RAC1_ORYSJ
ID RAC1_ORYSJ Reviewed; 214 AA.
AC Q9SSX0; Q0JPC8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Rac-like GTP-binding protein 1;
DE AltName: Full=OsRac1;
GN Name=RAC1; OrderedLocusNames=Os01g0229400, LOC_Os01g12900;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF GLY-19 AND THR-24.
RX PubMed=10485927; DOI=10.1073/pnas.96.19.10922;
RA Kawasaki T., Henmi K., Ono E., Hatakeyama S., Iwano M., Satoh H.,
RA Shimamoto K.;
RT "The small GTP-binding protein Rac is a regulator of cell death in
RT plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10922-10926(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-212.
RX PubMed=11149940; DOI=10.1073/pnas.98.2.759;
RA Ono E., Wong H.L., Kawasaki T., Hasegawa M., Kodama O., Shimamoto K.;
RT "Essential role of the small GTPase Rac in disease resistance of rice.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:759-764(2001).
RN [7]
RP FUNCTION.
RX PubMed=12237405; DOI=10.1073/pnas.192244099;
RA Suharsono U., Fujisawa Y., Kawasaki T., Iwasaki Y., Satoh H., Shimamoto K.;
RT "The heterotrimeric G protein alpha subunit acts upstream of the small
RT GTPase Rac in disease resistance of rice.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13307-13312(2002).
RN [8]
RP FUNCTION.
RX PubMed=15220467; DOI=10.1104/pp.103.036384;
RA Wong H.L., Sakamoto T., Kawasaki T., Umemura K., Shimamoto K.;
RT "Down-regulation of metallothionein, a reactive oxygen scavenger, by the
RT small GTPase OsRac1 in rice.";
RL Plant Physiol. 135:1447-1456(2004).
RN [9]
RP INTERACTION WITH MPK1/MAPK6.
RX PubMed=15951489; DOI=10.1104/pp.104.057414;
RA Lieberherr D., Thao N.P., Nakashima A., Umemura K., Kawasaki T.,
RA Shimamoto K.;
RT "A sphingolipid elicitor-inducible mitogen-activated protein kinase is
RT regulated by the small GTPase OsRac1 and heterotrimeric G-protein in
RT rice.";
RL Plant Physiol. 138:1644-1652(2005).
RN [10]
RP FUNCTION, AND INTERACTION WITH CCR1.
RX PubMed=16380417; DOI=10.1073/pnas.0509875103;
RA Kawasaki T., Koita H., Nakatsubo T., Hasegawa K., Wakabayashi K.,
RA Takahashi H., Umemura K., Umezawa T., Shimamoto K.;
RT "Cinnamoyl-CoA reductase, a key enzyme in lignin biosynthesis, is an
RT effector of small GTPase Rac in defense signaling in rice.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:230-235(2006).
RN [11]
RP NOMENCLATURE.
RX PubMed=16172097; DOI=10.1104/pp.105.063933;
RA Miki D., Itoh R., Shimamoto K.;
RT "RNA silencing of single and multiple members in a gene family of rice.";
RL Plant Physiol. 138:1903-1913(2005).
RN [12]
RP INTERACTION WITH RBOHB.
RX PubMed=19864426; DOI=10.1074/jbc.m109.058909;
RA Oda T., Hashimoto H., Kuwabara N., Akashi S., Hayashi K., Kojima C.,
RA Wong H.L., Kawasaki T., Shimamoto K., Sato M., Shimizu T.;
RT "Structure of the N-terminal regulatory domain of a plant NADPH oxidase and
RT its functional implications.";
RL J. Biol. Chem. 285:1435-1445(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 8-183 IN COMPLEX WITH GTP.
RX PubMed=25128531; DOI=10.1074/jbc.m114.603282;
RA Kosami K., Ohki I., Nagano M., Furuita K., Sugiki T., Kawano Y.,
RA Kawasaki T., Fujiwara T., Nakagawa A., Shimamoto K., Kojima C.;
RT "The crystal structure of the plant small GTPase OsRac1 reveals its mode of
RT binding to NADPH oxidase.";
RL J. Biol. Chem. 289:28569-28578(2014).
