ICE1_ARATH
ID ICE1_ARATH Reviewed; 494 AA.
AC Q9LSE2; Q0WR77; Q2V3S3; Q5PNR8;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Transcription factor ICE1;
DE AltName: Full=Basic helix-loop-helix protein 116;
DE Short=AtbHLH116;
DE Short=bHLH 116;
DE AltName: Full=Inducer of CBF expression 1;
DE AltName: Full=Transcription factor EN 45;
DE AltName: Full=Transcription factor SCREAM;
DE AltName: Full=bHLH transcription factor bHLH116;
GN Name=SCRM; Synonyms=BHLH116, EN45, ICE1; OrderedLocusNames=At3g26744;
GN ORFNames=MDJ14.1, MLJ15.14;
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 [MRNA] (ISOFORM 1), CHARACTERIZATION, AND MUTAGENESIS
RP OF ARG-236.
RX PubMed=12672693; DOI=10.1101/gad.1077503;
RA Chinnusamy V., Ohta M., Kanrar S., Lee B.-H., Hong X., Agarwal M.,
RA Zhu J.-K.;
RT "ICE1: a regulator of cold-induced transcriptome and freezing tolerance in
RT Arabidopsis.";
RL Genes Dev. 17:1043-1054(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF ARG-236
RP AND GLU-312, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH
RP SPCH; MUTE AND FAMA, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18641265; DOI=10.1105/tpc.108.060848;
RA Kanaoka M.M., Pillitteri L.J., Fujii H., Yoshida Y., Bogenschutz N.L.,
RA Takabayashi J., Zhu J.-K., Torii K.U.;
RT "SCREAM/ICE1 and SCREAM2 specify three cell-state transitional steps
RT leading to arabidopsis stomatal differentiation.";
RL Plant Cell 20:1775-1785(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12679534; DOI=10.1093/molbev/msg088;
RA Heim M.A., Jakoby M., Werber M., Martin C., Weisshaar B., Bailey P.C.;
RT "The basic helix-loop-helix transcription factor family in plants: a
RT genome-wide study of protein structure and functional diversity.";
RL Mol. Biol. Evol. 20:735-747(2003).
RN [9]
RP GENE FAMILY.
RX PubMed=12897250; DOI=10.1105/tpc.013839;
RA Toledo-Ortiz G., Huq E., Quail P.H.;
RT "The Arabidopsis basic/helix-loop-helix transcription factor family.";
RL Plant Cell 15:1749-1770(2003).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14600211; DOI=10.1105/tpc.151140;
RA Bailey P.C., Martin C., Toledo-Ortiz G., Quail P.H., Huq E., Heim M.A.,
RA Jakoby M., Werber M., Weisshaar B.;
RT "Update on the basic helix-loop-helix transcription factor gene family in
RT Arabidopsis thaliana.";
RL Plant Cell 15:2497-2502(2003).
RN [11]
RP UBIQUITINATION, AND INTERACTION WITH HOS1.
RX PubMed=16702557; DOI=10.1073/pnas.0602874103;
RA Dong C.H., Agarwal M., Zhang Y., Xie Q., Zhu J.K.;
RT "The negative regulator of plant cold responses, HOS1, is a RING E3 ligase
RT that mediates the ubiquitination and degradation of ICE1.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8281-8286(2006).
RN [12]
RP FUNCTION, SUMOYLATION AT LYS-393, AND MUTAGENESIS OF LYS-393.
RX PubMed=17416732; DOI=10.1105/tpc.106.048397;
RA Miura K., Jin J.B., Lee J., Yoo C.Y., Stirm V., Miura T., Ashworth E.N.,
RA Bressan R.A., Yun D.J., Hasegawa P.M.;
RT "SIZ1-mediated sumoylation of ICE1 controls CBF3/DREB1A expression and
RT freezing tolerance in Arabidopsis.";
RL Plant Cell 19:1403-1414(2007).
RN [13]
RP INTERACTION WITH HOS1.
RX PubMed=22960247; DOI=10.1093/pcp/pcs123;
RA Lee J.H., Kim J.J., Kim S.H., Cho H.J., Kim J., Ahn J.H.;
RT "The E3 ubiquitin ligase HOS1 regulates low ambient temperature-responsive
RT flowering in Arabidopsis thaliana.";
RL Plant Cell Physiol. 53:1802-1814(2012).
RN [14]
RP FUNCTION, AND INTERACTION WITH SPCH.
