ROGF1_ARATH
ID ROGF1_ARATH Reviewed; 548 AA.
AC Q93ZY2; Q9SVE2;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Rop guanine nucleotide exchange factor 1;
DE Short=AtRopGEF1;
DE AltName: Full=Kinase partner protein-like;
DE Short=KPP-like;
DE AltName: Full=Rho of plants guanine nucleotide exchange factor 1;
GN Name=ROPGEF1; OrderedLocusNames=At4g38430; ORFNames=F22I13.200;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DOMAIN, AND GENE FAMILY.
RX PubMed=15980860; DOI=10.1038/nature03883;
RA Berken A., Thomas C., Wittinghofer A.;
RT "A new family of RhoGEFs activates the Rop molecular switch in plants.";
RL Nature 436:1176-1180(2005).
RN [6]
RP FUNCTION, INTERACTION WITH ARAC11/ROP1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16415208; DOI=10.1105/tpc.105.036434;
RA Gu Y., Li S., Lord E.M., Yang Z.;
RT "Members of a novel class of Arabidopsis Rho guanine nucleotide exchange
RT factors control Rho GTPase-dependent polar growth.";
RL Plant Cell 18:366-381(2006).
RN [7]
RP INTERACTION WITH FER.
RX PubMed=20876100; DOI=10.1073/pnas.1005366107;
RA Duan Q., Kita D., Li C., Cheung A.Y., Wu H.M.;
RT "FERONIA receptor-like kinase regulates RHO GTPase signaling of root hair
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17821-17826(2010).
RN [8]
RP FUNCTION, INTERACTION WITH ARAC10/ROP11, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22500990; DOI=10.1016/j.febslet.2012.03.040;
RA Li Z., Liu D.;
RT "ROPGEF1 and ROPGEF4 are functional regulators of ROP11 GTPase in ABA-
RT mediated stomatal closure in Arabidopsis.";
RL FEBS Lett. 586:1253-1258(2012).
RN [9]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH ARAC11/ROP1; PRK1; PRK2;
RP PRK3 AND PRK4, AND MUTAGENESIS OF SER-458; SER-460; SER-480; SER-484;
RP SER-488 AND SER-501.
RX PubMed=23024212; DOI=10.1093/mp/sss103;
RA Chang F., Gu Y., Ma H., Yang Z.;
RT "AtPRK2 Promotes ROP1 activation via RopGEFs in the control of polarized
RT pollen tube growth.";
RL Mol. Plant 6:1187-1201(2013).
CC -!- FUNCTION: Guanine-nucleotide exchange factor (GEF) that acts as an
CC activator of Rop (Rho of plants) GTPases by promoting the exchange of
CC GDP for GTP. Acts downstream of PRK2 in the control of polarized pollen
CC tube growth by activating ARAC11/ROP1. In association with ROPGEF4,
CC acts as specific regulator of ARAC10/ROP11 function in ABA-mediated
CC stomatal closure. May play a role in the Rac/Rop-signaling pathway that
CC controls ROS-mediated root hair development.
CC {ECO:0000269|PubMed:15980860, ECO:0000269|PubMed:16415208,
CC ECO:0000269|PubMed:22500990, ECO:0000269|PubMed:23024212}.
CC -!- ACTIVITY REGULATION: Phosphorylation at Ser-460 and Ser-480 by PRK2
CC releases ROPGEF1 auto-inhibition, thereby activating ROPGEF1, which in
CC turn activates ARAC11/ROP1. {ECO:0000269|PubMed:23024212}.
CC -!- SUBUNIT: Interacts with ARAC10/ROP11 and FER. Forms a complex with
CC ARAC11/ROP1 and PRK2 (PubMed:23024212). Interacts in vitro (via PRONE
CC domain) with PRK1, PRK2, PRK3 and PRK4 (PubMed:23024212). The C-
CC terminal region is also important for the interaction with PRK2
CC (PubMed:23024212). {ECO:0000269|PubMed:16415208,
CC ECO:0000269|PubMed:20876100, ECO:0000269|PubMed:22500990,
CC ECO:0000269|PubMed:23024212}.
