GG3_ARATH
ID GG3_ARATH Reviewed; 251 AA.
AC Q6AWT8;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Guanine nucleotide-binding protein subunit gamma 3;
DE AltName: Full=Ggamma-subunit 3;
DE AltName: Full=Heterotrimeric G protein gamma-subunit 3;
DE Short=AtAGG3;
DE Flags: Precursor;
GN Name=GG3; Synonyms=AGG3; OrderedLocusNames=At5g20635; ORFNames=T1M15;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=22209167; DOI=10.1016/j.jplph.2011.11.010;
RA Thung L., Trusov Y., Chakravorty D., Botella J.R.;
RT "Ggamma1+Ggamma2+Ggamma3=Gbeta: the search for heterotrimeric G-protein
RT gamma subunits in Arabidopsis is over.";
RL J. Plant Physiol. 169:542-545(2012).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as a modulator or transducer in various transmembrane signaling
CC systems. The beta and gamma chains are required for the GTPase
CC activity, for replacement of GDP by GTP, and for G protein-effector
CC interaction. {ECO:0000269|PubMed:22209167}.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and siliques.
CC {ECO:0000269|PubMed:22209167}.
CC -!- DISRUPTION PHENOTYPE: Leaves with a roundish shape as well as rounder
CC and smaller flowers. {ECO:0000269|PubMed:22209167}.
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DR EMBL; AF296832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92869.1; -; Genomic_DNA.
DR EMBL; BT015160; AAT85756.1; -; mRNA.
DR EMBL; AK221695; BAD95404.1; -; mRNA.
DR RefSeq; NP_680175.2; NM_147870.4.
DR AlphaFoldDB; Q6AWT8; -.
DR BioGRID; 17461; 1.
DR STRING; 3702.AT5G20635.1; -.
DR iPTMnet; Q6AWT8; -.
DR PaxDb; Q6AWT8; -.
DR PRIDE; Q6AWT8; -.
DR ProteomicsDB; 224778; -.
DR EnsemblPlants; AT5G20635.1; AT5G20635.1; AT5G20635.
DR GeneID; 832186; -.
DR Gramene; AT5G20635.1; AT5G20635.1; AT5G20635.
DR KEGG; ath:AT5G20635; -.
DR Araport; AT5G20635; -.
DR TAIR; locus:504954807; AT5G20635.
DR eggNOG; ENOG502RZC5; Eukaryota.
DR HOGENOM; CLU_1117029_0_0_1; -.
DR InParanoid; Q6AWT8; -.
DR OrthoDB; 1546086at2759; -.
DR PRO; PR:Q6AWT8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6AWT8; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Lipoprotein; Methylation; Prenylation; Reference proteome; Transducer.
FT CHAIN 1..248
FT /note="Guanine nucleotide-binding protein subunit gamma 3"
FT /id="PRO_0000419817"
FT PROPEP 249..251
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000419818"
FT DOMAIN 46..126
FT /note="G protein gamma"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 248
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 251 AA; 27157 MW; AADF2FFF10EB98AF CRC64;
MSAPSGGGEG GGKESAAGGV SSSSLAPSSL PPPRPKSPPE YPDLYGKRRE AARVQMLERE
IGFLEGEIKF IEGVQPASRC IKEVSDFVVA NSDPLIPAQR KSRRSFRFWK WLCGPCLSLV
SFCCCCQSKC SCHLRKPKCC NCTSCSCIGS KCCDGSCCSN ICCCPRLSCP SCSCFRGCWC
SCPDMSCCIP SCFRSCSCTR PSCLNKKKSS CCSCNCKIRW SSCFSCPKVR LCSCCFCNCK
NLCSNPCCLA F