RC STRAIN=cv. Columbia;
RX PubMed=28507175; DOI=10.1104/pp.17.00615;
RA de Marcos A., Houbaert A., Trivino M., Delgado D., Martin-Trillo M.,
RA Russinova E., Fenoll C., Mena M.;
RT "A mutation in the bHLH domain of the SPCH transcription factor uncovers a
RT BR-dependent mechanism for stomatal development.";
RL Plant Physiol. 174:823-842(2017).
CC -!- FUNCTION: Transcriptional activator that regulates the cold-induced
CC transcription of CBF/DREB1 genes. Binds specifically to the MYC
CC recognition sites (5'-CANNTG-3') found in the CBF3/DREB1A promoter.
CC Mediates stomatal differentiation in the epidermis probably by
CC controlling successive roles of SPCH, MUTE, and FAMA. Functions as a
CC dimer with SPCH during stomatal initiation (PubMed:18641265,
CC PubMed:28507175). {ECO:0000269|PubMed:17416732,
CC ECO:0000269|PubMed:18641265, ECO:0000269|PubMed:28507175}.
CC -!- SUBUNIT: Homodimer (Probable). Efficient DNA binding requires
CC dimerization with another bHLH protein (By similarity). Interacts with
CC the C-terminal part of HOS1 (PubMed:18641265). Heterodimers with SPCH,
CC MUTE, and FAMA (PubMed:18641265, PubMed:28507175). {ECO:0000250,
CC ECO:0000269|PubMed:16702557, ECO:0000269|PubMed:18641265,
CC ECO:0000269|PubMed:22960247, ECO:0000269|PubMed:28507175, ECO:0000305}.
CC -!- INTERACTION:
CC Q9LSE2; Q84JU6: HOS1; NbExp=3; IntAct=EBI-15583266, EBI-15583242;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:18641265}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LSE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LSE2-2; Sequence=VSP_020190, VSP_020191;
CC -!- TISSUE SPECIFICITY: Widely expressed in the whole plant with high
CC expression in leaves and stem. Broad expression within stomatal cell
CC lineages of leaf epidermis. {ECO:0000269|PubMed:18641265}.
CC -!- INDUCTION: By high-salt stress, cold stress and abscisic acid (ABA)
CC treatment.
CC -!- PTM: Ubiquitinated. Cold-treatment induced association with the E3
CC ubiquitin ligase HOS1 targets the protein for proteolysis by the
CC ubiquitin-dependent proteasome pathway. Sumoylated at Lys-393 by SIZ1.
CC Sumoylated ICE1 represses HOS1 and MYB15 and facilitates the positive
CC regulation of CBF3/DREB1A-dependent cold signaling and freezing
CC tolerance. {ECO:0000269|PubMed:16702557, ECO:0000269|PubMed:17416732}.
CC -!- DISRUPTION PHENOTYPE: The ice1-2 scrm2-1 double mutant lacks stomata so
CC that the epidermis only contains pavement cells.
CC {ECO:0000269|PubMed:18641265}.
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DR EMBL; AY195621; AAP14668.1; -; mRNA.
DR EMBL; AB026648; BAB01738.1; -; Genomic_DNA.
DR EMBL; AB016889; BAB01738.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE77208.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77209.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77210.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65181.1; -; Genomic_DNA.
DR EMBL; AY079016; AAL84972.1; -; mRNA.
DR EMBL; BT020379; AAV85734.1; -; mRNA.
DR EMBL; AK228443; BAF00372.1; -; mRNA.
DR RefSeq; NP_001030774.1; NM_001035697.2. [Q9LSE2-1]
DR RefSeq; NP_001030776.2; NM_001035699.2. [Q9LSE2-1]
DR RefSeq; NP_001327170.1; NM_001338833.1. [Q9LSE2-2]
DR RefSeq; NP_189309.2; NM_113586.4. [Q9LSE2-1]
DR AlphaFoldDB; Q9LSE2; -.
DR SMR; Q9LSE2; -.
DR BioGRID; 7617; 22.
DR DIP; DIP-61175N; -.
DR IntAct; Q9LSE2; 2.
DR STRING; 3702.AT3G26744.1; -.
DR PaxDb; Q9LSE2; -.
DR PRIDE; Q9LSE2; -.