CC -!- FUNCTION: Small GTPase playing a general role in disease resistance
CC signaling pathway. Acts downstream of heterotrimeric G protein alpha
CC subunit. Regulates cell death and reactive oxygen species production,
CC probably through NADPH oxidase. Also involved in sphingolipid elicitor
CC (SE)-dependent defense signaling. Activates phytoalexin production and
CC alters defense-related genes. Down-regulates metallothionein 2b, a
CC reactive oxygen scavenger (PubMed:10485927, PubMed:11149940,
CC PubMed:12237405, PubMed:15220467). May control lignin synthesis through
CC regulation of both NADPH oxidase and CCR1 activities during defense
CC responses. Stimulates lignin synthesis in suspension cell culture
CC (PubMed:15951489). {ECO:0000269|PubMed:10485927,
CC ECO:0000269|PubMed:11149940, ECO:0000269|PubMed:12237405,
CC ECO:0000269|PubMed:15220467, ECO:0000269|PubMed:15951489}.
CC -!- SUBUNIT: May interact with MPK1/MAPK6 (PubMed:15951489). Binds to
CC RBOHB, preferentially in the GTP-bound form (PubMed:19864426).
CC Interacts with CCR1 in a GTP-dependent manner (PubMed:16380417).
CC {ECO:0000269|PubMed:15951489, ECO:0000269|PubMed:16380417,
CC ECO:0000269|PubMed:19864426}.
CC -!- INTERACTION:
CC Q9SSX0; Q6K9A2: CCR1; NbExp=3; IntAct=EBI-15561891, EBI-15561872;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11149940}. Membrane
CC {ECO:0000269|PubMed:11149940}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11149940}. Note=Associated with the membrane when
CC activated.
CC -!- PTM: May be palmitoylated.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB029508; BAA84492.1; -; mRNA.
DR EMBL; AP001859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP008207; BAF04400.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS71158.1; -; Genomic_DNA.
DR RefSeq; XP_015621645.1; XM_015766159.1.
DR PDB; 4U5X; X-ray; 1.90 A; A=8-183.
DR PDBsum; 4U5X; -.
DR AlphaFoldDB; Q9SSX0; -.
DR SMR; Q9SSX0; -.
DR DIP; DIP-61088N; -.
DR IntAct; Q9SSX0; 1.
DR STRING; 4530.OS01T0229400-01; -.
DR PaxDb; Q9SSX0; -.
DR PRIDE; Q9SSX0; -.
DR EnsemblPlants; Os01t0229400-02; Os01t0229400-02; Os01g0229400.
DR GeneID; 4325879; -.
DR Gramene; Os01t0229400-02; Os01t0229400-02; Os01g0229400.
DR KEGG; osa:4325879; -.
DR eggNOG; KOG0393; Eukaryota.
DR InParanoid; Q9SSX0; -.
DR OrthoDB; 1091615at2759; -.
DR BRENDA; 3.6.5.2; 4460.
DR PlantReactome; R-OSA-9611432; Recognition of fungal and bacterial pathogens and immunity response.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR ExpressionAtlas; Q9SSX0; baseline and differential.
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:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
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:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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 3D-structure; Apoptosis; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
KW Nucleotide-binding; Palmitate; Plant defense; Reference proteome.
FT CHAIN 1..214
FT /note="Rac-like GTP-binding protein 1"
FT /id="PRO_0000227570"
FT MOTIF 39..47
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 20..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25128531,
FT ECO:0007744|PDB:4U5X"
FT BINDING 42
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25128531,
FT ECO:0007744|PDB:4U5X"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25128531,
FT ECO:0007744|PDB:4U5X"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 123..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25128531,
FT ECO:0007744|PDB:4U5X"
FT BINDING 164..165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25128531,
FT ECO:0007744|PDB:4U5X"
FT MUTAGEN 19
FT /note="G->V: Constitutively active."
FT /evidence="ECO:0000269|PubMed:10485927"
FT MUTAGEN 24
FT /note="T->N: Constitutively inactive."
FT /evidence="ECO:0000269|PubMed:10485927"
FT MUTAGEN 212
FT /note="C->S: Loss of membrane localization."
FT /evidence="ECO:0000269|PubMed:11149940"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:4U5X"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:4U5X"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:4U5X"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:4U5X"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:4U5X"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4U5X"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:4U5X"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:4U5X"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:4U5X"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:4U5X"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:4U5X"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:4U5X"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:4U5X"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4U5X"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:4U5X"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:4U5X"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:4U5X"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:4U5X"
SQ SEQUENCE 214 AA; 23717 MW; AFBAF00E593C0152 CRC64;
MSSAAAATRF IKCVTVGDGA VGKTCMLICY TCNKFPTDYI PTVFDNFSAN VSVDGSVVNL
GLWDTAGQED YSRLRPLSYR GADVFILSFS LISRASYENV QKKWMPELRR FAPGVPVVLV
GTKLDLREDR AYLADHPASS IITTEQGEEL RKLIGAVAYI ECSSKTQRNI KAVFDTAIKV
VLQPPRHKDV TRKKLQSSSN RPVRRYFCGS ACFA
