ID RAC4_ORYSJ Reviewed; 215 AA.
AC Q67VP4; Q0DDC3; Q94JL4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Rac-like GTP-binding protein 4;
DE AltName: Full=GTPase protein ROP4;
DE AltName: Full=OsRac4;
GN Name=RAC4; Synonyms=ROP4; OrderedLocusNames=Os06g0234200, LOC_Os06g12790;
GN ORFNames=OsJ_20720 {ECO:0000312|EMBL:EEE65396.1}, OSJNBa0080E19.8-1,
GN OSJNBb0061B07.23-1;
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].
RX PubMed=14605221; DOI=10.1104/pp.103.029900;
RA Christensen T.M., Vejlupkova Z., Sharma Y.K., Arthur K.M., Spatafora J.W.,
RA Albright C.A., Meeley R.B., Duvick J.P., Quatrano R.S., Fowler J.E.;
RT "Conserved subgroups and developmental regulation in the monocot rop gene
RT family.";
RL Plant Physiol. 133:1791-1808(2003).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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; AF380335; AAK55445.1; -; mRNA.
DR EMBL; AP004785; BAD37775.1; -; Genomic_DNA.
DR EMBL; AP005170; BAD37916.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19150.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS96939.1; -; Genomic_DNA.
DR EMBL; CM000143; EEE65396.1; -; Genomic_DNA.
DR EMBL; AK061102; BAG87727.1; -; mRNA.
DR RefSeq; XP_015641323.1; XM_015785837.1.
DR AlphaFoldDB; Q67VP4; -.
DR SMR; Q67VP4; -.
DR STRING; 39947.Q67VP4; -.
DR PaxDb; 39947-Q67VP4; -.
DR EnsemblPlants; Os06t0234200-03; Os06t0234200-03; Os06g0234200.
DR GeneID; 4340590; -.
DR Gramene; Os06t0234200-03; Os06t0234200-03; Os06g0234200.
DR KEGG; osa:4340590; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q67VP4; -.
DR OMA; RRLGCFK; -.
DR OrthoDB; 3817092at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; Q67VP4; baseline and differential.
DR Genevisible; Q67VP4; OS.
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: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:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd04133; Rop_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR24072:SF315; RAC-LIKE GTP-BINDING PROTEIN 4; 1.
DR PANTHER; PTHR24072; RHO FAMILY GTPASE; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..215
FT /note="Rac-like GTP-binding protein 4"
FT /id="PRO_0000227573"
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"
SQ SEQUENCE 215 AA; 24079 MW; B8DE049731C009DA CRC64;
MASSASRFIK CVTVGDGAVG KTCMLICYTS NKFPTDYVPT VFDNFSANVV VDGTTVNLGL
WDTAGQEDYN RLRPLSYRGA DVFVLAFSLV SRASYENVMK KWLPELQHYA PGVPIVLVGT
KLDLREDKHY LLDHPSLVPV TTAQGEELRK HIGATCYIEC SSKTQQNVKA VFDAAIKVVI
KPPTKQRDRK KKKTRRGCSF FCKGVMSRRR LVCFK
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