DR ProteomicsDB; 228759; -. [Q9LSE2-1]
DR EnsemblPlants; AT3G26744.1; AT3G26744.1; AT3G26744. [Q9LSE2-1]
DR EnsemblPlants; AT3G26744.2; AT3G26744.2; AT3G26744. [Q9LSE2-1]
DR EnsemblPlants; AT3G26744.4; AT3G26744.4; AT3G26744. [Q9LSE2-1]
DR EnsemblPlants; AT3G26744.5; AT3G26744.5; AT3G26744. [Q9LSE2-2]
DR GeneID; 822287; -.
DR Gramene; AT3G26744.1; AT3G26744.1; AT3G26744. [Q9LSE2-1]
DR Gramene; AT3G26744.2; AT3G26744.2; AT3G26744. [Q9LSE2-1]
DR Gramene; AT3G26744.4; AT3G26744.4; AT3G26744. [Q9LSE2-1]
DR Gramene; AT3G26744.5; AT3G26744.5; AT3G26744. [Q9LSE2-2]
DR KEGG; ath:AT3G26744; -.
DR Araport; AT3G26744; -.
DR TAIR; locus:2090847; AT3G26744.
DR eggNOG; ENOG502QQ2A; Eukaryota.
DR HOGENOM; CLU_035660_5_0_1; -.
DR InParanoid; Q9LSE2; -.
DR PhylomeDB; Q9LSE2; -.
DR PRO; PR:Q9LSE2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSE2; baseline and differential.
DR Genevisible; Q9LSE2; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IPI:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0009960; P:endosperm development; IGI:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0010115; P:regulation of abscisic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0050826; P:response to freezing; IMP:TAIR.
DR GO; GO:0010162; P:seed dormancy process; IMP:TAIR.
DR GO; GO:0048317; P:seed morphogenesis; IMP:TAIR.
DR GO; GO:0010440; P:stomatal lineage progression; IMP:TAIR.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Developmental protein;
KW DNA-binding; Isopeptide bond; Nucleus; Reference proteome; Stress response;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..494
FT /note="Transcription factor ICE1"
FT /id="PRO_0000127235"
FT DOMAIN 303..352
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 344..365
FT /evidence="ECO:0000255"
FT COMPBIAS 30..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 393
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT VAR_SEQ 336..363
FT /note="MDRASILGDAIDYLKELLQRINDLHNEL -> VNTYFVSFISLRACLLVAVI
FT ENCCVVAL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_020190"
FT VAR_SEQ 364..494
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_020191"
FT MUTAGEN 236
FT /note="R->H: In scrm-D and ice1-1D; cold resistance and
FT excessive stomatal differentiation. Suppresses the cold-
FT induction of CBF3/DREB1A."
FT /evidence="ECO:0000269|PubMed:12672693,
FT ECO:0000269|PubMed:18641265"
FT MUTAGEN 312
FT /note="E->G: Loss of excessive stomatal differentiation;
FT when associated with H-236."
FT /evidence="ECO:0000269|PubMed:18641265"
FT MUTAGEN 393
FT /note="K->R: Loss of sumoylation. Increases freezing
FT sensitivity."
FT /evidence="ECO:0000269|PubMed:17416732"
FT CONFLICT 93
FT /note="C -> R (in Ref. 6; BAF00372)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="G -> C (in Ref. 6; BAF00372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 53539 MW; DCD56016F49E105B CRC64;
MGLDGNNGGG VWLNGGGGER EENEEGSWGR NQEDGSSQFK PMLEGDWFSS NQPHPQDLQM
LQNQPDFRYF GGFPFNPNDN LLLQHSIDSS SSCSPSQAFS LDPSQQNQFL STNNNKGCLL
NVPSSANPFD NAFEFGSESG FLNQIHAPIS MGFGSLTQLG NRDLSSVPDF LSARSLLAPE
SNNNNTMLCG GFTAPLELEG FGSPANGGFV GNRAKVLKPL EVLASSGAQP TLFQKRAAMR
QSSGSKMGNS ESSGMRRFSD DGDMDETGIE VSGLNYESDE INESGKAAES VQIGGGGKGK
KKGMPAKNLM AERRRRKKLN DRLYMLRSVV PKISKMDRAS ILGDAIDYLK ELLQRINDLH
NELESTPPGS LPPTSSSFHP LTPTPQTLSC RVKEELCPSS LPSPKGQQAR VEVRLREGRA
VNIHMFCGRR PGLLLATMKA LDNLGLDVQQ AVISCFNGFA LDVFRAEQCQ EGQEILPDQI
KAVLFDTAGY AGMI