CC -!- INTERACTION:
CC Q93ZY2; P49597: ABI1; NbExp=4; IntAct=EBI-4425188, EBI-782526;
CC Q93ZY2; Q9FLI3: AHG1; NbExp=2; IntAct=EBI-4425188, EBI-2363348;
CC Q93ZY2; O82481: ARAC10; NbExp=5; IntAct=EBI-4425188, EBI-1548072;
CC Q93ZY2; Q9SCZ4: FER; NbExp=4; IntAct=EBI-4425188, EBI-15880405;
CC Q93ZY2; Q9M811: ROPGEF11; NbExp=3; IntAct=EBI-4425188, EBI-16206717;
CC Q93ZY2; Q9FIF5: SAG113; NbExp=2; IntAct=EBI-4425188, EBI-2363373;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane
CC {ECO:0000269|PubMed:16415208}. Note=Localizes to the apical region of
CC the pollen tube plasma membrane to activate ARAC11/ROP1 and interacts
CC with ARAC10/ROP11 on plasma membrane in guard cells.
CC {ECO:0000269|PubMed:16415208}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, leaves, stems,
CC sepals, petals, anthers, pollen grains, stigmas and siliques.
CC {ECO:0000269|PubMed:16415208, ECO:0000269|PubMed:22500990}.
CC -!- DOMAIN: The PRONE (plant-specific Rop nucleotide exchanger) domain is
CC responsible for the GEF activity. The intrinsic dissociation of ROP4-
CC GDP is stimulated 15-fold by the PRONE domain (PubMed:15980860),
CC whereas that of ROP1-GDP is increased 350-fold (PubMed:16415208).
CC {ECO:0000269|PubMed:15980860, ECO:0000269|PubMed:16415208}.
CC -!- PTM: Phosphorylated at Ser-460 and Ser-480 by PRK2. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:22500990}.
CC -!- MISCELLANEOUS: Plants overexpressing ROPGEF1 or ROPGEF4 are relatively
CC insensitive to ABA-induced stomatal closure and become severely wilted
CC during drought stress. A similar phenotype is observed in plants
CC expressing a constitutively active ARAC10/ROP11 (PubMed:22500990).
CC {ECO:0000305|PubMed:22500990}.
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DR EMBL; AL035539; CAB37499.1; -; Genomic_DNA.
DR EMBL; AL161593; CAB80508.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86928.1; -; Genomic_DNA.
DR EMBL; AY056193; AAL07042.1; -; mRNA.
DR EMBL; AY056375; AAL08231.1; -; mRNA.
DR EMBL; AY133649; AAM91479.1; -; mRNA.
DR EMBL; BT000462; AAN17439.1; -; mRNA.
DR EMBL; BT000975; AAN41375.1; -; mRNA.
DR EMBL; AY084995; AAM61554.1; -; mRNA.
DR PIR; T05671; T05671.
DR RefSeq; NP_195556.1; NM_120005.4.
DR AlphaFoldDB; Q93ZY2; -.
DR SMR; Q93ZY2; -.
DR BioGRID; 15280; 8.
DR DIP; DIP-59393N; -.
DR IntAct; Q93ZY2; 15.
DR MINT; Q93ZY2; -.
DR STRING; 3702.AT4G38430.1; -.
DR iPTMnet; Q93ZY2; -.
DR PaxDb; Q93ZY2; -.
DR PRIDE; Q93ZY2; -.
DR ProteomicsDB; 228187; -.
DR EnsemblPlants; AT4G38430.1; AT4G38430.1; AT4G38430.
DR GeneID; 830000; -.
DR Gramene; AT4G38430.1; AT4G38430.1; AT4G38430.
DR KEGG; ath:AT4G38430; -.
