RIC7_ARATH
ID RIC7_ARATH Reviewed; 216 AA.
AC Q1G3K8;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=CRIB domain-containing protein RIC7;
DE AltName: Full=ROP-interactive CRIB motif-containing protein 7;
DE AltName: Full=Target of ROP protein RIC7;
GN Name=RIC7; OrderedLocusNames=At4g28556; ORFNames=F20O9;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 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 [5]
RP FUNCTION, INTERACTION WITH ARAC4/ROP2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18178769; DOI=10.1105/tpc.107.054544;
RA Jeon B.W., Hwang J.U., Hwang Y., Song W.Y., Fu Y., Gu Y., Bao F., Cho D.,
RA Kwak J.M., Yang Z., Lee Y.;
RT "The Arabidopsis small G protein ROP2 is activated by light in guard cells
RT and inhibits light-induced stomatal opening.";
RL Plant Cell 20:75-87(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 active ARAC4/ROP2 GTPase which is
CC involved in the prevention of excessive stomatal opening upon light
CC stimulation. Is involved in pollen tube growth regulation through its
CC interaction with ARAC11/ROP1. {ECO:0000269|PubMed:11752391,
CC ECO:0000269|PubMed:18178769}.
CC -!- SUBUNIT: Interacts with ARAC4/ROP2 and ARAC11/ROP1.
CC {ECO:0000269|PubMed:11752391, ECO:0000269|PubMed:18178769}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18178769}. Cytoplasm
CC {ECO:0000269|PubMed:11752391, ECO:0000269|PubMed:18178769}. Cell
CC membrane {ECO:0000269|PubMed:11752391, ECO:0000269|PubMed:18178769};
CC Peripheral membrane protein {ECO:0000305}. Note=In guard cells in the
CC dark localizes predominantly in the nucleus, but upon light
CC irradiation, it is found at the plasma membrane and in the cytoplasm.
CC {ECO:0000269|PubMed:18178769}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, guard cells, stems,
CC flowers, siliques and pollen. {ECO:0000269|PubMed:11752391,
CC ECO:0000269|PubMed:18178769}.
CC -!- MISCELLANEOUS: Over-expression of RIC7 in tobacco germinating pollen
CC reduces pollen tube elongation. {ECO:0000305|PubMed:11752391}.
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DR EMBL; AL021749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE85505.1; -; Genomic_DNA.
DR EMBL; DQ487576; ABF59238.1; -; mRNA.
DR RefSeq; NP_001031740.1; NM_001036663.2.
DR AlphaFoldDB; Q1G3K8; -.
DR PaxDb; Q1G3K8; -.
DR PRIDE; Q1G3K8; -.
DR ProteomicsDB; 236985; -.
DR EnsemblPlants; AT4G28556.1; AT4G28556.1; AT4G28556.
DR GeneID; 3770548; -.
DR Gramene; AT4G28556.1; AT4G28556.1; AT4G28556.
DR KEGG; ath:AT4G28556; -.
DR Araport; AT4G28556; -.
DR TAIR; locus:1009023333; AT4G28556.
DR eggNOG; ENOG502S2ZY; Eukaryota.
DR HOGENOM; CLU_086489_2_0_1; -.
DR OrthoDB; 1384435at2759; -.
DR PhylomeDB; Q1G3K8; -.
DR PRO; PR:Q1G3K8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q1G3K8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0009416; P:response to light stimulus; IDA:TAIR.
DR Gene3D; 3.90.810.10; -; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
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 Cell membrane; Cytoplasm; Growth regulation; Membrane; Nucleus;
KW Reference proteome.
FT CHAIN 1..216
FT /note="CRIB domain-containing protein RIC7"
FT /id="PRO_0000422730"
FT DOMAIN 36..49
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT REGION 52..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 216 AA; 23754 MW; 73293B11CA48BA5F CRC64;
MQLGMSSTKM KSLLKGLRYI SQVFAIEGEK EEEMQIGNPT DVKHVAHIGW DGPSDNATAP
SWMNDFKSSP VMESIQGLGE DDSSVKCQSE FGGRTRDLPK LPKSTRKSSS EKGSPTKERS
DKTKRRTSNK GTSSSRRTKD EDSTSSSRRT TKDEDSSLSQ HSAGLPEVPK KSKRKKSKEA
GNGGSSRSSR ISEADYMSDT GSDRSMPQFE DDRNGF
