Q9LSE2 · ICE1_ARATH

Function

function

Transcriptional activator that regulates the cold-induced transcription of CBF/DREB1 genes. Binds specifically to the MYC recognition sites (5'-CANNTG-3') found in the CBF3/DREB1A promoter. Mediates stomatal differentiation in the epidermis probably by controlling successive roles of SPCH, MUTE, and FAMA. Functions as a dimer with SPCH during stomatal initiation (PubMed:18641265, PubMed:28507175).

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnucleus
Molecular Functioncis-regulatory region sequence-specific DNA binding
Molecular Functioncore promoter sequence-specific DNA binding
Molecular FunctionDNA binding
Molecular FunctionDNA-binding transcription factor activity
Molecular Functionprotein dimerization activity
Molecular Functiontranscription cis-regulatory region binding
Biological Processabscisic acid-activated signaling pathway
Biological Processendosperm development
Biological Processnegative regulation of DNA-templated transcription
Biological Processpositive regulation of DNA-templated transcription
Biological Processregulation of abscisic acid biosynthetic process
Biological Processresponse to cold
Biological Processresponse to freezing
Biological Processseed dormancy process
Biological Processseed morphogenesis
Biological Processstomatal lineage progression

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Transcription factor ICE1
  • Alternative names
    • Basic helix-loop-helix protein 116 (AtbHLH116; bHLH 116)
    • Inducer of CBF expression 1
    • Transcription factor EN 45
    • Transcription factor SCREAM
    • bHLH transcription factor bHLH116

Gene names

    • Name
      SCRM
    • Synonyms
      BHLH116, EN45, ICE1
    • ORF names
      MDJ14.1, MLJ15.14
    • Ordered locus names
      At3g26744

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9LSE2
  • Secondary accessions
    • Q0WR77
    • Q2V3S3
    • Q5PNR8

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Nucleus

Keywords

Phenotypes & Variants

Disruption phenotype

The ice1-2 scrm2-1 double mutant lacks stomata so that the epidermis only contains pavement cells.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis236In scrm-D and ice1-1D; cold resistance and excessive stomatal differentiation. Suppresses the cold-induction of CBF3/DREB1A.
Mutagenesis312Loss of excessive stomatal differentiation; when associated with H-236.
Mutagenesis393Loss of sumoylation. Increases freezing sensitivity.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 23 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, cross-link.

Type
IDPosition(s)Description
ChainPRO_00001272351-494Transcription factor ICE1
Cross-link393Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modification

Ubiquitinated. Cold-treatment induced association with the E3 ubiquitin ligase HOS1 targets the protein for proteolysis by the ubiquitin-dependent proteasome pathway. Sumoylated at Lys-393 by SIZ1. Sumoylated ICE1 represses HOS1 and MYB15 and facilitates the positive regulation of CBF3/DREB1A-dependent cold signaling and freezing tolerance.

Keywords

Proteomic databases

Expression

Tissue specificity

Widely expressed in the whole plant with high expression in leaves and stem. Broad expression within stomatal cell lineages of leaf epidermis.

Induction

By high-salt stress, cold stress and abscisic acid (ABA) treatment.

Gene expression databases

Interaction

Subunit

Homodimer (Probable). Efficient DNA binding requires dimerization with another bHLH protein (By similarity).
Interacts with the C-terminal part of HOS1 (PubMed:18641265).
Heterodimers with SPCH, MUTE, and FAMA (PubMed:18641265, PubMed:28507175).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY Q9LSE2HOS1 Q84JU63EBI-15583266, EBI-15583242
BINARY Q9LSE2LFR Q9LS903EBI-15583266, EBI-40270350

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain, coiled coil.

Type
IDPosition(s)Description
Region1-58Disordered
Compositional bias30-58Polar residues
Compositional bias240-255Polar residues
Region240-264Disordered
Region281-306Disordered
Domain303-352bHLH
Coiled coil344-365
Region363-384Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9LSE2-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    494
  • Mass (Da)
    53,539
  • Last updated
    2000-10-01 v1
  • MD5 Checksum
    EBF6FAB44F3301780827D48023484084
MGLDGNNGGGVWLNGGGGEREENEEGSWGRNQEDGSSQFKPMLEGDWFSSNQPHPQDLQMLQNQPDFRYFGGFPFNPNDNLLLQHSIDSSSSCSPSQAFSLDPSQQNQFLSTNNNKGCLLNVPSSANPFDNAFEFGSESGFLNQIHAPISMGFGSLTQLGNRDLSSVPDFLSARSLLAPESNNNNTMLCGGFTAPLELEGFGSPANGGFVGNRAKVLKPLEVLASSGAQPTLFQKRAAMRQSSGSKMGNSESSGMRRFSDDGDMDETGIEVSGLNYESDEINESGKAAESVQIGGGGKGKKKGMPAKNLMAERRRRKKLNDRLYMLRSVVPKISKMDRASILGDAIDYLKELLQRINDLHNELESTPPGSLPPTSSSFHPLTPTPQTLSCRVKEELCPSSLPSPKGQQARVEVRLREGRAVNIHMFCGRRPGLLLATMKALDNLGLDVQQAVISCFNGFALDVFRAEQCQEGQEILPDQIKAVLFDTAGYAGMI

Q9LSE2-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 336-363: MDRASILGDAIDYLKELLQRINDLHNEL → VNTYFVSFISLRACLLVAVIENCCVVAL
    • 364-494: Missing

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1I9LRH4A0A1I9LRH4_ARATHICE1476

Features

Showing features for compositional bias, sequence conflict, alternative sequence.

Type
IDPosition(s)Description
Compositional bias30-58Polar residues
Sequence conflict93in Ref. 6; BAF00372
Sequence conflict190in Ref. 6; BAF00372
Compositional bias240-255Polar residues
Alternative sequenceVSP_020190336-363in isoform 2
Alternative sequenceVSP_020191364-494in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY195621
EMBL· GenBank· DDBJ
AAP14668.1
EMBL· GenBank· DDBJ
mRNA
AB026648
EMBL· GenBank· DDBJ
BAB01738.1
EMBL· GenBank· DDBJ
Genomic DNA
AB016889
EMBL· GenBank· DDBJ
BAB01738.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE77208.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE77209.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE77210.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
ANM65181.1
EMBL· GenBank· DDBJ
Genomic DNA
AY079016
EMBL· GenBank· DDBJ
AAL84972.1
EMBL· GenBank· DDBJ
mRNA
BT020379
EMBL· GenBank· DDBJ
AAV85734.1
EMBL· GenBank· DDBJ
mRNA
AK228443
EMBL· GenBank· DDBJ
BAF00372.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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