RAC10_ARATH
ID RAC10_ARATH Reviewed; 215 AA.
AC O82481;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Rac-like GTP-binding protein ARAC10;
DE AltName: Full=GTPase protein ROP11;
GN Name=ARAC10; Synonyms=ROP11; OrderedLocusNames=At5g62880;
GN ORFNames=MQB2.180, MQB2.20;
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].
RC STRAIN=cv. Columbia, and 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [3]
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 [4]
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 [5]
RP PALMITOYLATION AT CYS-202 AND CYS-208, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF CYS-202 AND CYS-208.
RX PubMed=12368496; DOI=10.1105/tpc.005561;
RA Lavy M., Bracha-Drori K., Sternberg H., Yalovsky S.;
RT "A cell-specific, prenylation-independent mechanism regulates targeting of
RT type II RACs.";
RL Plant Cell 14:2431-2450(2002).
RN [6]
RP FUNCTION, INTERACTION WITH ICR5, AND SUBCELLULAR LOCATION.
RX PubMed=22984069; DOI=10.1126/science.1222597;
RA Oda Y., Fukuda H.;
RT "Initiation of cell wall pattern by a Rho- and microtubule-driven symmetry
RT breaking.";
RL Science 337:1333-1336(2012).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=24280391; DOI=10.1105/tpc.113.117853;
RA Oda Y., Fukuda H.;
RT "Rho of plant GTPase signaling regulates the behavior of Arabidopsis
RT kinesin-13A to establish secondary cell wall patterns.";
RL Plant Cell 25:4439-4450(2013).
CC -!- FUNCTION: Involved in local disassembly of cortical microtubules when
CC associated with ICR5 and KIN13A. {ECO:0000269|PubMed:22984069,
CC ECO:0000269|PubMed:24280391}.
CC -!- SUBUNIT: Component of the active ARAC10-IRC5-KIN13A complex
CC (PubMed:24280391). Interacts with ICR5 (PubMed:22984069).
CC {ECO:0000269|PubMed:22984069, ECO:0000269|PubMed:24280391}.
CC -!- INTERACTION:
CC O82481; Q93ZY2: ROPGEF1; NbExp=5; IntAct=EBI-1548072, EBI-4425188;
CC O82481; Q0WNP7: ROPGEF4; NbExp=5; IntAct=EBI-1548072, EBI-7819454;
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Cytoplasm. Cytoplasm,
CC cytoskeleton. Note=Recruited along cortical microtubules upon
CC interaction with ICR5. {ECO:0000269|PubMed:22984069}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AF079485; AAC63014.1; -; mRNA.
DR EMBL; AF115467; AAF40238.1; -; Genomic_DNA.
DR EMBL; AB009053; BAB10857.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97667.1; -; Genomic_DNA.
DR EMBL; BT002997; AAO22805.1; -; mRNA.
DR EMBL; BT004459; AAO42453.1; -; mRNA.
DR PIR; T51824; T51824.
DR RefSeq; NP_201093.1; NM_125682.5.
DR AlphaFoldDB; O82481; -.
DR SMR; O82481; -.
DR BioGRID; 21651; 18.
DR DIP; DIP-39043N; -.
DR IntAct; O82481; 18.
DR MINT; O82481; -.
DR STRING; 3702.AT5G62880.1; -.
DR PaxDb; O82481; -.
DR PRIDE; O82481; -.
DR ProteomicsDB; 236293; -.
DR EnsemblPlants; AT5G62880.1; AT5G62880.1; AT5G62880.
DR GeneID; 836408; -.
DR Gramene; AT5G62880.1; AT5G62880.1; AT5G62880.
DR KEGG; ath:AT5G62880; -.
DR Araport; AT5G62880; -.
DR TAIR; locus:2170778; AT5G62880.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; O82481; -.
DR OMA; NHACNIV; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; O82481; -.
DR PRO; PR:O82481; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O82481; baseline and differential.
DR Genevisible; O82481; AT.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009531; C:secondary cell wall; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:TAIR.
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:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IDA:TAIR.
DR GO; GO:0009664; P:plant-type cell wall organization; IMP:TAIR.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:2001009; P:regulation of plant-type cell wall cellulose biosynthetic process; IGI: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; Cytoskeleton; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Palmitate; Reference proteome.
FT CHAIN 1..215
FT /note="Rac-like GTP-binding protein ARAC10"
FT /id="PRO_0000198924"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 202
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:12368496"
FT LIPID 208
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:12368496"
FT MUTAGEN 202
FT /note="C->S: Affects the membrane location."
FT /evidence="ECO:0000269|PubMed:12368496"
FT MUTAGEN 208
FT /note="C->S: Affects the membrane location."
FT /evidence="ECO:0000269|PubMed:12368496"
SQ SEQUENCE 215 AA; 23879 MW; 02575631F7582E3B CRC64;
MASSASKFIK CVTVGDGAVG KTCMLICYTS NKFPTDYIPT VFDNFSANVV VEGTTVNLGL
WDTAGQEDYN RLRPLSYRGA DVFVLSFSLV SRASYENVFK KWIPELQHFA PGVPLVLVGT
KLDLREDKHY LADHPGLSPV TTAQGEELRK LIGATYYIEC SSKTQQNVKA VFDSAIKEVI
KPLVKQKEKT KKKKKQKSNH GCLSNVLCGR IVTRH
