ROGF8_ARATH
ID ROGF8_ARATH Reviewed; 523 AA.
AC Q9LV40; Q1PEM4;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Rho guanine nucleotide exchange factor 8 {ECO:0000303|PubMed:15980860};
DE Short=AtRopGEF8 {ECO:0000303|PubMed:15980860};
DE AltName: Full=Rho of plants guanine nucleotide exchange factor 8 {ECO:0000303|PubMed:15980860};
GN Name=ROPGEF8 {ECO:0000303|PubMed:15980860};
GN OrderedLocusNames=At3g24620 {ECO:0000312|Araport:AT3G24620};
GN ORFNames=MOB24.21 {ECO:0000312|EMBL:BAB02015.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP GENE FAMILY.
RX PubMed=15980860; DOI=10.1038/nature03883;
RA Berken A., Thomas C., Wittinghofer A.;
RT "A new family of RhoGEFs activates the Rop molecular switch in plants.";
RL Nature 436:1176-1180(2005).
RN [5]
RP INTERACTION WITH ARAC11/ROP1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16415208; DOI=10.1105/tpc.105.036434;
RA Gu Y., Li S., Lord E.M., Yang Z.;
RT "Members of a novel class of Arabidopsis Rho guanine nucleotide exchange
RT factors control Rho GTPase-dependent polar growth.";
RL Plant Cell 18:366-381(2006).
RN [6]
RP INTERACTION WITH ARAC10/ROP11, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22500990; DOI=10.1016/j.febslet.2012.03.040;
RA Li Z., Liu D.;
RT "ROPGEF1 and ROPGEF4 are functional regulators of ROP11 GTPase in ABA-
RT mediated stomatal closure in Arabidopsis.";
RL FEBS Lett. 586:1253-1258(2012).
RN [7]
RP INTERACTION WITH PRK6.
RX PubMed=26961657; DOI=10.1038/nature17413;
RA Takeuchi H., Higashiyama T.;
RT "Tip-localized receptors control pollen tube growth and LURE sensing in
RT Arabidopsis.";
RL Nature 531:245-248(2016).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 76-440, FUNCTION, SUBUNIT,
RP INTERACTION WITH ARAC5/ROP4, AND MUTAGENESIS OF LEU-98; PHE-161; GLU-175;
RP TRP-234; TRP-235 AND GLU-413.
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 76-440, SUBUNIT, AND INTERACTION
RP WITH ARAC5/ROP4.
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: Guanine-nucleotide exchange factor (GEF) that acts as an
CC activator of Rop (Rho of plants) GTPases by promoting the exchange of
CC GDP for GTP. Active as homodimer. {ECO:0000269|PubMed:17218277}.
CC -!- SUBUNIT: Homodimer. The homodimer interacts with ARAC5/ROP4. Interacts
CC with ARAC11/ROP1 and ARAC10/ROP11. Interacts with PRK6
CC (PubMed:26961657). {ECO:0000269|PubMed:16415208,
CC ECO:0000269|PubMed:17218277, ECO:0000269|PubMed:19335195,
CC ECO:0000269|PubMed:22500990, ECO:0000269|PubMed:26961657}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16415208,
CC ECO:0000269|PubMed:22500990}. Note=Localizes to the apical region of
CC the pollen tube plasma membrane.
CC -!- TISSUE SPECIFICITY: Expressed in pollen grains and pollen tubes.
CC {ECO:0000269|PubMed:16415208, ECO:0000269|PubMed:22500990}.
CC -!- DOMAIN: The PRONE (plant-specific Rop nucleotide exchanger) domain is
CC responsible for the GEF activity.
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DR EMBL; AB020746; BAB02015.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76930.1; -; Genomic_DNA.
DR EMBL; DQ446693; ABE65963.1; -; mRNA.
DR RefSeq; NP_189105.1; NM_113373.2.
DR PDB; 2NTX; X-ray; 2.20 A; A/B=76-440.
DR PDB; 2NTY; X-ray; 3.10 A; A/B=76-440.
DR PDB; 2WBL; X-ray; 2.90 A; A/B=76-440.
DR PDBsum; 2NTX; -.
DR PDBsum; 2NTY; -.
DR PDBsum; 2WBL; -.
DR AlphaFoldDB; Q9LV40; -.
DR SMR; Q9LV40; -.
DR BioGRID; 7389; 3.
DR IntAct; Q9LV40; 2.
DR MINT; Q9LV40; -.
DR STRING; 3702.AT3G24620.1; -.
DR iPTMnet; Q9LV40; -.
DR PaxDb; Q9LV40; -.
DR PRIDE; Q9LV40; -.
DR ProteomicsDB; 227962; -.
DR EnsemblPlants; AT3G24620.1; AT3G24620.1; AT3G24620.
DR GeneID; 822058; -.
