BLI_ARATH
ID BLI_ARATH Reviewed; 714 AA.
AC Q9LIQ9;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein BLISTER {ECO:0000303|PubMed:20647345};
DE AltName: Full=Protein KOLD SENSITIV-1 {ECO:0000303|PubMed:20674078};
GN Name=BLI {ECO:0000303|PubMed:20647345};
GN Synonyms=KOS1 {ECO:0000303|PubMed:20674078};
GN OrderedLocusNames=At3g23980 {ECO:0000312|Araport:AT3G23980};
GN ORFNames=F14O13.17 {ECO:0000312|EMBL:BAB03016.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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, INTERACTION WITH CLF, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=20647345; DOI=10.1105/tpc.109.073403;
RA Schatlowski N., Stahl Y., Hohenstatt M.L., Goodrich J., Schubert D.;
RT "The CURLY LEAF interacting protein BLISTER controls expression of
RT polycomb-group target genes and cellular differentiation of Arabidopsis
RT thaliana.";
RL Plant Cell 22:2291-2305(2010).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20674078; DOI=10.1016/j.jplph.2010.07.001;
RA Purdy S.J., Bussell J.D., Nelson D.C., Villadsen D., Smith S.M.;
RT "A nuclear-localized protein, KOLD SENSITIV-1, affects the expression of
RT cold-responsive genes during prolonged chilling in Arabidopsis.";
RL J. Plant Physiol. 168:263-269(2011).
CC -!- FUNCTION: Is required for normal leaf, flower and seed development and
CC controls cotyledon and leaf patterning by inhibiting premature
CC differentiation. Regulates the expression of a subset of PcG target
CC genes. Is required for the repression of the floral specific genes PI,
CC SEP2, and SEP3, but also for the activation of FLC (PubMed:20647345).
CC Involved in response to cold. Involved in the regulation of COR15A,
CC COR15B, BAM3 and AMY3 transcripts, and ascorbate levels in response to
CC prolonged chilling temperatures (PubMed:20674078).
CC {ECO:0000269|PubMed:20647345, ECO:0000269|PubMed:20674078}.
CC -!- SUBUNIT: Interacts with CLF. {ECO:0000269|PubMed:20647345}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20647345,
CC ECO:0000269|PubMed:20674078}. Cytoplasm {ECO:0000269|PubMed:20647345}.
CC Note=May shuttle between the nucleus and the cytoplasm.
CC {ECO:0000269|PubMed:20647345}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, emerging lateral roots,
CC shoot apical meristem (SAM), vasculature of cotyledons, leaves, sepals
CC and carpels. {ECO:0000269|PubMed:20647345}.
CC -!- DEVELOPMENTAL STAGE: During embryo development, expressed in the basal
CC part and the vasculature of heart stage and torpedo stage embryos.
CC {ECO:0000269|PubMed:20647345}.
CC -!- DISRUPTION PHENOTYPE: Pleiotropic phenotype with defects in cotyledon,
CC leaf, flower and seed development, slow growth, severe epidermal
CC defects, including loss of cell adhesion, outgrowth of cells and
CC increased cotyledon cell size. {ECO:0000269|PubMed:20647345}.
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DR EMBL; AP001297; BAB03016.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76841.1; -; Genomic_DNA.
DR RefSeq; NP_189040.3; NM_113303.4.
DR AlphaFoldDB; Q9LIQ9; -.
DR SMR; Q9LIQ9; -.
DR STRING; 3702.AT3G23980.1; -.
DR iPTMnet; Q9LIQ9; -.
DR PaxDb; Q9LIQ9; -.
DR PRIDE; Q9LIQ9; -.
DR ProteomicsDB; 240547; -.
DR EnsemblPlants; AT3G23980.1; AT3G23980.1; AT3G23980.
DR GeneID; 821982; -.
DR Gramene; AT3G23980.1; AT3G23980.1; AT3G23980.
DR KEGG; ath:AT3G23980; -.
DR Araport; AT3G23980; -.
DR TAIR; locus:2076071; AT3G23980.
DR eggNOG; ENOG502RCM2; Eukaryota.
DR HOGENOM; CLU_019488_0_0_1; -.
DR InParanoid; Q9LIQ9; -.
DR OMA; MPKQNDD; -.
DR OrthoDB; 624404at2759; -.
DR PhylomeDB; Q9LIQ9; -.
DR PRO; PR:Q9LIQ9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIQ9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0048826; P:cotyledon morphogenesis; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0009965; P:leaf morphogenesis; IGI:TAIR.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR GO; GO:0010091; P:trichome branching; IMP:TAIR.
DR InterPro; IPR044194; BLISTER.
DR PANTHER; PTHR47490; PTHR47490; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Developmental protein; Growth regulation; Nucleus;
KW Reference proteome; Stress response.
FT CHAIN 1..714
FT /note="Protein BLISTER"
FT /id="PRO_0000440869"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 356..525
FT /evidence="ECO:0000255"
FT COMPBIAS 10..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 78384 MW; 5C97E1F9A7D4A1CB CRC64;
MASATSSRRQ EDVEAGRRKL EQFRKRKAAE KAKKASQNTQ PVDNSQQSVI DSDGAGASIS
NGPLKQSAES TSNETHTKDV YNLSFSNTAM DDGSKERSRQ DDGQESVGKV DFSNSLELIG
SSKDLTVNTR PEVVPYSNID KQSSESFDRA STLRETASLF SGTSMQMDGF IHGSGLTSSR
KDSLQPTTRM AGSFDEVAKN QQGSGELGGS IVQKPTLSSS YLFNSPDTSS RPSEPSDFSV
NITSSSPLNS AKSEATVKRS RPSFLDSLNI SRAPETQYQH PEIQADLVTS SGSQLSGSDG
FGPSYISGRR DSNGPSSLTS GASDYPNPFE KFRSSLYPAA NGVMPGFTDF SMPKQNDDFT
ALEQHIEDLT QEKFSLQRDL DASRALAESL ASENSSMTDT YNQQRGLVNQ LKDDMERLYQ
QIQAQMGELE SVRVEYANAQ LECNAADERS QILASEVISL EDKALRLRSN ELKLERELEK
AQTEMLSYKK KLQSLEKDRQ DLQSTIKALQ EEKKVLQTMV QKASSGGKST DLSKNSTSRK
NVSTSTEGLA ISDTTPESSN QETDSTTLLE SDSSNTAIIP ETRQLTLEGF SLSVPADQMR
VIHNINTLIA ELAIEKEELV QALSSELSRS AHVQELNKEL SRKLEAQTQR LELVTAQKMA
IDNVSPEKQQ PDTHVVQERT PIADEGDEVV ERVLGWIMKM FPGGPSKRRT SKLL
