RAC4_ARATH
ID RAC4_ARATH Reviewed; 195 AA.
AC Q38919;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Rac-like GTP-binding protein ARAC4 {ECO:0000303|PubMed:9349271};
DE Short=AtRAC4 {ECO:0000303|PubMed:11102387};
DE AltName: Full=GTPase protein ROP2 {ECO:0000303|PubMed:11971133};
DE Flags: Precursor;
GN Name=ARAC4 {ECO:0000303|PubMed:9349271};
GN Synonyms=ROP2 {ECO:0000303|PubMed:11971133};
GN OrderedLocusNames=At1g20090 {ECO:0000312|Araport:AT1G20090};
GN ORFNames=T20H2.12 {ECO:0000312|EMBL:AAF79903.1};
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=9349271; DOI=10.1023/a:1005804508902;
RA Winge P., Brembu T., Bones A.M.;
RT "Cloning and characterization of rac-like cDNAs from Arabidopsis
RT thaliana.";
RL Plant Mol. Biol. 35:483-495(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9765526; DOI=10.1104/pp.118.2.407;
RA Li H., Wu G., Ware D., Davis K.R., Yang Z.;
RT "Arabidopsis Rho-related GTPases: differential gene expression in pollen
RT and polar localization in fission yeast.";
RL Plant Physiol. 118:407-417(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
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 [6]
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 [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11971133; DOI=10.1105/tpc.010359;
RA Jones M.A., Shen J., Fu Y., Li H., Yang Z., Grierson C.S.;
RT "The Arabidopsis Rop2 GTPase is a positive regulator of both root hair
RT initiation and tip growth.";
RL Plant Cell 14:763-776(2002).
RN [8]
RP INTERACTION WITH PIR.
RX PubMed=15294869; DOI=10.1242/dev.01307;
RA Basu D., El-Din El-Assal S., Le J., Mallery E.L., Szymanski D.B.;
RT "Interchangeable functions of Arabidopsis PIROGI and the human WAVE complex
RT subunit SRA1 during leaf epidermal development.";
RL Development 131:4345-4355(2004).
RN [9]
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).
RN [10]
RP INTERACTION WITH SPK1.
RC STRAIN=cv. Columbia;
RX PubMed=18308939; DOI=10.1073/pnas.0710294105;
RA Basu D., Le J., Zakharova T., Mallery E.L., Szymanski D.B.;
RT "A SPIKE1 signaling complex controls actin-dependent cell morphogenesis
RT through the heteromeric WAVE and ARP2/3 complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:4044-4049(2008).
RN [11]
RP INTERACTION WITH ICR1 AND ICR5.
RX PubMed=20832900; DOI=10.1016/j.ejcb.2010.08.003;
RA Mucha E., Hoefle C., Huckelhoven R., Berken A.;
RT "RIP3 and AtKinesin-13A - a novel interaction linking Rho proteins of
RT plants to microtubules.";
RL Eur. J. Cell Biol. 89:906-916(2010).
RN [12]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27251533; DOI=10.1038/nplants.2015.162;
RA Stanislas T., Hueser A., Barbosa I.C.R., Kiefer C.S., Brackmann K.,
RA Pietra S., Gustavsson A., Zourelidou M., Schwechheimer C., Grebe M.;
RT "Arabidopsis D6PK is a lipid domain-dependent mediator of root epidermal
RT planar polarity.";
RL Nat. Plants 1:15162-15162(2015).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=30770391; DOI=10.1242/dev.168559;
RA Gendre D., Baral A., Dang X., Esnay N., Boutte Y., Stanislas T., Vain T.,
RA Claverol S., Gustavsson A., Lin D., Grebe M., Bhalerao R.P.;
RT "Rho-of-plant activated root hair formation requires Arabidopsis YIP4a/b
RT gene function.";
RL Development 146:0-0(2019).
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 (By similarity). Involved in cell polarity control
CC during the actin-dependent tip growth of root hairs, thus regulating
CC root hair length and root hair initiation (PubMed:30770391). May
CC regulate a WAVE complex that activates the Arp2/3 complex.
CC {ECO:0000250, ECO:0000269|PubMed:11971133,
CC ECO:0000269|PubMed:30770391}.