DR Gramene; AT3G24620.1; AT3G24620.1; AT3G24620.
DR KEGG; ath:AT3G24620; -.
DR Araport; AT3G24620; -.
DR TAIR; locus:2091742; AT3G24620.
DR eggNOG; ENOG502QSGR; Eukaryota.
DR HOGENOM; CLU_019073_1_0_1; -.
DR InParanoid; Q9LV40; -.
DR OMA; PMAADQK; -.
DR OrthoDB; 482824at2759; -.
DR PhylomeDB; Q9LV40; -.
DR EvolutionaryTrace; Q9LV40; -.
DR PRO; PR:Q9LV40; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LV40; baseline and differential.
DR Genevisible; Q9LV40; AT.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR InterPro; IPR005512; PRONE_dom.
DR InterPro; IPR038937; RopGEF.
DR PANTHER; PTHR33101; PTHR33101; 1.
DR Pfam; PF03759; PRONE; 1.
DR PROSITE; PS51334; PRONE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Guanine-nucleotide releasing factor; Membrane;
KW Reference proteome.
FT CHAIN 1..523
FT /note="Rho guanine nucleotide exchange factor 8"
FT /id="PRO_0000406608"
FT DOMAIN 76..440
FT /note="PRONE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00663"
FT REGION 44..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 98
FT /note="L->D: Loss of homodimerization and GEF activity."
FT /evidence="ECO:0000269|PubMed:17218277"
FT MUTAGEN 161
FT /note="F->A: Decreases GEF activity 25-fold; when
FT associated with A-175."
FT /evidence="ECO:0000269|PubMed:17218277"
FT MUTAGEN 175
FT /note="E->A: Decreases GEF activity 25-fold; when
FT associated with A-161."
FT /evidence="ECO:0000269|PubMed:17218277"
FT MUTAGEN 234
FT /note="W->S: Decreases GEF activity 14-fold."
FT /evidence="ECO:0000269|PubMed:17218277"
FT MUTAGEN 235
FT /note="W->S: Loss of GEF activity."
FT /evidence="ECO:0000269|PubMed:17218277"
FT MUTAGEN 413
FT /note="E->A: Decreases GEF activity 20-fold."
FT /evidence="ECO:0000269|PubMed:17218277"
FT CONFLICT 278
FT /note="E -> EK (in Ref. 3; ABE65963)"
FT /evidence="ECO:0000305"
FT HELIX 80..97
FT /evidence="ECO:0007829|PDB:2NTX"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:2NTX"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2WBL"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:2NTX"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2WBL"
FT HELIX 138..152
FT /evidence="ECO:0007829|PDB:2NTX"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:2NTX"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:2NTX"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:2NTX"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:2NTX"
FT HELIX 188..204
FT /evidence="ECO:0007829|PDB:2NTX"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:2NTX"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:2WBL"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:2NTY"
FT HELIX 248..277
FT /evidence="ECO:0007829|PDB:2NTX"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:2NTX"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:2NTX"
FT HELIX 299..305
FT /evidence="ECO:0007829|PDB:2NTX"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:2WBL"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:2NTX"
FT HELIX 324..343
FT /evidence="ECO:0007829|PDB:2NTX"
FT HELIX 360..380
FT /evidence="ECO:0007829|PDB:2NTX"
FT HELIX 388..396
FT /evidence="ECO:0007829|PDB:2NTX"
FT HELIX 400..436
FT /evidence="ECO:0007829|PDB:2NTX"
SQ SEQUENCE 523 AA; 58741 MW; F84808EC9F70811F CRC64;
MVAALERGLS ASKSFNFKRM FDSSSTKQQQ SQTIVVENGD SHIVESNTPE SQNSDSFVES
PVESSLPMIS PLTRPGKRSE RQQADMEMMK DRFAKLLLGE DMSGGGKGVS SALALSNAIT
NLAASIFGEQ TKLQPMPQDR QARWKKEIDW LLSVTDHIVE FVPSQQTSKD GVCTEIMVTR
QRGDLLMNIP ALRKLDAMLI DTLDNFRGHN EFWYVSRDSE EGQQARNDRT NDKWWLPPVK
VPPGGLSEPS RRMLYFQKDS VTQVQKAAMA INAQVLSEME IPESYIDSLP KNGRASLGDS
IYKSITEEWF DPEQFLAMLD MSTEHKVLDL KNRIEASVVI WKRKLHTKDT KSSWGSAVSL
EKRELFEERA ETILVLLKQK FPGLPQSSLD ISKIQFNKDV GQAVLESYSR ILESLAYTVM
SRIEDVLYTD TLALKQTLLA EETSDGGRTT ETDSESAGSS NSGEEAEKHD PHSKTLLDFM
GWNDNSSKGG DKPTKSPNLT PKKLSYLEKL ENLNGFRSPK DRH
