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Rac-like GTP-binding protein ARAC11 (GTPase protein ROP1)

 RAC11_ARATH             Reviewed;         197 AA.
P92978;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 2.
27-SEP-2017, entry version 135.
RecName: Full=Rac-like GTP-binding protein ARAC11;
AltName: Full=GTPase protein ROP1;
Flags: Precursor;
Name=ARAC11; Synonyms=RAC11, ROP1; OrderedLocusNames=At3g51300;
ORFNames=F24M12.340;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=9765526; DOI=10.1104/pp.118.2.407;
Li H., Wu G., Ware D., Davis K.R., Yang Z.;
"Arabidopsis Rho-related GTPases: differential gene expression in
pollen and polar localization in fission yeast.";
Plant Physiol. 118:407-417(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Landsberg erecta;
PubMed=11102387;
Winge P., Brembu T., Kristensen R., Bones A.M.;
"Genetic structure and evolution of RAC-GTPases in Arabidopsis
thaliana.";
Genetics 156:1959-1971(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
INTERACTION WITH UGT1.
PubMed=11283335; DOI=10.1105/tpc.13.4.769;
Hong Z., Zhang Z., Olson J.M., Verma D.P.S.;
"A novel UDP-glucose transferase is part of the callose synthase
complex and interacts with phragmoplastin at the forming cell plate.";
Plant Cell 13:769-779(2001).
[7]
INTERACTION WITH ICR1; ICR2; ICR3; ICR4 AND ICR5.
PubMed=19825600; DOI=10.1093/mp/ssn051;
Li S., Gu Y., Yan A., Lord E., Yang Z.B.;
"RIP1 (ROP Interactive Partner 1)/ICR1 marks pollen germination sites
and may act in the ROP1 pathway in the control of polarized pollen
growth.";
Mol. Plant 1:1021-1035(2008).
[8]
INTERACTION WITH ICR1 AND ICR5.
PubMed=20832900; DOI=10.1016/j.ejcb.2010.08.003;
Mucha E., Hoefle C., Huckelhoven R., Berken A.;
"RIP3 and AtKinesin-13A - a novel interaction linking Rho proteins of
plants to microtubules.";
Eur. J. Cell Biol. 89:906-916(2010).
[9]
INTERACTION WITH ROPGEF1 AND PRK2.
PubMed=23024212; DOI=10.1093/mp/sss103;
Chang F., Gu Y., Ma H., Yang Z.;
"AtPRK2 Promotes ROP1 activation via RopGEFs in the control of
polarized pollen tube growth.";
Mol. Plant 6:1187-1201(2013).
-!- FUNCTION: May be involved in cell polarity control during the
actin-dependent tip growth of pollen tubes. May regulate callose
synthase 1 (CALS1) activity through the interaction with UGT1.
{ECO:0000269|PubMed:9765526}.
-!- FUNCTION: Inactive GDP-bound Rho GTPases reside in the cytosol,
are found in a complex with Rho GDP-dissociation inhibitors (Rho
GDIs), and are released from the GDI protein in order to
translocate to membranes upon activation. {ECO:0000250}.
-!- SUBUNIT: Part of a complex containing ROPGEF1 and PRK2
(PubMed:23024212). Interacts with UGT1, ICR1, ICR2, ICR3, ICR4 and
ICR5. {ECO:0000269|PubMed:11283335, ECO:0000269|PubMed:19825600,
ECO:0000269|PubMed:20832900, ECO:0000269|PubMed:23024212}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Note=Associated with the membrane when activated.
-!- TISSUE SPECIFICITY: Exclusively expressed in mature pollen and
pollen tubes. {ECO:0000269|PubMed:9765526}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U49971; AAC78390.1; -; Genomic_DNA.
EMBL; AF085480; AAC35850.1; -; Genomic_DNA.
EMBL; AL132980; CAB62652.1; -; Genomic_DNA.
EMBL; CP002686; AEE78776.1; -; Genomic_DNA.
EMBL; AF375412; AAK52996.1; -; mRNA.
EMBL; AY066054; AAL47421.1; -; mRNA.
PIR; T45761; T45761.
RefSeq; NP_190698.1; NM_114989.4.
UniGene; At.28445; -.
ProteinModelPortal; P92978; -.
SMR; P92978; -.
BioGrid; 9611; 22.
IntAct; P92978; 3.
STRING; 3702.AT3G51300.1; -.
PaxDb; P92978; -.
EnsemblPlants; AT3G51300.1; AT3G51300.1; AT3G51300.
GeneID; 824293; -.
Gramene; AT3G51300.1; AT3G51300.1; AT3G51300.
KEGG; ath:AT3G51300; -.
Araport; AT3G51300; -.
TAIR; locus:2080878; AT3G51300.
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
HOGENOM; HOG000233974; -.
InParanoid; P92978; -.
KO; K04392; -.
OMA; YSAQMSV; -.
OrthoDB; EOG09360LB1; -.
PhylomeDB; P92978; -.
Reactome; R-ATH-194840; Rho GTPase cycle.
PRO; PR:P92978; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; P92978; baseline and differential.
Genevisible; P92978; AT.
GO; GO:0045177; C:apical part of cell; IDA:TAIR.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005730; C:nucleolus; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0009524; C:phragmoplast; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; TAS:TAIR.
GO; GO:0005819; C:spindle; IDA:TAIR.
GO; GO:0005525; F:GTP binding; ISS:TAIR.
GO; GO:0032794; F:GTPase activating protein binding; IPI:TAIR.
GO; GO:0003924; F:GTPase activity; ISS:TAIR.
GO; GO:0051650; P:establishment of vesicle localization; IDA:TAIR.
GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
GO; GO:0030834; P:regulation of actin filament depolymerization; IGI:TAIR.
GO; GO:0030833; P:regulation of actin filament polymerization; IGI:TAIR.
GO; GO:0017157; P:regulation of exocytosis; IDA:TAIR.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR003578; Small_GTPase_Rho.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51420; RHO; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
Methylation; Nucleotide-binding; Prenylation; Reference proteome.
CHAIN 1 194 Rac-like GTP-binding protein ARAC11.
/FTId=PRO_0000198925.
PROPEP 195 197 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000227587.
NP_BIND 13 20 GTP. {ECO:0000250}.
NP_BIND 60 64 GTP. {ECO:0000250}.
NP_BIND 118 121 GTP. {ECO:0000250}.
MOTIF 35 43 Effector region. {ECO:0000255}.
COMPBIAS 182 189 Poly-Lys.
MOD_RES 194 194 Cysteine methyl ester. {ECO:0000255}.
LIPID 194 194 S-geranylgeranyl cysteine. {ECO:0000255}.
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


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