CC -!- SUBUNIT: Interacts with SPK1, ICR1, ICR5 and PIR.
CC {ECO:0000269|PubMed:15294869, ECO:0000269|PubMed:17267444,
CC ECO:0000269|PubMed:18308939, ECO:0000269|PubMed:20832900}.
CC -!- INTERACTION:
CC Q38919; Q9SCZ4: FER; NbExp=2; IntAct=EBI-1548187, EBI-15880405;
CC Q38919; Q8SAB7: SPK1; NbExp=3; IntAct=EBI-1548187, EBI-1547917;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q38937}. Cell
CC membrane {ECO:0000269|PubMed:27251533, ECO:0000269|PubMed:30770391};
CC Peripheral membrane protein {ECO:0000255}. Note=Associated with the
CC membrane when activated. The localization to the plasma membrane
CC requires YIP4A and YIP4B (PubMed:30770391). Accumulates in a sterol-
CC enriched, polar membrane domain during root hair initiation
CC (PubMed:27251533). {ECO:0000269|PubMed:27251533,
CC ECO:0000269|PubMed:30770391}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11971133,
CC ECO:0000269|PubMed:9765526}.
CC -!- DEVELOPMENTAL STAGE: In root trichoblasts, accumulates into patches at
CC the basal end of the cell before a hair bulge is visible and remain
CC concentrated at the tip of the bulge and in the growing hair.
CC {ECO:0000269|PubMed:30770391}.
CC -!- DISRUPTION PHENOTYPE: Fewer and shorter root hairs.
CC {ECO:0000269|PubMed:30770391}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; U45236; AAC49854.1; -; mRNA.
DR EMBL; U49972; AAC78391.1; -; Genomic_DNA.
DR EMBL; AF115471; AAF40243.1; -; Genomic_DNA.
DR EMBL; AC022472; AAF79903.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29934.1; -; Genomic_DNA.
DR EMBL; AF332438; AAG48801.1; -; mRNA.
DR EMBL; AF360154; AAK25864.1; -; mRNA.
DR EMBL; AY056308; AAL07157.1; -; mRNA.
DR PIR; T48864; T48864.
DR RefSeq; NP_173437.1; NM_101863.4.
DR AlphaFoldDB; Q38919; -.
DR SMR; Q38919; -.
DR BioGRID; 23837; 9.
DR DIP; DIP-29818N; -.
DR IntAct; Q38919; 5.
DR STRING; 3702.AT1G20090.1; -.
DR PaxDb; Q38919; -.
DR PRIDE; Q38919; -.
DR ProteomicsDB; 236689; -.
DR EnsemblPlants; AT1G20090.1; AT1G20090.1; AT1G20090.
DR GeneID; 838598; -.
DR Gramene; AT1G20090.1; AT1G20090.1; AT1G20090.
DR KEGG; ath:AT1G20090; -.
DR Araport; AT1G20090; -.
DR TAIR; locus:2198566; AT1G20090.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q38919; -.
DR OMA; EKPICME; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q38919; -.
DR PRO; PR:Q38919; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q38919; baseline and differential.
DR Genevisible; Q38919; AT.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:TAIR.
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:0000902; P:cell morphogenesis; IGI: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:0000226; P:microtubule cytoskeleton organization; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; 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:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IDA:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP:UniProtKB.
DR GO; GO:0048766; P:root hair initiation; IMP:UniProtKB.
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 Cell membrane; Cytoplasm; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..192
FT /note="Rac-like GTP-binding protein ARAC4"
FT /id="PRO_0000198918"
FT PROPEP 193..195
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000227583"
FT MOTIF 34..42
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT BINDING 30..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 117..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT MOD_RES 192
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 192
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 195 AA; 21636 MW; 90899399AB7EA658 CRC64;
MASRFIKCVT VGDGAVGKTC MLISYTSNTF PTDYVPTVFD NFSANVVVDG NTVNLGLWDT
AGQEDYNRLR PLSYRGADVF ILAFSLISKA SYENIAKKWI PELRHYAPGV PIILVGTKLD
LRDDKQFFID HPGAVPITTN QGEELKKLIG SAVYIECSSK TQQNVKAVFD AAIKVVLQPP
KQKKKKKNKN RCAFL
