DRG3_ARATH
ID DRG3_ARATH Reviewed; 369 AA.
AC Q9SVA6;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Developmentally-regulated G-protein 3;
DE Short=AtDRG3;
DE AltName: Full=Developmentally-regulated G-protein 1;
DE Short=AtDRG1;
GN Name=DRG3; Synonyms=DRG1; OrderedLocusNames=At4g39520; ORFNames=F23K16.150;
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=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 [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;
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 [4]
RP INTERACTION WITH PHOSPHATIDIC ACID, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15272872; DOI=10.1111/j.1365-313x.2004.02152.x;
RA Testerink C., Dekker H.L., Lim Z.-Y., Johns M.K., Holmes A.B.,
RA De Koster C.G., Ktistakis N.T., Munnik T.;
RT "Isolation and identification of phosphatidic acid targets from plants.";
RL Plant J. 39:527-536(2004).
RN [5]
RP FUNCTION.
RX PubMed=19460440; DOI=10.1016/j.pep.2009.05.009;
RA O'Connell A., Robin G., Kobe B., Botella J.R.;
RT "Biochemical characterization of Arabidopsis developmentally regulated G-
RT proteins (DRGs).";
RL Protein Expr. Purif. 67:88-95(2009).
CC -!- FUNCTION: Binds GDP and GTP, and has low GTPase activity in vitro.
CC {ECO:0000269|PubMed:19460440}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000255|PROSITE-ProRule:PRU01047}.
CC -!- CAUTION: The nomenclature of the 3 Arabidopsis DRG genes is ambiguous;
CC in the literature several gene names have been used for the same
CC protein. {ECO:0000305}.
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DR EMBL; AL078620; CAB44687.1; -; Genomic_DNA.
DR EMBL; AL161595; CAB80615.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87081.1; -; Genomic_DNA.
DR EMBL; AY035034; AAK59539.1; -; mRNA.
DR PIR; T09368; T09368.
DR RefSeq; NP_195662.1; NM_120112.4.
DR AlphaFoldDB; Q9SVA6; -.
DR SMR; Q9SVA6; -.
DR BioGRID; 15386; 10.
DR STRING; 3702.AT4G39520.1; -.
DR PaxDb; Q9SVA6; -.
DR PRIDE; Q9SVA6; -.
DR ProteomicsDB; 224303; -.
DR EnsemblPlants; AT4G39520.1; AT4G39520.1; AT4G39520.
DR GeneID; 830106; -.
DR Gramene; AT4G39520.1; AT4G39520.1; AT4G39520.
DR KEGG; ath:AT4G39520; -.
DR Araport; AT4G39520; -.
DR TAIR; locus:2122536; AT4G39520.
DR eggNOG; KOG1487; Eukaryota.
DR HOGENOM; CLU_044997_0_0_1; -.
DR InParanoid; Q9SVA6; -.
DR OMA; SAKHPGQ; -.
DR OrthoDB; 754662at2759; -.
DR PhylomeDB; Q9SVA6; -.
DR PRO; PR:Q9SVA6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SVA6; baseline and differential.
DR Genevisible; Q9SVA6; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IDA:TAIR.
DR GO; GO:0003924; F:GTPase activity; IDA:TAIR.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR CDD; cd01896; DRG; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR045001; DRG.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR031662; GTP-binding_2.
DR InterPro; IPR006074; GTP1-OBG_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR PANTHER; PTHR43127; PTHR43127; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF16897; MMR_HSR1_Xtn; 1.
DR Pfam; PF02824; TGS; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS00905; GTP1_OBG; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..369
FT /note="Developmentally-regulated G-protein 3"
FT /id="PRO_0000424833"
FT DOMAIN 66..291
FT /note="OBG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT DOMAIN 291..367
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT BINDING 72..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 118..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 249..252
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
SQ SEQUENCE 369 AA; 41144 MW; 7235DC68F06DADFB CRC64;
MSTIMQKIKE IEDEMAKTQK NKATSHHLGL LKAKLAKLRR DLLAPPTKGG GGGAGEGFDV
TKSGDSRVGL VGFPSVGKST LLNKLTGTFS EVASYEFTTL TCIPGVITYR GAKIQLLDLP
GIIEGAKDGK GRGRQVISTA RTCNCILIVL DAIKPITHKR LIEKELEGFG IRLNKEPPNL
TFRKKDKGGI NLTSTVAVTH LDLDTVKAIC GEYRMHNADI TLRYDATADD LIDVIEGSRI
YMPCIYAVNK IDSITLEELE ILDKLPHYCP VSAHLEWNLD GLLDKIWEYL DLTRIYTKPK
AMNPDYDDPV ILSSKKRTVE DFCIRIHKDM LKQFKYALVW GSSAKHKPQR VGKEHELEDE
DVVQIVKKI
