RIC1_ARATH
ID RIC1_ARATH Reviewed; 224 AA.
AC F4IVV0; O22796;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=CRIB domain-containing protein RIC1;
DE AltName: Full=ROP-interactive CRIB motif-containing protein 1;
DE AltName: Full=Target of ROP protein RIC1;
GN Name=RIC1; OrderedLocusNames=At2g33460; ORFNames=F4P9.23;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 FUNCTION, INTERACTION WITH ARAC11/ROP1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND MUTAGENESIS OF HIS-37 AND
RP HIS-40.
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 [4]
RP FUNCTION, INTERACTION WITH ARAC4/ROP2, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=19818614; DOI=10.1016/j.cub.2009.08.052;
RA Fu Y., Xu T., Zhu L., Wen M., Yang Z.;
RT "A ROP GTPase signaling pathway controls cortical microtubule ordering and
RT cell expansion in Arabidopsis.";
RL Curr. Biol. 19:1827-1832(2009).
RN [6]
RP FUNCTION.
RX PubMed=21535258; DOI=10.1111/j.1365-313x.2011.04552.x;
RA Fujita M., Himmelspach R., Hocart C.H., Williamson R.E., Mansfield S.D.,
RA Wasteneys G.O.;
RT "Cortical microtubules optimize cell-wall crystallinity to drive
RT unidirectional growth in Arabidopsis.";
RL Plant J. 66:915-928(2011).
RN [7]
RP FUNCTION.
RX PubMed=22683261; DOI=10.1016/j.cub.2012.05.020;
RA Chen X., Naramoto S., Robert S., Tejos R., Loefke C., Lin D., Yang Z.,
RA Friml J.;
RT "ABP1 and ROP6 GTPase signaling regulate clathrin-mediated endocytosis in
RT Arabidopsis roots.";
RL Curr. Biol. 22:1326-1332(2012).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23078108; DOI=10.1111/pce.12028;
RA Choi Y., Lee Y., Kim S.Y., Lee Y., Hwang J.U.;
RT "Arabidopsis ROP-interactive CRIB motif-containing protein 1 (RIC1)
RT positively regulates auxin signalling and negatively regulates abscisic
RT acid (ABA) signalling during root development.";
RL Plant Cell Environ. 36:945-955(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 cortical microtubule organization. Promotes microtubule
CC bundling and formation of well-ordered microtubule arrays in the neck
CC region of pavement cells. This restricts cell lateral expansion to
CC generate the narrow neck morphology of pavement cells. Its function is
CC inhibited when it interacts with activated ARAC4/ROP2. Represses
CC ARAC4/ROP2 activation and antagonizes the RIC4-actin pathway that
CC promotes the assembly of cortical actin microfilaments. Acts as
CC downstream effector of ARAC3/ROP6 which functions in a signaling
CC pathway that negatively regulates clathrin-mediated endocytosis and
CC internalization of PIN1 and PIN2. Required for the asymmetric auxin
CC distribution during root gravitropism and vascular patterning.
CC Positively regulates auxin responses, but negatively regulates ABA
CC responses during lateral root development and primary root elongation.
CC {ECO:0000269|PubMed:11752391, ECO:0000269|PubMed:15766531,
CC ECO:0000269|PubMed:19818614, ECO:0000269|PubMed:21535258,
CC ECO:0000269|PubMed:22683261, ECO:0000269|PubMed:23078108}.
CC -!- SUBUNIT: Interacts with ARAC11/ROP1. {ECO:0000269|PubMed:11752391,
CC ECO:0000269|PubMed:15766531}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15766531}. Cytoplasm {ECO:0000269|PubMed:11752391,
CC ECO:0000269|PubMed:15766531, ECO:0000269|PubMed:23078108}.
CC Note=Associates with and promotes the organization of cortical
CC microtubules in leaf epidermal pavement cells. Localizes to punctate
CC loci in the cytoplasm of root cells. {ECO:0000269|PubMed:23078108}.
