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RAC9_ARATH
ID   RAC9_ARATH              Reviewed;         209 AA.
AC   Q9XGU0; O80508;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Rac-like GTP-binding protein ARAC9;
DE   AltName: Full=GTPase protein ROP8;
DE   Flags: Precursor;
GN   Name=ARAC9; Synonyms=ROP8; OrderedLocusNames=At2g44690; ORFNames=F16B22.18;
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;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   INTERACTION WITH SPK1.
RX   PubMed=17267444; DOI=10.1242/dev.02792;
RA   Uhrig J.F., Mutondo M., Zimmermann I., Deeks M.J., Machesky L.M.,
RA   Thomas P., Uhrig S., Rambke C., Hussey P.J., Huelskamp M.;
RT   "The role of Arabidopsis SCAR genes in ARP2-ARP3-dependent cell
RT   morphogenesis.";
RL   Development 134:967-977(2007).
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   -!- SUBUNIT: Interacts with SPK1. {ECO:0000269|PubMed:17267444}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Note=Associated with the
CC       membrane when activated.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000305}.
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DR   EMBL; AF156896; AAD42972.1; -; mRNA.
DR   EMBL; AC003672; AAC27471.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10456.1; -; Genomic_DNA.
DR   PIR; T01596; T01596.
DR   RefSeq; NP_566024.1; NM_130033.3.
DR   AlphaFoldDB; Q9XGU0; -.
DR   SMR; Q9XGU0; -.
DR   BioGRID; 4413; 7.
DR   IntAct; Q9XGU0; 6.
DR   STRING; 3702.AT2G44690.1; -.
DR   PaxDb; Q9XGU0; -.
DR   PRIDE; Q9XGU0; -.
DR   ProteomicsDB; 236417; -.
DR   EnsemblPlants; AT2G44690.1; AT2G44690.1; AT2G44690.
DR   GeneID; 819077; -.
DR   Gramene; AT2G44690.1; AT2G44690.1; AT2G44690.
DR   KEGG; ath:AT2G44690; -.
DR   Araport; AT2G44690; -.
DR   TAIR; locus:2042326; AT2G44690.
DR   eggNOG; KOG0393; Eukaryota.
DR   HOGENOM; CLU_041217_21_3_1; -.
DR   InParanoid; Q9XGU0; -.
DR   OMA; HHCASAP; -.
DR   OrthoDB; 1091615at2759; -.
DR   PhylomeDB; Q9XGU0; -.
DR   PRO; PR:Q9XGU0; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9XGU0; baseline and differential.
DR   Genevisible; Q9XGU0; AT.
DR   GO; GO:0000421; C:autophagosome membrane; 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:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0006914; P:autophagy; IDA:TAIR.
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: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: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; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN           1..206
FT                   /note="Rac-like GTP-binding protein ARAC9"
FT                   /id="PRO_0000198923"
FT   PROPEP          207..209
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000227586"
FT   MOTIF           47..55
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
FT   BINDING         25..32
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         72..76
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         130..133
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         206
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           206
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   209 AA;  22972 MW;  B09E41B1E86F00C9 CRC64;
     MSASMAATST SSATATTFIK CVTVGDGAVG KTCLLISYTS NTFPTDYVPT VFDNFNANVL
     VDGKTVNLGL WDTAGQEDYN RVRPLSYRGA DVFILAFSLI SRPSFENIAK KWVPELRHYA
     PTVPIVLVGT KSDLRDNMQF PKNYPGACTI FPEQGQELRK EIGALAYIEC SSKAQMNVKA
     VFDEAIKVVL HPPSKTKKRK RKIGLCHVL
 
 
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