RAC5_ARATH
ID RAC5_ARATH Reviewed; 196 AA.
AC Q38937; O48545; Q9LQT0; Q9ZRD5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Rac-like GTP-binding protein ARAC5 {ECO:0000303|PubMed:9349271};
DE Short=AtRAC5 {ECO:0000303|PubMed:11102387};
DE AltName: Full=GTPase protein ROP4 {ECO:0000303|PubMed:10798620};
DE Flags: Precursor;
GN Name=ARAC5 {ECO:0000303|PubMed:9349271};
GN Synonyms=ATGP3 {ECO:0000303|PubMed:8843944},
GN ROP4 {ECO:0000303|PubMed:10798620};
GN OrderedLocusNames=At1g75840 {ECO:0000312|Araport:AT1G75840};
GN ORFNames=T4O12.8 {ECO:0000312|EMBL:AAF26755.1};
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].
RX PubMed=8843944; DOI=10.1007/bf00040720;
RA Biermann B.J., Randall S.K., Crowell D.N.;
RT "Identification and isoprenylation of plant GTP-binding proteins.";
RL Plant Mol. Biol. 31:1021-1028(1996).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA], 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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RHO GDI-1.
RX PubMed=10798620; DOI=10.1023/a:1006341210147;
RA Bischoff F., Vahlkamp L., Molendijk A.J., Palme K.;
RT "Localization of AtROP4 and AtROP6 and interaction with the guanine
RT nucleotide dissociation inhibitor AtRhoGDI1 from Arabidopsis.";
RL Plant Mol. Biol. 42:515-530(2000).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11387211; DOI=10.1093/emboj/20.11.2779;
RA Molendijk A.J., Bischoff F., Rajendrakumar C.S.V., Friml J., Braun M.,
RA Gilroy S., Palme K.;
RT "Arabidopsis thaliana Rop GTPases are localized to tips of root hairs and
RT control polar growth.";
RL EMBO J. 20:2779-2788(2001).
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 FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-180 IN COMPLEX WITH GDP,
RP INTERACTION WITH ROPGEF8, AND MUTAGENESIS OF GLU-65.
RX PubMed=17218277; DOI=10.1016/j.molcel.2006.11.023;
RA Thomas C., Fricke I., Scrima A., Berken A., Wittinghofer A.;
RT "Structural evidence for a common intermediate in small G protein-GEF
RT reactions.";
RL Mol. Cell 25:141-149(2007).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 76-440, AND INTERACTION WITH
RP ROPGEF8.
RX PubMed=19335195; DOI=10.1515/bc.2009.049;
RA Thomas C., Fricke I., Weyand M., Berken A.;
RT "3D structure of a binary ROP-PRONE complex: the final intermediate for a
RT complete set of molecular snapshots of the RopGEF reaction.";
RL Biol. Chem. 390:427-435(2009).
CC -!- FUNCTION: Involved in cell polarity control during the actin-dependent
CC tip growth of root hairs, thus regulating root hair length and root
CC hair initiation. {ECO:0000269|PubMed:11387211,
CC ECO:0000269|PubMed:30770391}.
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:0000269|PubMed:11387211}.
CC -!- SUBUNIT: Interacts with GDI1 and ROPGEF8 homodimer (PubMed:10798620,
CC PubMed:17218277, PubMed:19335195). Binds to SPK1 (PubMed:18308939).
CC {ECO:0000269|PubMed:10798620, ECO:0000269|PubMed:17218277,
CC ECO:0000269|PubMed:18308939, ECO:0000269|PubMed:19335195}.
