RIC4_ARATH
ID RIC4_ARATH Reviewed; 153 AA.
AC Q9FFD5;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=CRIB domain-containing protein RIC4;
DE AltName: Full=ROP-interactive CRIB motif-containing protein 4;
DE AltName: Full=Target of ROP protein RIC4;
GN Name=RIC4; OrderedLocusNames=At5g16490; ORFNames=MQK4.23;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH ARAC11/ROP1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11752391; DOI=10.2307/3871538;
RA Wu G., Gu Y., Li S., Yang Z.;
RT "A genome-wide analysis of Arabidopsis Rop-interactive CRIB motif-
RT containing proteins that act as Rop GTPase targets.";
RL Plant Cell 13:2841-2856(2001).
RN [6]
RP FUNCTION, INTERACTION WITH ARAC4/ROP2, AND SUBCELLULAR LOCATION.
RX PubMed=15766531; DOI=10.1016/j.cell.2004.12.026;
RA Fu Y., Gu Y., Zheng Z., Wasteneys G., Yang Z.;
RT "Arabidopsis interdigitating cell growth requires two antagonistic pathways
RT with opposing action on cell morphogenesis.";
RL Cell 120:687-700(2005).
RN [7]
RP FUNCTION, INTERACTION WITH ARAC11/ROP1, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF HIS-107 AND HIS-110.
RX PubMed=15824136; DOI=10.1083/jcb.200409140;
RA Gu Y., Fu Y., Dowd P., Li S., Vernoud V., Gilroy S., Yang Z.;
RT "A Rho family GTPase controls actin dynamics and tip growth via two
RT counteracting downstream pathways in pollen tubes.";
RL J. Cell Biol. 169:127-138(2005).
RN [8]
RP FUNCTION.
RX PubMed=18591430; DOI=10.1083/jcb.200801086;
RA Lee Y.J., Szumlanski A., Nielsen E., Yang Z.;
RT "Rho-GTPase-dependent filamentous actin dynamics coordinate vesicle
RT targeting and exocytosis during tip growth.";
RL J. Cell Biol. 181:1155-1168(2008).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=21124849; DOI=10.1371/journal.pone.0015481;
RA Oikawa A., Joshi H.J., Rennie E.A., Ebert B., Manisseri C.,
RA Heazlewood J.L., Scheller H.V.;
RT "An integrative approach to the identification of Arabidopsis and rice
RT genes involved in xylan and secondary wall development.";
RL PLoS ONE 5:E15481-E15481(2010).
RN [10]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23118477; DOI=10.1093/mp/sss101;
RA Venus Y., Oelmueller R.;
RT "Arabidopsis ROP1 and ROP6 influence germination time, root morphology, the
RT formation of F-actin bundles, and symbiotic fungal interactions.";
RL Mol. Plant 6:872-886(2013).
CC -!- FUNCTION: Functions as downstream effector of Rho-related GTP binding
CC proteins of the 'Rho of Plants' (ROPs) family. Participates in the
CC propagation of ROP GTPase signals in specific cellular responses.
CC Required for actin cortical microfilament assembly. Activated by
CC ARAC4/ROP2 to promote the assembly of cortical actin microfilaments
CC required for lobe formation and lateral expansion of pavement cells.
CC Interaction with, and activation by ARAC4/ROP2 is inhibited by RIC1.
CC Functions as downstream effector of ARAC11/ROP1 to promote the assembly
CC of apical F-actin associated with vesicle accumulation in the tip of
CC the growing pollen tube. Counteracts the ARAC11/ROP1-RIC3 pathway,
CC which activates calcium signaling that leads to apical F-actin
CC disassembly associated with exocytosis, to control actin dynamics and
CC pollen tube apical growth. Downstream of ARAC11/ROP1, is involved in
CC the growth responses to the root-colonizing endophytic fungus P.indica.
CC {ECO:0000269|PubMed:11752391, ECO:0000269|PubMed:15766531,
CC ECO:0000269|PubMed:15824136, ECO:0000269|PubMed:18591430,
CC ECO:0000269|PubMed:23118477}.
