GTG1_ARATH
ID GTG1_ARATH Reviewed; 468 AA.
AC Q9XIP7; G0WVT6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=GPCR-type G protein 1;
GN Name=GTG1; OrderedLocusNames=At1g64990; ORFNames=F13O11.29;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23001037; DOI=10.1105/tpc.112.098681;
RA Jaffe F.W., Freschet G.E., Valdes B.M., Runions J., Terry M.J.,
RA Williams L.E.;
RT "G protein-coupled receptor-type G proteins are required for light-
RT dependent seedling growth and fertility in Arabidopsis.";
RL Plant Cell 24:3649-3668(2012).
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;
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 FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION, INTERACTION
RP WITH GPA1, AND DISRUPTION PHENOTYPE.
RX PubMed=19135895; DOI=10.1016/j.cell.2008.12.026;
RA Pandey S., Nelson D.C., Assmann S.M.;
RT "Two novel GPCR-type G proteins are abscisic acid receptors in
RT Arabidopsis.";
RL Cell 136:136-148(2009).
CC -!- FUNCTION: Abscisic acid receptor. The GDP-bound form exhibits greater
CC abscisic acid binding than the GTP-bound form (PubMed:19135895).
CC Required for seedling growth and fertility (PubMed:23001037).
CC {ECO:0000269|PubMed:19135895, ECO:0000269|PubMed:23001037}.
CC -!- ACTIVITY REGULATION: The GTPase activity is Mg(2+) dependent and is
CC strongly inhibited by the interaction with GPA1.
CC -!- SUBUNIT: Interacts with GPA1. {ECO:0000269|PubMed:19135895}.
CC -!- INTERACTION:
CC Q9XIP7; P18064: GPA1; NbExp=2; IntAct=EBI-2214605, EBI-443890;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19135895};
CC Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:23001037}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23001037}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, leaves, stems, roots,
CC flowers and guard cells. {ECO:0000269|PubMed:19135895}.
CC -!- INDUCTION: Not induced by abscisic acid, cold, salt or drought
CC treatments. {ECO:0000269|PubMed:19135895}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC GTG2. The double mutants gtg1 and gtg2 are hyposensitive to abscisic
CC acid. {ECO:0000269|PubMed:19135895}.
CC -!- MISCELLANEOUS: Has both a topology similar to GPCRs and a GTP-
CC binding/GTPase activity.
CC -!- SIMILARITY: Belongs to the Golgi pH regulator (TC 1.A.38) family.
CC {ECO:0000305}.
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DR EMBL; HM776216; AEF15911.1; -; mRNA.
DR EMBL; AC006193; AAD38272.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34312.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34313.1; -; Genomic_DNA.
DR EMBL; AY070446; AAL49849.1; -; mRNA.
DR PIR; E96673; E96673.
DR RefSeq; NP_001031235.1; NM_001036158.2.
DR RefSeq; NP_176679.2; NM_105173.4.
DR AlphaFoldDB; Q9XIP7; -.
DR SMR; Q9XIP7; -.
DR BioGRID; 28028; 1.
DR IntAct; Q9XIP7; 1.
DR STRING; 3702.AT1G64990.2; -.
DR PaxDb; Q9XIP7; -.
DR PRIDE; Q9XIP7; -.
DR ProteomicsDB; 247346; -.
DR EnsemblPlants; AT1G64990.1; AT1G64990.1; AT1G64990.
DR EnsemblPlants; AT1G64990.2; AT1G64990.2; AT1G64990.
DR GeneID; 842807; -.
DR Gramene; AT1G64990.1; AT1G64990.1; AT1G64990.
DR Gramene; AT1G64990.2; AT1G64990.2; AT1G64990.
DR KEGG; ath:AT1G64990; -.
DR Araport; AT1G64990; -.
DR TAIR; locus:2010796; AT1G64990.
DR eggNOG; KOG2417; Eukaryota.
DR HOGENOM; CLU_030540_1_0_1; -.
DR InParanoid; Q9XIP7; -.
DR OMA; IEIGVHW; -.
DR OrthoDB; 1065554at2759; -.
DR PhylomeDB; Q9XIP7; -.
DR PRO; PR:Q9XIP7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XIP7; baseline and differential.
DR Genevisible; Q9XIP7; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; TAS:TAIR.
DR GO; GO:0010427; F:abscisic acid binding; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IDA:TAIR.
DR GO; GO:0051020; F:GTPase binding; IPI:TAIR.
DR GO; GO:0009791; P:post-embryonic development; IGI:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IGI:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IGI:TAIR.
DR InterPro; IPR025969; ABA_GPCR_dom.
DR InterPro; IPR022535; Golgi_pH-regulator_cons_dom.
DR InterPro; IPR015672; GPHR/GTG.
DR PANTHER; PTHR15948; PTHR15948; 1.
DR Pfam; PF12430; ABA_GPCR; 1.
DR Pfam; PF12537; GPHR_N; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Endoplasmic reticulum; Golgi apparatus;
KW GTP-binding; Membrane; Nucleotide-binding; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..468
FT /note="GPCR-type G protein 1"
FT /id="PRO_0000367058"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT COILED 243..279
FT /evidence="ECO:0000255"
FT BINDING 382..411
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 53546 MW; B267D260A6E4BF8B CRC64;
MSYGWAIYEG TVVIASLSLL GWAGLWFLNR RLYKEYEEKR ALVQIIFSVV FAFSCNLLQL
VLFEIIPVLS REARMINWKV DLFCLILLLV FMLPYYHCYL MLRNSGVRRE RASVGAFLFL
SAFLYAFWRM GVHFPMPSAD KGFFTMPQLV SRIGVIGVTL MAVLSGFGAV NLPYSYISLF
IREIEEADII SLERQLIQST ETCIAKKKKI ILCQLEVERN QGSEENQKRS SFFRRIVGTV
VRSVQDDQKE QDIKILEAEV EALEELSKQL FLEVYELRQA KDAAAYSRTW KGHVQNLLGY
ACSIYCVYKM LKSLQSVVFK EAGTKDPVTT MISIFLRLFD IGVDAALLSQ YISLLFIGML
IVISVRGFLT NLMKFFFAVS RVGSGSSSNV VLFLSEIMGM YFLSSILLIR KSLRNEYRGI
ITDVLGGDIQ FDFYHRWFDA IFVASAFLSL VLLSAHYTSR QSDKHAIE
