XLG3_ARATH
ID XLG3_ARATH Reviewed; 848 AA.
AC Q9C516;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Extra-large guanine nucleotide-binding protein 3;
DE AltName: Full=Extra-large GTP-binding protein 3;
DE Short=Extra-large G-protein 3;
GN Name=XLG3; OrderedLocusNames=At1g31930; ORFNames=F5M6.7, T12O21.16;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18397373; DOI=10.1111/j.1365-313x.2008.03506.x;
RA Pandey S., Monshausen G.B., Ding L., Assmann S.M.;
RT "Regulation of root-wave response by extra large and conventional G
RT proteins in Arabidopsis thaliana.";
RL Plant J. 55:311-322(2008).
RN [7]
RP INDUCTION.
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 [8]
RP COFACTOR, GTP-BINDING, AND MUTAGENESIS OF SER-444.
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 with GB1 in
CC the positive regulation of root waving and root skewing. {ECO:0000250,
CC ECO:0000269|PubMed:17999646, ECO:0000269|PubMed:18397373}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:22232549};
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 (460-611) is required for self-activation.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Severely compromised root
CC waving and abnormal root skewing response. Hypersensitivity to ethylene
CC (ACC). {ECO:0000269|PubMed:17999646, ECO:0000269|PubMed:18397373}.
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}.
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DR EMBL; GQ229390; ACT10805.1; -; mRNA.
DR EMBL; AC074309; AAG50792.1; -; Genomic_DNA.
DR EMBL; AC079041; AAG50710.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31417.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31418.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31419.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58207.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58208.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58209.1; -; Genomic_DNA.
DR EMBL; AK229561; BAF01414.1; -; mRNA.
DR EMBL; AK317243; BAH19924.1; -; mRNA.
DR EMBL; AK317663; BAH20323.1; -; mRNA.
DR PIR; E86443; E86443.
DR RefSeq; NP_001185125.1; NM_001198196.1.
DR RefSeq; NP_001319126.1; NM_001332988.1.
DR RefSeq; NP_001320661.1; NM_001332989.1.
DR RefSeq; NP_001320662.1; NM_001332990.1.
DR RefSeq; NP_174475.1; NM_102929.2.
DR RefSeq; NP_849737.1; NM_179406.2.
DR AlphaFoldDB; Q9C516; -.
DR SMR; Q9C516; -.
DR IntAct; Q9C516; 1.
DR STRING; 3702.AT1G31930.1; -.
DR iPTMnet; Q9C516; -.
DR PaxDb; Q9C516; -.
DR PRIDE; Q9C516; -.
DR ProteomicsDB; 234420; -.
DR EnsemblPlants; AT1G31930.1; AT1G31930.1; AT1G31930.
DR EnsemblPlants; AT1G31930.2; AT1G31930.2; AT1G31930.
DR EnsemblPlants; AT1G31930.3; AT1G31930.3; AT1G31930.
DR EnsemblPlants; AT1G31930.4; AT1G31930.4; AT1G31930.
DR EnsemblPlants; AT1G31930.5; AT1G31930.5; AT1G31930.
DR EnsemblPlants; AT1G31930.6; AT1G31930.6; AT1G31930.
DR GeneID; 840083; -.
DR Gramene; AT1G31930.1; AT1G31930.1; AT1G31930.
DR Gramene; AT1G31930.2; AT1G31930.2; AT1G31930.
DR Gramene; AT1G31930.3; AT1G31930.3; AT1G31930.
DR Gramene; AT1G31930.4; AT1G31930.4; AT1G31930.
DR Gramene; AT1G31930.5; AT1G31930.5; AT1G31930.
DR Gramene; AT1G31930.6; AT1G31930.6; AT1G31930.
DR KEGG; ath:AT1G31930; -.
DR Araport; AT1G31930; -.
DR TAIR; locus:2034446; AT1G31930.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_006703_0_0_1; -.
DR InParanoid; Q9C516; -.
DR OMA; KWMEMFE; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; Q9C516; -.
DR PRO; PR:Q9C516; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C516; baseline and differential.
DR Genevisible; Q9C516; 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:2000280; P:regulation of root development; IGI:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IMP:TAIR.
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 PRINTS; PR00318; GPROTEINA.
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 Reference proteome; Transducer; Zinc; Zinc-finger.
FT CHAIN 1..848
FT /note="Extra-large guanine nucleotide-binding protein 3"
FT /id="PRO_0000423399"
FT DOMAIN 429..826
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT ZN_FING 176..218
FT /note="RING-type; degenerate"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..445
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 499..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..616
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 652..661
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 728..735
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 796..801
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 824..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 156..173
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 72..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 437..445
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 608..616
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 616
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 732..735
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MUTAGEN 444
FT /note="S->N: Strongly reduces GTP-binding and GTPase
FT activity."
FT /evidence="ECO:0000269|PubMed:22232549"
SQ SEQUENCE 848 AA; 96171 MW; A275FF1061405F8A CRC64;
MEKKDEGESW KEMVRKMLPP GAPLPEDPSE FDYSIALEYT GPPPVHDIPR VSPVDVNPRV
NNPIPLPVSR IAGGVTSSSG GSPASSESVV SVLHNNPESS SGSASVSPVS GHRQNGNQVR
RPVVKFKPVD DHDRIEGREA AEEEDNNVEA ETERERKVHE CTASTKRRKK KKKSECYRCG
KAKWENKETC IVCDEKYCGN CVLRAMGSMP EGRKCVSCIG QAIDESKRSK LGKHSRVLSR
LLSPLEVKQI MKAEKECTAN QLRPEQLIVN GYPLKPEEMA DLLNCLLPPQ KLKPGRYWYD
KESGLWGKEG EKPDRVISSN LNFTGKLSPD ASNGNTEVYI NGREITKLEL RILKLANVQC
PRDTHFWVYD DGRYEEEGQN NIRGNIWEKA STRFMCALFS LPVPQGQPRG TVQPSSNYAT
VPNYIEHKKI QKLLLLGIEG SGTSTIFKQA KFLYGNKFSV EELQDIKLMV QSNMYRYLSI
LLDGRERFEE EALSHTRGLN AVEGDSGGEE ANDEGTVTTP QSVYTLNPRL KHFSDWLLDI
IATGDLDAFF PAATREYAPL VEEVWKDPAI QATYRRKDEL HFLPDVAEYF LSRAMEVSSN
EYEPSERDIV YAEGVTQGNG LAFMEFSLSD HSPMSESYPE NPDALSSPQP KYQLIRVNAK
GMNDSCKWVE MFEDVRAVIF CISLSDYDQI NITPESSGTV QYQNKMIQSK ELFESMVKHP
CFKDTPFILI LNKYDQFEEK LNRAPLTSCD WFSDFCPVRT NNNVQSLAYQ AYFYVAMKFK
LLYFSITGQK LFVWQARARD RANVDEGFKY VREVLKWDEE KEESYLNGGG EDSFYSTDMS
SSPYRPEE