CC -!- SUBUNIT: Interacts with ARAC4/ROP2 and ARAC11/ROP1.
CC {ECO:0000269|PubMed:11752391, ECO:0000269|PubMed:15766531,
CC ECO:0000269|PubMed:15824136}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11752391,
CC ECO:0000305|PubMed:15766531, ECO:0000305|PubMed:15824136,
CC ECO:0000305|PubMed:21124849}; Peripheral membrane protein
CC {ECO:0000305|PubMed:11752391, ECO:0000305|PubMed:15766531,
CC ECO:0000305|PubMed:15824136, ECO:0000305|PubMed:21124849}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers,
CC siliques and pollen. {ECO:0000269|PubMed:11752391}.
CC -!- INDUCTION: By the root-colonizing endophytic fungus P.indica.
CC {ECO:0000269|PubMed:23118477}.
CC -!- DISRUPTION PHENOTYPE: Increased rate of seed germination.
CC {ECO:0000269|PubMed:23118477}.
CC -!- MISCELLANEOUS: Over-expression of RIC4 in tobacco germinating pollen
CC induces depolarized pollen tube growth. {ECO:0000305|PubMed:11752391}.
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DR EMBL; AB005242; BAB09617.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92300.1; -; Genomic_DNA.
DR EMBL; BT010523; AAQ65146.1; -; mRNA.
DR EMBL; AK176878; BAD44641.1; -; mRNA.
DR RefSeq; NP_197153.1; NM_121654.3.
DR AlphaFoldDB; Q9FFD5; -.
DR BioGRID; 16786; 2.
DR IntAct; Q9FFD5; 1.
DR STRING; 3702.AT5G16490.1; -.
DR PaxDb; Q9FFD5; -.
DR PRIDE; Q9FFD5; -.
DR EnsemblPlants; AT5G16490.1; AT5G16490.1; AT5G16490.
DR GeneID; 831510; -.
DR Gramene; AT5G16490.1; AT5G16490.1; AT5G16490.
DR KEGG; ath:AT5G16490; -.
DR Araport; AT5G16490; -.
DR TAIR; locus:2171332; AT5G16490.
DR eggNOG; ENOG502S24M; Eukaryota.
DR HOGENOM; CLU_114322_1_0_1; -.
DR InParanoid; Q9FFD5; -.
DR OMA; DPIRGWD; -.
DR OrthoDB; 1602959at2759; -.
DR PhylomeDB; Q9FFD5; -.
DR PRO; PR:Q9FFD5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFD5; baseline and differential.
DR Genevisible; Q9FFD5; AT.
DR GO; GO:0016324; C:apical plasma membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0010215; P:cellulose microfibril organization; IMP:TAIR.
DR GO; GO:0051650; P:establishment of vesicle localization; IDA:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:TAIR.
DR GO; GO:0017157; P:regulation of exocytosis; IDA:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 3.90.810.10; -; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR044509; RIC2/4.
DR PANTHER; PTHR46931; PTHR46931; 1.
DR Pfam; PF00786; PBD; 1.
DR PROSITE; PS50108; CRIB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Growth regulation; Membrane;
KW Reference proteome.
FT CHAIN 1..153
FT /note="CRIB domain-containing protein RIC4"
FT /id="PRO_0000422727"
FT DOMAIN 99..112
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT MUTAGEN 107
FT /note="H->D: Loss of interaction with ARAC11/ROP1; when
FT associated with D110."
FT /evidence="ECO:0000269|PubMed:15824136"
FT MUTAGEN 110
FT /note="H->D: Loss of interaction with ARAC11/ROP1; when
FT associated with D107."
FT /evidence="ECO:0000269|PubMed:15824136"
SQ SEQUENCE 153 AA; 17013 MW; 97A2CC68FD26C81F CRC64;
MRDRMERLVV LPFSIGCISV SSVAVLSPLS KPHHHHSRQV IREQEEEDNM KNVFKFLAVS
KPEISIGINR IFKSFKTISQ LFADKDEEKE EVETSGMEIG VPTNVKHVSH IGWESGLTAA
TGPGKGWEDL IPPELLAAAA SKKEINPHLH PTL
