C3H46_ORYSJ
ID C3H46_ORYSJ Reviewed; 390 AA.
AC Q5Z807; A0A0P0X0K1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Zinc finger CCCH domain-containing protein 46;
DE Short=OsC3H46;
DE AltName: Full=Protein LEAF AND TILLER ANGLE INCREASED CONTROLLER {ECO:0000303|PubMed:18953406};
DE Short=OsLIC {ECO:0000303|PubMed:18953406};
GN Name=LIC {ECO:0000303|PubMed:18953406};
GN OrderedLocusNames=Os06g0704300, LOC_Os06g49080; ORFNames=OJ1215_E11.23;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [5]
RP NOMENCLATURE.
RX PubMed=18221561; DOI=10.1186/1471-2164-9-44;
RA Wang D., Guo Y., Wu C., Yang G., Li Y., Zheng C.;
RT "Genome-wide analysis of CCCH zinc finger family in Arabidopsis and rice.";
RL BMC Genomics 9:44-44(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY
RP 24-EPIBRASSINOLIDE.
RX PubMed=18953406; DOI=10.1371/journal.pone.0003521;
RA Wang L., Xu Y., Zhang C., Ma Q., Joo S.H., Kim S.K., Xu Z., Chong K.;
RT "OsLIC, a novel CCCH-Type zinc finger protein with transcription
RT activation, mediates rice architecture via brassinosteroids signaling.";
RL PLoS ONE 3:E3521-E3521(2008).
RN [7]
RP FUNCTION, INTERACTION WITH GSK1 AND GSK4, SUBCELLULAR LOCATION, INDUCTION
RP BY 24-EPIBRASSINOLIDE, AND PHOSPHORYLATION.
RX PubMed=22570626; DOI=10.1371/journal.pgen.1002686;
RA Zhang C., Xu Y., Guo S., Zhu J., Huan Q., Liu H., Wang L., Luo G., Wang X.,
RA Chong K.;
RT "Dynamics of brassinosteroid response modulated by negative regulator LIC
RT in rice.";
RL PLoS Genet. 8:E1002686-E1002686(2012).
CC -!- FUNCTION: Transcriptional activator that binds double-stranded DNA and
CC the single-stranded RNA polymers poly(rA), poly(rU) and poly(rG), but
CC not poly(rC). Mediates optimal plant architecture through
CC brassinosteroid (BR) signaling. May act as a negative regulator in
CC sterol homeostasis (PubMed:18953406). Acts as negative regulator of BR
CC signaling. Binds to the specific DNA sequence 5'-CTCGC-3' of BZR1
CC promoter and negatively regulates BZR1. Acts as an antagonistic
CC transcription factor of BZR1 to attenuate the BR signaling pathway and
CC regulate leaf bending. Represses the expression of ILI1, and activates
CC that of IBH1 to balance the regulation activity of BZR1
CC (PubMed:22570626). {ECO:0000269|PubMed:18953406,
CC ECO:0000269|PubMed:22570626}.
CC -!- SUBUNIT: Interacts with GSK1 and GSK4. {ECO:0000269|PubMed:22570626}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18953406,
CC ECO:0000269|PubMed:22570626}. Cytoplasm {ECO:0000269|PubMed:18953406,
CC ECO:0000269|PubMed:22570626}. Note=Brassinosteroid promotes nuclear
CC localization. Phosphorylation represses nuclear localization.
CC {ECO:0000269|PubMed:22570626}.
CC -!- TISSUE SPECIFICITY: Expressed in the adaxial face of the collar, nodes
CC and the basal region of elongating internodes.
CC {ECO:0000269|PubMed:18953406}.
CC -!- INDUCTION: Induced by 24-epibrassinolide. {ECO:0000269|PubMed:18953406,
CC ECO:0000269|PubMed:22570626}.
CC -!- PTM: Phosphorylated on serine and threonine residues by GSK1.
CC Phosphorylation represses nuclear localization.
CC {ECO:0000269|PubMed:22570626}.
CC -!- MISCELLANEOUS: Plants silencing LIC are short, have increased leaf and
CC tiller angles, and display both reduced number of rachises and seeds
CC (PubMed:18953406). Plants over-expressing LIC show erect leaves
CC (PubMed:22570626). {ECO:0000269|PubMed:18953406,
CC ECO:0000269|PubMed:22570626}.
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DR EMBL; AP004324; BAD54049.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF20421.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS99381.1; -; Genomic_DNA.
DR EMBL; AK107008; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015641399.1; XM_015785913.1.
DR AlphaFoldDB; Q5Z807; -.
DR SMR; Q5Z807; -.
DR STRING; 4530.OS06T0704300-01; -.
DR PaxDb; Q5Z807; -.
DR PRIDE; Q5Z807; -.
DR EnsemblPlants; Os06t0704300-01; Os06t0704300-01; Os06g0704300.
DR GeneID; 4341994; -.
DR Gramene; Os06t0704300-01; Os06t0704300-01; Os06g0704300.
DR KEGG; osa:4341994; -.
DR eggNOG; ENOG502QVMW; Eukaryota.
DR HOGENOM; CLU_044925_0_0_1; -.
DR InParanoid; Q5Z807; -.
DR OMA; KWSIGEI; -.
DR OrthoDB; 1562631at2759; -.
DR PlantReactome; R-OSA-5632095; Brassinosteroid signaling.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q5Z807; OS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1900458; P:negative regulation of brassinosteroid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR InterPro; IPR045072; MKRN-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR11224; PTHR11224; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Activator; Brassinosteroid signaling pathway; Cytoplasm; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..390
FT /note="Zinc finger CCCH domain-containing protein 46"
FT /id="PRO_0000346840"
FT ZN_FING 2..29
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 27..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..211
FT /note="Required for transcriptional activation activity"
FT /evidence="ECO:0000269|PubMed:18953406"
FT REGION 230..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 298
FT /note="F -> S (in Ref. 4; AK107008)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="D -> V (in Ref. 4; AK107008)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 42663 MW; 806E8A1CD2B35F7D CRC64;
MSRRQEICRN FQRGSCKYGA QCRYLHASPH QQQQQQQAKP NPFGFGTGSR QQQQPSFGSQ
FQQQQQQQQK PNPFGFGVQG ANAQSRNAPG PAKPFQNKWV RDPSAPTKQT EAVQPPQAQA
AHTSCEDPQS CRQQISEDFK NEAPIWKLTC YAHLRNGPCN IKGDISFEEL RAKAYEEGKQ
GHSLQSIVEG ERNLQNAKLM EFTNLLNSAR PSQTPSFPTM SSFPEVKNNS SFGASQTNGP
PVFSSFSQIG AATNIGPGPG TTAPGMPASS PFGHPSSAPL AAPTFGSSQM KFGVSSVFGN
QGSGQPFGSF QAPRFPSSKS PASSVQHRDI DRQSQELLNG MVTPPSVMFE ESVGNNKNEN
QDDSIWLKEK WAIGEIPLDE PPQRHVSHVF
