RAC11_ARATH
ID RAC11_ARATH Reviewed; 197 AA.
AC P92978;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Rac-like GTP-binding protein ARAC11 {ECO:0000303|PubMed:11102387};
DE EC=3.6.5.- {ECO:0000305};
DE AltName: Full=GTPase protein ROP1 {ECO:0000303|PubMed:9765526};
DE Flags: Precursor;
GN Name=ARAC11 {ECO:0000303|PubMed:11102387};
GN Synonyms=RAC11 {ECO:0000303|PubMed:11102387},
GN ROP1 {ECO:0000303|PubMed:9765526};
GN OrderedLocusNames=At3g51300 {ECO:0000312|Araport:AT3G51300};
GN ORFNames=F24M12.340 {ECO:0000312|EMBL:CAB62652.1};
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 [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9765526; DOI=10.1104/pp.118.2.407;
RA Li H., Wu G., Ware D., Davis K.R., Yang Z.;
RT "Arabidopsis Rho-related GTPases: differential gene expression in pollen
RT and polar localization in fission yeast.";
RL Plant Physiol. 118:407-417(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11102387; DOI=10.1093/genetics/156.4.1959;
RA Winge P., Brembu T., Kristensen R., Bones A.M.;
RT "Genetic structure and evolution of RAC-GTPases in Arabidopsis thaliana.";
RL Genetics 156:1959-1971(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 INTERACTION WITH UGT1.
RX PubMed=11283335; DOI=10.2307/3871339;
RA Hong Z., Zhang Z., Olson J.M., Verma D.P.S.;
RT "A novel UDP-glucose transferase is part of the callose synthase complex
RT and interacts with phragmoplastin at the forming cell plate.";
RL Plant Cell 13:769-779(2001).
RN [7]
RP INTERACTION WITH ICR1; ICR2; ICR3; ICR4 AND ICR5.
RX PubMed=19825600; DOI=10.1093/mp/ssn051;
RA Li S., Gu Y., Yan A., Lord E., Yang Z.B.;
RT "RIP1 (ROP Interactive Partner 1)/ICR1 marks pollen germination sites and
RT may act in the ROP1 pathway in the control of polarized pollen growth.";
RL Mol. Plant 1:1021-1035(2008).
RN [8]
RP INTERACTION WITH PHIP1.
RX PubMed=18621982; DOI=10.1104/pp.108.120527;
RA Ma L., Xie B., Hong Z., Verma D.P.S., Zhang Z.;
RT "A novel RNA-binding protein associated with cell plate formation.";
RL Plant Physiol. 148:223-234(2008).
RN [9]
RP INTERACTION WITH ICR1 AND ICR5.
RX PubMed=20832900; DOI=10.1016/j.ejcb.2010.08.003;
RA Mucha E., Hoefle C., Huckelhoven R., Berken A.;
RT "RIP3 and AtKinesin-13A - a novel interaction linking Rho proteins of
RT plants to microtubules.";
RL Eur. J. Cell Biol. 89:906-916(2010).
RN [10]
RP INTERACTION WITH ROPGEF1 AND PRK2.
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: May be involved in cell polarity control during the actin-
CC dependent tip growth of pollen tubes. May regulate callose synthase 1
CC (CALS1) activity through the interaction with UGT1.
CC {ECO:0000269|PubMed:9765526}.
CC -!- FUNCTION: Inactive GDP-bound Rho GTPases reside in the cytosol, are
CC found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and
CC are released from the GDI protein in order to translocate to membranes
CC upon activation. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000305};
CC -!- SUBUNIT: Part of a complex containing ROPGEF1 and PRK2
CC (PubMed:23024212). Interacts with UGT1, ICR1, ICR2, ICR3, ICR4 and
CC ICR5. Interacts with PHIP1 when activated by GTP (PubMed:18621982).
CC {ECO:0000269|PubMed:11283335, ECO:0000269|PubMed:18621982,
CC ECO:0000269|PubMed:19825600, ECO:0000269|PubMed:20832900,
CC ECO:0000269|PubMed:23024212}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=Associated with the
CC membrane when activated.
CC -!- TISSUE SPECIFICITY: Exclusively expressed in mature pollen and pollen
CC tubes. {ECO:0000269|PubMed:9765526}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; U49971; AAC78390.1; -; Genomic_DNA.
DR EMBL; AF085480; AAC35850.1; -; Genomic_DNA.
DR EMBL; AL132980; CAB62652.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78776.1; -; Genomic_DNA.
DR EMBL; AF375412; AAK52996.1; -; mRNA.
DR EMBL; AY066054; AAL47421.1; -; mRNA.
DR PIR; T45761; T45761.
DR RefSeq; NP_190698.1; NM_114989.4.
DR AlphaFoldDB; P92978; -.
DR SMR; P92978; -.
DR BioGRID; 9611; 22.
DR IntAct; P92978; 3.
DR STRING; 3702.AT3G51300.1; -.
DR PaxDb; P92978; -.
DR PRIDE; P92978; -.
DR ProteomicsDB; 234822; -.
DR EnsemblPlants; AT3G51300.1; AT3G51300.1; AT3G51300.
DR GeneID; 824293; -.
DR Gramene; AT3G51300.1; AT3G51300.1; AT3G51300.
DR KEGG; ath:AT3G51300; -.
DR Araport; AT3G51300; -.
DR TAIR; locus:2080878; AT3G51300.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; P92978; -.
DR OMA; TVNKRPC; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; P92978; -.
DR PRO; PR:P92978; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P92978; baseline and differential.
DR Genevisible; P92978; AT.
DR GO; GO:0045177; C:apical part of cell; IDA:TAIR.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; ISS:TAIR.
DR GO; GO:0032794; F:GTPase activating protein binding; IPI:TAIR.
DR GO; GO:0003924; F:GTPase activity; ISS:TAIR.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051650; P:establishment of vesicle localization; IDA:TAIR.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030834; P:regulation of actin filament depolymerization; IGI:TAIR.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IGI:TAIR.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IDA:TAIR.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..194
FT /note="Rac-like GTP-binding protein ARAC11"
FT /id="PRO_0000198925"
FT PROPEP 195..197
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000227587"
FT MOTIF 35..43
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 194
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 194
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 197 AA; 21619 MW; DAF48ED8D3051AC5 CRC64;
MSASRFVKCV TVGDGAVGKT CLLISYTSNT FPTDYVPTVF DNFSANVVVN GSTVNLGLWD
TAGQEDYNRL RPLSYRGADV FILAFSLISK ASYENVSKKW IPELKHYAPG VPIVLVGTKL
DLRDDKQFFI DHPGAVPITT AQGEELRKQI GAPTYIECSS KTQENVKAVF DAAIRVVLQP
PKQKKKKSKA QKACSIL
