DRG1_ARATH
ID DRG1_ARATH Reviewed; 399 AA.
AC Q9LQK0; O04174; Q94K69; Q9LNQ8;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Developmentally-regulated G-protein 1;
DE Short=AtDRG1;
DE AltName: Full=Developmentally-regulated G-protein 2A;
DE Short=AtDRG2a;
GN Name=DRG1; Synonyms=DRG2A; OrderedLocusNames=At1g17470;
GN ORFNames=F1L3.17, F28G4.4;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10080710; DOI=10.1023/a:1006178710443;
RA Devitt M.L., Maas K.J., Stafstrom J.P.;
RT "Characterization of DRGs, developmentally regulated GTP-binding proteins,
RT from pea and Arabidopsis.";
RL Plant Mol. Biol. 39:75-82(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=10380799; DOI=10.1023/a:1006137221259;
RA Etheridge N., Trusov Y., Verbelen J.P., Botella J.R.;
RT "Characterization of ATDRG1, a member of a new class of GTP-binding
RT proteins in plants.";
RL Plant Mol. Biol. 39:1113-1126(1999).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH PHOSPHATIDIC ACID, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=cv. Columbia;
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 [8]
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. May interact
CC with phosphatidic acid (PA). {ECO:0000269|PubMed:19460440}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:10380799}. Cytoplasm {ECO:0000269|PubMed:10380799}.
CC -!- TISSUE SPECIFICITY: Expressed in actively growing tissues and
CC reproductive organs. Mostly expressed in leaves, stems and siliques.
CC Also present in flowers and flower buds, and, to a lower extent, in
CC roots. {ECO:0000269|PubMed:10080710, ECO:0000269|PubMed:10380799}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79465.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF014822; AAB67830.1; -; mRNA.
DR EMBL; U66408; AAB53256.1; -; mRNA.
DR EMBL; AC007843; AAF97313.1; -; Genomic_DNA.
DR EMBL; AC022492; AAF79465.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29595.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29596.1; -; Genomic_DNA.
DR EMBL; AF370258; AAK44073.1; -; mRNA.
DR EMBL; BT021092; AAX12862.1; -; mRNA.
DR RefSeq; NP_001077555.1; NM_001084086.1.
DR RefSeq; NP_173190.1; NM_101609.4.
DR AlphaFoldDB; Q9LQK0; -.
DR SMR; Q9LQK0; -.
DR BioGRID; 23560; 1.
DR STRING; 3702.AT1G17470.1; -.
DR PaxDb; Q9LQK0; -.
DR PRIDE; Q9LQK0; -.
DR ProteomicsDB; 224301; -.
DR DNASU; 838320; -.
DR EnsemblPlants; AT1G17470.1; AT1G17470.1; AT1G17470.
DR EnsemblPlants; AT1G17470.2; AT1G17470.2; AT1G17470.
DR GeneID; 838320; -.
DR Gramene; AT1G17470.1; AT1G17470.1; AT1G17470.
DR Gramene; AT1G17470.2; AT1G17470.2; AT1G17470.
DR KEGG; ath:AT1G17470; -.
DR Araport; AT1G17470; -.
DR TAIR; locus:2018826; AT1G17470.
DR eggNOG; KOG1486; Eukaryota.
DR HOGENOM; CLU_044997_0_0_1; -.
DR InParanoid; Q9LQK0; -.
DR OMA; EHEGANI; -.
DR OrthoDB; 754662at2759; -.
DR PhylomeDB; Q9LQK0; -.
DR PRO; PR:Q9LQK0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQK0; baseline and differential.
DR Genevisible; Q9LQK0; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
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 Cytoplasm; Cytoplasmic vesicle; GTP-binding; Lipid-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..399
FT /note="Developmentally-regulated G-protein 1"
FT /id="PRO_0000412608"
FT DOMAIN 63..288
FT /note="OBG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT DOMAIN 288..366
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 367..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69..76
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 115..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 246..249
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT CONFLICT 92
FT /note="Y -> C (in Ref. 5; AAK44073)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="N -> I (in Ref. 1; AAB67830 and 2; AAB53256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 44639 MW; B6A2AF943E9C413B CRC64;
MGIIERIKEI EAEMARTQKN KATEYHLGQL KAKIAKLRTQ LLEPPKGASG GGEGFEVTKY
GHGRVALIGF PSVGKSTLLT MLTGTHSEAA SYEFTTLTCI PGVIHYNDTK IQLLDLPGII
EGASEGKGRG RQVIAVAKSS DLVLMVLDAS KSEGHRQILT KELEAVGLRL NKTPPQIYFK
KKKTGGISFN TTAPLTHIDE KLCYQILHEY KIHNAEVLFR ENATVDDFID VIEGNRKYIK
CVYVYNKIDV VGIDDVDRLS RQPNSIVISC NLKLNLDRLL ARMWDEMGLV RVYSKPQGQQ
PDFDEPFVLS SDRGGCTVED FCNHVHRTLV KDMKYALVWG TSTRHNPQNC GLSQHLEDED
VVQIVKKKER DEGGRGRFKS HSNAPARIAD REKKAPLKQ
