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Extra-large guanine nucleotide-binding protein 1 (Extra-large GTP-binding protein 1) (Extra-large G-protein 1)

 XLG1_ARATH              Reviewed;         888 AA.
O80462; O81224; O81225; Q93Y21;
18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 2.
20-JUN-2018, entry version 133.
RecName: Full=Extra-large guanine nucleotide-binding protein 1;
AltName: Full=Extra-large GTP-binding protein 1;
Short=Extra-large G-protein 1;
Name=XLG1; Synonyms=XLG; OrderedLocusNames=At2g23460;
ORFNames=F26B6.11;
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 [GENOMIC DNA / MRNA], GTP-BINDING, AND TISSUE
SPECIFICITY.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=10394945; DOI=10.1023/A:1026483823176;
Lee Y.R., Assmann S.M.;
"Arabidopsis thaliana 'extra-large GTP-binding protein' (AtXLG1): a
new class of G-protein.";
Plant Mol. Biol. 40:55-64(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
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).
[6]
COFACTOR, GTP-BINDING, AND MUTAGENESIS OF SER-497.
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. {ECO:0000250, ECO:0000269|PubMed:17999646}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:22232549};
-!- 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:10394945, ECO:0000269|PubMed:17999646}.
-!- DOMAIN: The helical domain (514-664) is required for self-
activation. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: No visible phenotype.
{ECO:0000269|PubMed:17999646}.
-!- 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=AAK96856.1; Type=Erroneous termination; Positions=780; Note=Translated as Glu.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF060941; AAC19352.1; -; mRNA.
EMBL; AF060942; AAC19353.1; -; Genomic_DNA.
EMBL; AC003040; AAC23761.2; -; Genomic_DNA.
EMBL; CP002685; AEC07458.1; -; Genomic_DNA.
EMBL; AY054665; AAK96856.1; ALT_TERM; mRNA.
PIR; T01135; T01135.
PIR; T51593; T51593.
RefSeq; NP_565553.1; NM_127910.3.
UniGene; At.48510; -.
UniGene; At.66350; -.
ProteinModelPortal; O80462; -.
SMR; O80462; -.
STRING; 3702.AT2G23460.1; -.
PaxDb; O80462; -.
PRIDE; O80462; -.
EnsemblPlants; AT2G23460.1; AT2G23460.1; AT2G23460.
GeneID; 816878; -.
Gramene; AT2G23460.1; AT2G23460.1; AT2G23460.
KEGG; ath:AT2G23460; -.
Araport; AT2G23460; -.
TAIR; locus:2046738; AT2G23460.
eggNOG; KOG0082; Eukaryota.
eggNOG; ENOG410XNVQ; LUCA.
HOGENOM; HOG000241648; -.
InParanoid; O80462; -.
OMA; KLCEANQ; -.
OrthoDB; EOG093602MX; -.
PhylomeDB; O80462; -.
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:O80462; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; O80462; baseline and differential.
Genevisible; O80462; 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:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:GO_Central.
CDD; cd00066; G-alpha; 1.
Gene3D; 1.10.400.10; -; 3.
InterPro; IPR001019; Gprotein_alpha_su.
InterPro; IPR011025; GproteinA_insert.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR10218; PTHR10218; 1.
Pfam; PF00503; G-alpha; 1.
PRINTS; PR00318; GPROTEINA.
SMART; SM00275; G_alpha; 1.
SUPFAM; SSF47895; SSF47895; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
1: Evidence at protein level;
Calcium; Complete proteome; GTP-binding; Metal-binding;
Nucleotide-binding; Nucleus; Reference proteome; TonB box; Transducer;
Zinc; Zinc-finger.
CHAIN 1 888 Extra-large guanine nucleotide-binding
protein 1.
/FTId=PRO_0000423397.
ZN_FING 225 268 RING-type; degenerate.
NP_BIND 490 498 GTP. {ECO:0000250}.
NP_BIND 661 669 GTP. {ECO:0000250}.
NP_BIND 706 710 GTP; degenerate. {ECO:0000250}.
NP_BIND 774 777 GTP. {ECO:0000250}.
MOTIF 90 97 TonB box.
MOTIF 205 222 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 104 110 Poly-Glu.
COMPBIAS 196 199 Poly-Glu.
METAL 497 497 Calcium. {ECO:0000255}.
METAL 669 669 Calcium. {ECO:0000255}.
MUTAGEN 497 497 S->N: Strongly reduces GTP-binding and
GTPase activity.
{ECO:0000269|PubMed:22232549}.
CONFLICT 45 45 C -> R (in Ref. 1; AAC19353).
{ECO:0000305}.
CONFLICT 204 204 L -> Q (in Ref. 1; AAC19353).
{ECO:0000305}.
CONFLICT 249 249 N -> S (in Ref. 1; AAC19353).
{ECO:0000305}.
CONFLICT 336 336 S -> P (in Ref. 1; AAC19353).
{ECO:0000305}.
CONFLICT 641 641 S -> N (in Ref. 1; AAC19353).
{ECO:0000305}.
CONFLICT 660 660 L -> V (in Ref. 1; AAC19353).
{ECO:0000305}.
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


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