RIC3_ARATH
ID RIC3_ARATH Reviewed; 220 AA.
AC F4I5N6; P93814;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=CRIB domain-containing protein RIC3;
DE AltName: Full=ROP-interactive CRIB motif-containing protein 3;
DE AltName: Full=Target of ROP protein RIC3;
GN Name=RIC3; OrderedLocusNames=At1g04450; ORFNames=F19P19.8;
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=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 [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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GENE FAMILY, AND
RP 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 [4]
RP FUNCTION, INTERACTION WITH ARAC11/ROP1, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF HIS-36 AND HIS-39.
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 [5]
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).
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 Functions as downstream effector of ARAC11/ROP1 to activate calcium
CC signaling that leads to F-actin disassembly associated with exocytosis
CC in the tip of the growing pollen tube. Counteracts the ARAC11/ROP1-RIC4
CC pathway, which promotes apical F-actin assembly associated with vesicle
CC accumulation, to control actin dynamics and pollen tube apical growth.
CC {ECO:0000269|PubMed:11752391, ECO:0000269|PubMed:15824136,
CC ECO:0000269|PubMed:18591430}.
CC -!- SUBUNIT: Interacts with ARAC11/ROP1. {ECO:0000269|PubMed:15824136}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11752391,
CC ECO:0000269|PubMed:15824136}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and pollen.
CC {ECO:0000269|PubMed:11752391}.
CC -!- MISCELLANEOUS: Over-expression of RIC3 in tobacco germinating pollen
CC induces depolarized pollen tube growth. {ECO:0000305|PubMed:11752391}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70429.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC000104; AAB70429.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27700.1; -; Genomic_DNA.
DR PIR; G86176; G86176.
DR RefSeq; NP_171940.1; NM_100325.4.
DR AlphaFoldDB; F4I5N6; -.
DR BioGRID; 24748; 1.
DR STRING; 3702.AT1G04450.1; -.
DR iPTMnet; F4I5N6; -.
DR PaxDb; F4I5N6; -.
DR PRIDE; F4I5N6; -.
DR ProteomicsDB; 236253; -.
DR EnsemblPlants; AT1G04450.1; AT1G04450.1; AT1G04450.
DR GeneID; 839513; -.
DR Gramene; AT1G04450.1; AT1G04450.1; AT1G04450.
DR KEGG; ath:AT1G04450; -.
DR Araport; AT1G04450; -.
DR TAIR; locus:2018369; AT1G04450.
DR eggNOG; ENOG502SSMW; Eukaryota.
DR HOGENOM; CLU_086489_0_1_1; -.
DR InParanoid; F4I5N6; -.
DR OMA; ASDMQPK; -.
DR OrthoDB; 1384435at2759; -.
DR PRO; PR:F4I5N6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I5N6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA: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:0050850; P:positive regulation of calcium-mediated signaling; IMP:TAIR.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:TAIR.
DR GO; GO:0030834; P:regulation of actin filament depolymerization; IMP:TAIR.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; IMP:TAIR.
DR GO; GO:0017157; P:regulation of exocytosis; IDA: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 PROSITE; PS50108; CRIB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Growth regulation; Reference proteome.
FT CHAIN 1..220
FT /note="CRIB domain-containing protein RIC3"
FT /id="PRO_0000422726"
FT DOMAIN 28..41
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REGION 39..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 36
FT /note="H->D: Loss of interaction with ARAC11/ROP1; when
FT associated with D39."
FT /evidence="ECO:0000269|PubMed:15824136"
FT MUTAGEN 39
FT /note="H->D: Loss of interaction with ARAC11/ROP1; when
FT associated with D36."
FT /evidence="ECO:0000269|PubMed:15824136"
SQ SEQUENCE 220 AA; 24256 MW; A15369C2ECFFDCA2 CRC64;
MATVKGLLKG LRYITQIFDE EKDKDMQIGF PTDVKHVAHI GSDGPATNVP SWMGDFKPQE
NENGQVVSRA DANNNQIGEG VGLQELLPPT DKPKHKKTRR KSETVSQNGS PPRRNSSASA
SDMQPKNTRR HHRSRHGSID SSNDPSVRRR RVVSVTTNDM EGSYPLSDSS THSRKSTSRH
RKPKGSGGGE LSMKKTKGKT ENPIVESVDT CNDNNISDKE