DR Araport; AT4G38430; -.
DR TAIR; locus:2121828; AT4G38430.
DR eggNOG; ENOG502QPIY; Eukaryota.
DR HOGENOM; CLU_019073_2_1_1; -.
DR InParanoid; Q93ZY2; -.
DR OMA; QSDRCGS; -.
DR OrthoDB; 482824at2759; -.
DR PhylomeDB; Q93ZY2; -.
DR PRO; PR:Q93ZY2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93ZY2; baseline and differential.
DR Genevisible; Q93ZY2; AT.
DR GO; GO:0016324; C:apical plasma membrane; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:2001108; P:positive regulation of Rho guanyl-nucleotide exchange factor activity; IMP:TAIR.
DR GO; GO:2000012; P:regulation of auxin polar transport; IMP:TAIR.
DR GO; GO:0080092; P:regulation of pollen tube growth; IGI:TAIR.
DR InterPro; IPR005512; PRONE_dom.
DR InterPro; IPR038937; RopGEF.
DR PANTHER; PTHR33101; PTHR33101; 1.
DR Pfam; PF03759; PRONE; 1.
DR PROSITE; PS51334; PRONE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
KW Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1..548
FT /note="Rop guanine nucleotide exchange factor 1"
FT /id="PRO_0000234058"
FT DOMAIN 81..462
FT /note="PRONE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00663"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..548
FT /note="Involved in auto-inhibition"
FT COMPBIAS 16..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MUTAGEN 458
FT /note="S->A: No effect on function in polarized pollen tube
FT growth."
FT /evidence="ECO:0000269|PubMed:23024212"
FT MUTAGEN 460
FT /note="S->A: Loss of function in polarized pollen tube
FT growth."
FT /evidence="ECO:0000269|PubMed:23024212"
FT MUTAGEN 480
FT /note="S->A: Loss of function in polarized pollen tube
FT growth."
FT /evidence="ECO:0000269|PubMed:23024212"
FT MUTAGEN 484
FT /note="S->A: No effect on function in polarized pollen tube
FT growth."
FT /evidence="ECO:0000269|PubMed:23024212"
FT MUTAGEN 488
FT /note="S->A: No effect on function in polarized pollen tube
FT growth."
FT /evidence="ECO:0000269|PubMed:23024212"
FT MUTAGEN 501
FT /note="S->A: No effect on function in polarized pollen tube
FT growth."
FT /evidence="ECO:0000269|PubMed:23024212"
FT CONFLICT 548
FT /note="D -> G (in Ref. 3; AAL07042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 60848 MW; 7E6A8086E0FA5EC6 CRC64;
MGSLSSEEDD EVSSERCGSY SPSADISESE SSSSFSCHRF DGEGASSSIP SSPRVVAGRG
FYFPAPVMLP VIGGKDVVWD DKQPDNDLSE IEMMKERFAK LLLGEDMSGG GKGVCTALAI
SNAITNLSAT VFGELWRLEP LAPQKKAMWR RELEWLLCVS DSIVELIPSI QQFPGGGTYE
IMETRPRSDL YANLPALKKL DAMLIDMLDA FSDTEFWYTD RGIVLGDCDK DSYNSPASVR
QEDKWWLPCP KVPPNGLSEE ARKKLQQCRD FANQILKAAL AINSGVLAEM EIPDPYLETL
PKSGKECLGE IIYQYLTANK FSPECLLDCL DLSSEHQTLE IANRIEAAVH VWRQKNGRRH
KKQAKLKLSS WGGKVKGLVN DNERNDFLVQ RAETLLQSLR IRFPGLPQTT LDMNKIQYNK
DVGQSILESY SRVMESMAFN ITARIDDVLY VDDAMRRSIS VTESLSLFSI NGLNPQKAFS
VQSSPHGSPF ATPALSVASR SPRRAPPLYS VKRNGTREKG IVGETEKAWS YAGNLSSRRV
TGVTPERD
