RAC2_ORYSJ
ID RAC2_ORYSJ Reviewed; 214 AA.
AC Q68Y52; Q0DGS9; Q9SSW9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Rac-like GTP-binding protein 2;
DE AltName: Full=OsRac2;
GN Name=RAC2; OrderedLocusNames=Os05g0513800, LOC_Os05g43820;
GN ORFNames=B1155G07.15, OsJ_19185 {ECO:0000312|EMBL:EEE64345.1}, P0022D06.2;
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], AND TISSUE SPECIFICITY.
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
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).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=Associated with the
CC membrane when activated.
CC -!- PTM: May be palmitoylated.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AB029509; BAA84493.1; -; mRNA.
DR EMBL; AC130604; AAV59301.1; -; Genomic_DNA.
DR EMBL; AC132485; AAU03100.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17944.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS94867.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE64345.1; -; Genomic_DNA.
DR RefSeq; XP_015638759.1; XM_015783273.1.
DR AlphaFoldDB; Q68Y52; -.
DR SMR; Q68Y52; -.
DR STRING; 4530.OS05T0513800-01; -.
DR PaxDb; Q68Y52; -.
DR PRIDE; Q68Y52; -.
DR EnsemblPlants; Os05t0513800-01; Os05t0513800-01; Os05g0513800.
DR GeneID; 4339304; -.
DR Gramene; Os05t0513800-01; Os05t0513800-01; Os05g0513800.
DR KEGG; osa:4339304; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q68Y52; -.
DR OMA; ITHHQQK; -.
DR OrthoDB; 1091615at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; Q68Y52; baseline and differential.
DR Genevisible; Q68Y52; OS.
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: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 2: Evidence at transcript level;
KW Cytoplasm; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW Palmitate; Reference proteome.
FT CHAIN 1..214
FT /note="Rac-like GTP-binding protein 2"
FT /id="PRO_0000227571"
FT MOTIF 36..44
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 214 AA; 23537 MW; E7E5910E7794868A CRC64;
MSGATKFIKC VTVGDGAVGK TCMLICYTSN KFPTDYIPTV FDNFSANVSV DGNIVNLGLW
DTAGQEDYSR LRPLSYRGAD IFVLAFSLIS RASYENVLKK WMPELRRFAP NVPIVLVGTK
LDLRDHRSYL ADHPAASAIT TAQGEELRKQ IGAAAYIECS SKTQQNIKAV FDTAIKVVLQ
PPRRRGETTM ARKKTRRSTG CSLKNLMCGS ACVV
