XLG1_ARATH
ID XLG1_ARATH Reviewed; 888 AA.
AC O80462; O81224; O81225; Q93Y21;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Extra-large guanine nucleotide-binding protein 1;
DE AltName: Full=Extra-large GTP-binding protein 1;
DE Short=Extra-large G-protein 1;
GN Name=XLG1; Synonyms=XLG; OrderedLocusNames=At2g23460; ORFNames=F26B6.11;
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], GTP-BINDING, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=10394945; DOI=10.1023/a:1026483823176;
RA Lee Y.R., Assmann S.M.;
RT "Arabidopsis thaliana 'extra-large GTP-binding protein' (AtXLG1): a new
RT class of G-protein.";
RL Plant Mol. Biol. 40:55-64(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, NOMENCLATURE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP 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 [6]
RP COFACTOR, GTP-BINDING, AND MUTAGENESIS OF SER-497.
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. {ECO:0000250,
CC ECO:0000269|PubMed:17999646}.
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:10394945, ECO:0000269|PubMed:17999646}.
CC -!- DOMAIN: The helical domain (514-664) is required for self-activation.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17999646}.
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=AAK96856.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF060941; AAC19352.1; -; mRNA.
DR EMBL; AF060942; AAC19353.1; -; Genomic_DNA.
DR EMBL; AC003040; AAC23761.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07458.1; -; Genomic_DNA.
DR EMBL; AY054665; AAK96856.1; ALT_TERM; mRNA.
DR PIR; T01135; T01135.
DR PIR; T51593; T51593.
DR RefSeq; NP_565553.1; NM_127910.3.
DR AlphaFoldDB; O80462; -.
DR SMR; O80462; -.
DR STRING; 3702.AT2G23460.1; -.
DR PaxDb; O80462; -.
DR PRIDE; O80462; -.
DR ProteomicsDB; 234295; -.
DR EnsemblPlants; AT2G23460.1; AT2G23460.1; AT2G23460.
DR GeneID; 816878; -.
DR Gramene; AT2G23460.1; AT2G23460.1; AT2G23460.
DR KEGG; ath:AT2G23460; -.
DR Araport; AT2G23460; -.
DR TAIR; locus:2046738; AT2G23460.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_006703_0_1_1; -.
DR InParanoid; O80462; -.
DR OMA; WASNESI; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; O80462; -.
DR PRO; PR:O80462; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80462; baseline and differential.
DR Genevisible; O80462; 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 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.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
PE 1: Evidence at protein level;
KW Calcium; GTP-binding; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; TonB box; Transducer; Zinc; Zinc-finger.
FT CHAIN 1..888
FT /note="Extra-large guanine nucleotide-binding protein 1"
FT /id="PRO_0000423397"
FT DOMAIN 482..879
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT ZN_FING 225..268
FT /note="RING-type; degenerate"
FT REGION 98..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..498
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 661..669
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 702..711
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 770..777
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 843..848
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT MOTIF 90..97
FT /note="TonB box"
FT MOTIF 205..222
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 102..117
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 490..498
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 497
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 661..669
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 669
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 774..777
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MUTAGEN 497
FT /note="S->N: Strongly reduces GTP-binding and GTPase
FT activity."
FT /evidence="ECO:0000269|PubMed:22232549"
FT CONFLICT 45
FT /note="C -> R (in Ref. 1; AAC19353)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="L -> Q (in Ref. 1; AAC19353)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="N -> S (in Ref. 1; AAC19353)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="S -> P (in Ref. 1; AAC19353)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="S -> N (in Ref. 1; AAC19353)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="L -> V (in Ref. 1; AAC19353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 888 AA; 98796 MW; 61F57223CE663648 CRC64;
MPLKEDDCCL FAEEYDGPPL SYNIPCAVPI NVEKIPVAAV VSPVCISDNM SFPVIQPILS
VESKKFLIDS VSPTSVIANC GSNQLELVSD SITVSPTSVI EHTEEEEEEE GGDGEDCELS
SSGELLLRSC SVKESLDLNE SSSNPLVPDW ESNESVLSMD YPSSRVTGDC VSETNGDGKK
QPVVTFLGIA SDDGFEEEES CSNLRRVRVV PVKKQPQTKG KKGSCYRCFK GSRFTEKEVC
LVCDAKYCNS CVLRAMGSMP EGRKCVTCIG FPIDESKRGS LGKCSRMLKR LLNDLEVKQI
MKTERFCEAN QLPAEYVYVN GQPLYPEELV TLQTCSNPPK KLKPGDYWYD KVSGLWGKEG
EKPYQIISPH LNVGGPISPE ASNGNTQVFI NGREITKVEL RMLQLAGVQC AGNPHFWVNE
DGSYQEEGQK NTKGYIWGKA GTKLLCAVLS LPVPSKSTAN ASGEQLYSAN SRSILDHLEH
RTLQKILLVG NSGSGTSTIF KQAKILYKDV PFLEDERENI KVIIQTNVYG YLGMLLEGRE
RFEEEALALR NTKQCVLENI PADEGDAKSN DKTVTMYSIG PRLKAFSDWL LKTMAAGNLG
VIFPAASREY APLVEELWRD AAIQATYKRR SELGLLPSVA SYFLERAIDV LTPDYEPSDL
DILYAEGVTS SSGLACLDFS FPQTASEENL DPSDHHDSLL RYQLIRVPSR GLGENCKWID
MFEDVGMVVF VVSMSDYDQV SEDGTNKMLL TKKLFESIIT HPIFENMDFL LILNKYDLLE
EKVERVPLAR CEWFQDFNPV VSRHRGSNNG NPTLGQLAFH FMAVKFKRFY SSLTGKKLFV
SSSKSLDPNS VDSSLKLAME ILKWSEERTN ICMSEYSMYS TEPSSFSN
