE, FUNCTION, AND INTERACTION WITH GB1.
PubMed=19825634; DOI=10.1093/mp/ssp001;
Zhu H., Li G.J., Ding L., Cui X., Berg H., Assmann S.M., Xia Y.;
"Arabidopsis extra large G-protein 2 (XLG2) interacts with the Gbeta
subunit of heterotrimeric G protein and functions in disease
resistance.";
Mol. Plant 2:513-525(2009).
[5]
INTERACTION WITH RTV1, FUNCTION, COFACTOR, GTP-BINDING, AND
MUTAGENESIS OF THR-476.
PubMed=22232549; DOI=10.1074/jbc.M111.317412;
Heo J.B., Sung S., Assmann S.M.;
"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.";
J. Biol. Chem. 287:8242-8253(2012).
-!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
involved as modulators or transducers in various transmembrane
signaling systems (By similarity). Binds GTP with specificity.
Plays a role in the root morphogenesis by regulation of the cell
proliferation. Acts as a positive regulator in resistance to
pathogen that triggers the salicylic acid (SA) pathway. Promotes
the DNA binding activity of RTV1 specifically to promoter regions
of FT and SOC1 in vivo leading to the activation of floral
integrator genes. {ECO:0000250, ECO:0000269|PubMed:17999646,
ECO:0000269|PubMed:19825634, ECO:0000269|PubMed:22232549}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:22232549};
-!- SUBUNIT: Interacts with GB1. Component of a G-protein complex at
least composed of XLG2 and GB1. Interacts with RTV1.
{ECO:0000269|PubMed:19825634, ECO:0000269|PubMed:22232549}.
-!- INTERACTION:
Q9XIB5:REM19; NbExp=4; IntAct=EBI-6868693, EBI-6869217;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17999646}.
-!- TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in vascular
tissues, root and shoot meristems and lateral root primordia.
{ECO:0000269|PubMed:17999646}.
-!- INDUCTION: By bacterial pathogen P.syringae.
{ECO:0000269|PubMed:19825634}.
-!- DOMAIN: The helical domain (492-627) is required for self-
activation. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Enhanced
susceptibility to P.syringae. {ECO:0000269|PubMed:17999646,
ECO:0000269|PubMed:19825634}.
-!- MISCELLANEOUS: Dark-grown xlg1-1 xlg2-1 xlg3-1 triple mutant
plants showed markedly increased primary root length compared with
wild-type plants. Dark-grown roots of the xlg triple mutants also
showed altered sensitivity to sugars, abscisic acid (ABA)
hyposensitivity and ethylene hypersensitivity, whereas seed
germination in xlg triple mutants was hypersensitive to osmotic
stress and ABA (PubMed:17999646). {ECO:0000305|PubMed:17999646}.
-!- SIMILARITY: Belongs to the G-alpha family. XLG subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB36716.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB80156.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; GQ229389; ACT10804.1; -; mRNA.
EMBL; AL035521; CAB36716.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161585; CAB80156.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE86367.1; -; Genomic_DNA.
PIR; T04785; T04785.
RefSeq; NP_195165.2; NM_119604.4.
UniGene; At.27827; -.
ProteinModelPortal; C6KIE6; -.
SMR; C6KIE6; -.
BioGrid; 14871; 5.
IntAct; C6KIE6; 2.
STRING; 3702.AT4G34390.1; -.
iPTMnet; C6KIE6; -.
PaxDb; C6KIE6; -.
PRIDE; C6KIE6; -.
EnsemblPlants; AT4G34390.1; AT4G34390.1; AT4G34390.
GeneID; 829589; -.
Gramene; AT4G34390.1; AT4G34390.1; AT4G34390.
KEGG; ath:AT4G34390; -.
Araport; AT4G34390; -.
TAIR; locus:2116204; AT4G34390.
eggNOG; KOG0082; Eukaryota.
eggNOG; ENOG410XNVQ; LUCA.
HOGENOM; HOG000241648; -.
InParanoid; C6KIE6; -.
OMA; YTYLAMV; -.
OrthoDB; EOG093602Q0; -.
PhylomeDB; C6KIE6; -.
Reactome; R-ATH-112043; PLC beta mediated events.
Reactome; R-ATH-202040; G-protein activation.
Reactome; R-ATH-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
Reactome; R-ATH-399997; Acetylcholine regulates insulin secretion.
Reactome; R-ATH-416476; G alpha (q) signalling events.
Reactome; R-ATH-416482; G alpha (12/13) signalling events.
Reactome; R-ATH-418555; G alpha (s) signalling events.
Reactome; R-ATH-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
PRO; PR:C6KIE6; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; C6KIE6; baseline and differential.
Genevisible; C6KIE6; AT.
GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
GO; GO:0001664; F:G-protein coupled receptor binding; IBA:GO_Central.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004871; F:signal transducer activity; IBA:GO_Central.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
CDD; cd00066; G-alpha; 1.
Gene3D; 1.10.400.10; -; 1.
InterPro; IPR001019; Gprotein_alpha_su.
InterPro; IPR011025; GproteinA_insert.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR10218; PTHR10218; 1.
Pfam; PF00503; G-alpha; 1.
SMART; SM00275; G_alpha; 1.
SUPFAM; SSF47895; SSF47895; 1.
SUPFAM; SSF52540; SSF52540; 2.
1: Evidence at protein level;
Calcium; Complete proteome; GTP-binding; Metal-binding;
Nucleotide-binding; Nucleus; Plant defense; Reference proteome;
Transducer; Zinc; Zinc-finger.
CHAIN 1 861 Extra-large guanine nucleotide-binding
protein 2.
/FTId=PRO_0000423398.
ZN_FING 214 257 RING-type; degenerate.
NP_BIND 469 477 GTP. {ECO:0000250}.
NP_BIND 624 632 GTP. {ECO:0000250}.
NP_BIND 669 673 GTP; degenerate. {ECO:0000250}.
NP_BIND 741 744 GTP. {ECO:0000250}.
MOTIF 204 211 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 122 130 Poly-Ser.
METAL 476 476 Calcium. {ECO:0000255}.
METAL 632 632 Calcium. {ECO:0000255}.
MUTAGEN 476 476 T->A: Strongly reduces GTP-binding and
GTPase activity.
{ECO:0000269|PubMed:22232549}.
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


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