CC -!- INTERACTION:
CC Q38937; Q9SFC6: GDI1; NbExp=2; IntAct=EBI-1751308, EBI-1751328;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10798620}. Membrane
CC {ECO:0000269|PubMed:10798620}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10798620}. Cell membrane
CC {ECO:0000250|UniProtKB:Q38919}; Peripheral membrane protein
CC {ECO:0000255}. Note=Associated with the membrane when activated. The
CC localization to the plasma membrane requires YIP4A and YIP4B (By
CC similarity). {ECO:0000250|UniProtKB:Q38919}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Preferentially expressed at the tip of
CC root hairs. {ECO:0000269|PubMed:11387211, 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26755.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U64920; AAD00114.1; -; mRNA.
DR EMBL; U52350; AAC49855.1; -; mRNA.
DR EMBL; AF031428; AAC78242.1; -; mRNA.
DR EMBL; AF115472; AAF40244.1; -; Genomic_DNA.
DR EMBL; AC007396; AAF26755.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35764.1; -; Genomic_DNA.
DR EMBL; AY062800; AAL32878.1; -; mRNA.
DR EMBL; AY081600; AAM10162.1; -; mRNA.
DR PIR; T48865; T48865.
DR RefSeq; NP_177712.1; NM_106234.3.
DR PDB; 2NTY; X-ray; 3.10 A; C/D=1-180.
DR PDBsum; 2NTY; -.
DR AlphaFoldDB; Q38937; -.
DR SMR; Q38937; -.
DR BioGRID; 29136; 9.
DR DIP; DIP-29820N; -.
DR IntAct; Q38937; 3.
DR STRING; 3702.AT1G75840.1; -.
DR PaxDb; Q38937; -.
DR PRIDE; Q38937; -.
DR ProteomicsDB; 236300; -.
DR EnsemblPlants; AT1G75840.1; AT1G75840.1; AT1G75840.
DR GeneID; 843917; -.
DR Gramene; AT1G75840.1; AT1G75840.1; AT1G75840.
DR KEGG; ath:AT1G75840; -.
DR Araport; AT1G75840; -.
DR TAIR; locus:2204380; AT1G75840.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q38937; -.
DR OMA; EINAVKF; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q38937; -.
DR EvolutionaryTrace; Q38937; -.
DR PRO; PR:Q38937; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q38937; baseline and differential.
DR Genevisible; Q38937; 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; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:TAIR.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
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: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: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 3D-structure; Cell membrane; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..193
FT /note="Rac-like GTP-binding protein ARAC5"
FT /id="PRO_0000198919"
FT PROPEP 194..196
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000227584"
FT MOTIF 35..43
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 16..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 119..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 159..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 193
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 193
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
FT MUTAGEN 65
FT /note="E->A: Strongly impairs GEF-dependent nucleotide
FT exchange."
FT /evidence="ECO:0000269|PubMed:17218277"
FT CONFLICT 22
FT /note="M -> I (in Ref. 3; AAC78242)"
FT /evidence="ECO:0000305"
FT CONFLICT 88..89
FT /note="IS -> YC (in Ref. 1; AAD00114)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="N -> H (in Ref. 3; AAC78242)"
FT /evidence="ECO:0000305"
FT CONFLICT 189..195
FT /note="NKNRCVF -> TKAQKACSI (in Ref. 1; AAD00114)"
FT /evidence="ECO:0000305"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:2NTY"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:2NTY"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:2NTY"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:2NTY"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:2NTY"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:2NTY"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:2NTY"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:2NTY"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:2NTY"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2NTY"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:2NTY"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:2NTY"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2NTY"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:2NTY"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:2NTY"
SQ SEQUENCE 196 AA; 21777 MW; 631317F3DA441A35 CRC64;
MSASRFIKCV TVGDGAVGKT CMLISYTSNT FPTDYVPTVF DNFSANVVVD GNTVNLGLWD
TAGQEDYNRL RPLSYRGADV FILAFSLISK ASYENVAKKW IPELRHYAPG VPIILVGTKL
DLRDDKQFFI DHPGAVPITT NQGEELKKLI GSPIYIECSS KTQQNVKAVF DAAIKVVLQP
PKQKKKKKNK NRCVFL