CC -!- TISSUE SPECIFICITY: Expressed in columella cells from the root tip and
CC epidermal cells at the base of lateral roots, leaves, stems, flowers,
CC anthers, pollen and siliques. {ECO:0000269|PubMed:11752391,
CC ECO:0000269|PubMed:23078108}.
CC -!- INDUCTION: By auxin and abscisic acid (ABA) in roots.
CC {ECO:0000269|PubMed:23078108}.
CC -!- DISRUPTION PHENOTYPE: Reduced primary root elongation.
CC {ECO:0000269|PubMed:15766531, ECO:0000269|PubMed:19818614,
CC ECO:0000269|PubMed:23078108}.
CC -!- MISCELLANEOUS: Over-expression of RIC1 in tobacco germinating pollen
CC reduces pollen tube elongation. {ECO:0000305|PubMed:11752391}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB80663.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002332; AAB80663.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08837.1; -; Genomic_DNA.
DR PIR; G84745; G84745.
DR RefSeq; NP_180904.2; NM_128906.3.
DR AlphaFoldDB; F4IVV0; -.
DR BioGRID; 3258; 8.
DR STRING; 3702.AT2G33460.1; -.
DR PaxDb; F4IVV0; -.
DR PRIDE; F4IVV0; -.
DR ProteomicsDB; 236980; -.
DR EnsemblPlants; AT2G33460.1; AT2G33460.1; AT2G33460.
DR GeneID; 817911; -.
DR Gramene; AT2G33460.1; AT2G33460.1; AT2G33460.
DR KEGG; ath:AT2G33460; -.
DR Araport; AT2G33460; -.
DR TAIR; locus:2051033; AT2G33460.
DR eggNOG; ENOG502S3JH; Eukaryota.
DR HOGENOM; CLU_086489_0_1_1; -.
DR InParanoid; F4IVV0; -.
DR OMA; RHNRSAH; -.
DR OrthoDB; 1384435at2759; -.
DR PRO; PR:F4IVV0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IVV0; baseline and differential.
DR Genevisible; F4IVV0; AT.
DR GO; GO:0016324; C:apical plasma membrane; IDA:TAIR.
DR GO; GO:0010005; C:cortical microtubule, transverse to long axis; IDA:TAIR.
DR GO; GO:0000902; P:cell morphogenesis; IMP:TAIR.
DR GO; GO:0010215; P:cellulose microfibril organization; IMP:TAIR.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR044510; RIC1-like.
DR PANTHER; PTHR46325; PTHR46325; 1.
DR Pfam; PF00786; PBD; 1.
DR SMART; SM00285; PBD; 1.
DR PROSITE; PS50108; CRIB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Developmental protein; Growth regulation;
KW Reference proteome.
FT CHAIN 1..224
FT /note="CRIB domain-containing protein RIC1"
FT /id="PRO_0000422724"
FT DOMAIN 29..42
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REGION 38..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 37
FT /note="H->D: Loss of interaction with ARAC11/ROP1."
FT /evidence="ECO:0000269|PubMed:11752391"
FT MUTAGEN 40
FT /note="H->D: Loss of interaction with ARAC11/ROP1; when
FT associated with D37."
FT /evidence="ECO:0000269|PubMed:11752391"
SQ SEQUENCE 224 AA; 24140 MW; 7679F15DA4C3E133 CRC64;
MATTMKGLLK GLRYITQIFD EEKEQEMQIG FPTDVKHVAH IGSDGPTNTT PSWMNDFKTQ
EHEKGQVVSR GNSNKYNPQG TNQRGAGLKE LLPSNTNEKP KQKTRRKPGG AASPNHNGSP
PRKSSGNAAS SDEPSKHSRH NRSAHGSTDS SNDQEPSVRR RRGGIPAPDT EVPNQIPDGS
APPRKATSRP RKLKGSSAGG EGSIKKSSKG KPENSVDTTC NDII
