GTG2_ARATH
ID GTG2_ARATH Reviewed; 467 AA.
AC Q0WQG8; G0WVT7; Q304A2; Q3E9V6; Q9T087;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=GPCR-type G protein 2;
GN Name=GTG2; OrderedLocusNames=At4g27630; ORFNames=T29A15.120;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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] (ISOFORM 1).
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 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 Q0WQG8; P18064: GPA1; NbExp=2; IntAct=EBI-2214623, EBI-443890;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19135895};
CC Multi-pass membrane protein {ECO:0000269|PubMed:19135895}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:23001037}; Multi-pass membrane
CC protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23001037}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0WQG8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0WQG8-2; Sequence=VSP_036623, VSP_036624;
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 GTG1. 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB38275.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81413.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HM776217; AEF15912.1; -; mRNA.
DR EMBL; AL035602; CAB38275.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161571; CAB81413.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85370.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85371.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67757.1; -; Genomic_DNA.
DR EMBL; AK228729; BAF00631.1; -; mRNA.
DR PIR; T05868; T05868.
DR RefSeq; NP_001320077.1; NM_001341872.1. [Q0WQG8-2]
DR RefSeq; NP_194493.2; NM_118899.4. [Q0WQG8-1]
DR RefSeq; NP_849555.1; NM_179224.2. [Q0WQG8-2]
DR AlphaFoldDB; Q0WQG8; -.
DR SMR; Q0WQG8; -.
DR BioGRID; 14161; 1.
DR IntAct; Q0WQG8; 1.
DR STRING; 3702.AT4G27630.3; -.
DR PaxDb; Q0WQG8; -.
DR PRIDE; Q0WQG8; -.
DR ProteomicsDB; 247236; -. [Q0WQG8-1]
DR EnsemblPlants; AT4G27630.1; AT4G27630.1; AT4G27630. [Q0WQG8-2]
DR EnsemblPlants; AT4G27630.2; AT4G27630.2; AT4G27630. [Q0WQG8-1]
DR EnsemblPlants; AT4G27630.6; AT4G27630.6; AT4G27630. [Q0WQG8-2]
DR GeneID; 828874; -.
DR Gramene; AT4G27630.1; AT4G27630.1; AT4G27630. [Q0WQG8-2]
DR Gramene; AT4G27630.2; AT4G27630.2; AT4G27630. [Q0WQG8-1]
DR Gramene; AT4G27630.6; AT4G27630.6; AT4G27630. [Q0WQG8-2]
DR KEGG; ath:AT4G27630; -.
DR Araport; AT4G27630; -.
DR eggNOG; KOG2417; Eukaryota.
DR HOGENOM; CLU_030540_1_0_1; -.
DR InParanoid; Q0WQG8; -.
DR OMA; HFNFYHR; -.
DR PhylomeDB; Q0WQG8; -.
DR PRO; PR:Q0WQG8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q0WQG8; baseline and differential.
DR Genevisible; Q0WQG8; 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010427; F:abscisic acid binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IBA:GO_Central.
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 Alternative splicing; Cell membrane; Coiled coil; Endoplasmic reticulum;
KW Golgi apparatus; GTP-binding; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..467
FT /note="GPCR-type G protein 2"
FT /id="PRO_0000367059"
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 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT COILED 243..276
FT /evidence="ECO:0000255"
FT BINDING 381..410
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..119
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036623"
FT VAR_SEQ 120..139
FT /note="LTAFLYAFWRMGIHFPMPSD -> MLKILSPTCWTTLLKHPFIL (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036624"
FT CONFLICT 72
FT /note="E -> G (in Ref. 4; BAF00631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 53514 MW; DC2F48C3EA82D05E CRC64;
MGYGWGIFEG MLVIGSLCLL GSAGLWFLNR RLYKEYEEKR ALVQIIFSVV FAFSCNLLQL
VLFEIIPVLS REARMVNWKV DLFCLIVLLV FMLPYYHCYL MLRNTGVRRE RAAVGALLFL
TAFLYAFWRM GIHFPMPSDK GFFSMPQLVS RIGVIGVTLM AVLSGFGAVN LPYSYISLFI
REIEESEIKS LERQLMQSME TCIAKKKKIL LCQVEVERSL VSEEHQKGKS FFRRFVGTVV
RSVQDDQKEQ DIKLMEAEVE GLEELSKQLF LEIYELRQAK DAAAFSRTWK GHVQNFLGYA
CSIYCVYKML KSLQSVVFKE AGTKDPVTMM ISIFLQFFDI GVDAALLSQY ISLLFIGMLI
VISVRGFLTN LMKFFFAVSR VGSGSSSNVV LFLSEIMGMY FLSSILLIRK SLRNEYRGII
TDVLGGDIQF DFYHRWFDAI FVASAFLSLL LLSAHYTSRQ IDKHPID
