BEL1_ARATH
ID BEL1_ARATH Reviewed; 611 AA.
AC Q38897; Q93Y33; Q9FN59;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Homeobox protein BEL1 homolog;
GN Name=BEL1; Synonyms=BELL1; OrderedLocusNames=At5g41410; ORFNames=MYC6.12;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=8521490; DOI=10.1016/0092-8674(95)90186-8;
RA Reiser L., Modrusan Z., Margossian L., Samach A., Ohad N., Haughn G.W.,
RA Fischer R.L.;
RT "The BELL1 gene encodes a homeodomain protein involved in pattern formation
RT in the Arabidopsis ovule primordium.";
RL Cell 83:735-742(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION.
RX PubMed=12244239; DOI=10.2307/3869754;
RA Modrusan Z., Reiser L., Feldmann K.A., Fischer R.L., Haughn G.W.;
RT "Homeotic transformation of ovules into carpel-like structures in
RT Arabidopsis.";
RL Plant Cell 6:333-349(1994).
RN [6]
RP HETERODIMERIZATION DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=11701881; DOI=10.2307/3871587;
RA Bellaoui M., Pidkowich M.S., Samach A., Kushalappa K., Kohalmi S.E.,
RA Modrusan Z., Crosby W.L., Haughn G.W.;
RT "The Arabidopsis BELL1 and KNOX TALE homeodomain proteins interact through
RT a domain conserved between plants and animals.";
RL Plant Cell 13:2455-2470(2001).
RN [7]
RP GENE FAMILY ORGANIZATION.
RX PubMed=15120075; DOI=10.1016/j.cub.2004.04.032;
RA Smith H.M.S., Campbell B.C.C., Hake S.;
RT "Competence to respond to floral inductive signals requires the homeobox
RT genes PENNYWISE and POUND-FOOLISH.";
RL Curr. Biol. 14:812-817(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH MADS-BOX FACTORS.
RX PubMed=17693535; DOI=10.1105/tpc.107.051797;
RA Brambilla V., Battaglia R., Colombo M., Masiero S., Bencivenga S.,
RA Kater M.M., Colombo L.;
RT "Genetic and molecular interactions between BELL1 and MADS box factors
RT support ovule development in Arabidopsis.";
RL Plant Cell 19:2544-2556(2007).
RN [9]
RP INTERACTION WITH TALE/KNOX PROTEINS.
RX PubMed=17873098; DOI=10.1105/tpc.106.048769;
RA Kumar R., Kushalappa K., Godt D., Pidkowich M.S., Pastorelli S.,
RA Hepworth S.R., Haughn G.W.;
RT "The Arabidopsis BEL1-LIKE HOMEODOMAIN proteins SAW1 and SAW2 act
RT redundantly to regulate KNOX expression spatially in leaf margins.";
RL Plant Cell 19:2719-2735(2007).
RN [10]
RP INTERACTION WITH KNATM.
RX PubMed=18398054; DOI=10.1105/tpc.108.058495;
RA Magnani E., Hake S.;
RT "KNOX lost the OX: the Arabidopsis KNATM gene defines a novel class of KNOX
RT transcriptional regulators missing the homeodomain.";
RL Plant Cell 20:875-887(2008).
RN [11]
RP FUNCTION.
RX PubMed=22786869; DOI=10.1105/tpc.112.100164;
RA Bencivenga S., Simonini S., Benkova E., Colombo L.;
RT "The transcription factors BEL1 and SPL are required for cytokinin and
RT auxin signaling during ovule development in Arabidopsis.";
RL Plant Cell 24:2886-2897(2012).
RN [12]
RP INTERACTION WITH BZIP30.
RX PubMed=27402171; DOI=10.1111/tpj.13264;
RA Lozano-Sotomayor P., Chavez Montes R.A., Silvestre-Vano M.,
RA Herrera-Ubaldo H., Greco R., Pablo-Villa J., Galliani B.M.,
RA Diaz-Ramirez D., Weemen M., Boutilier K., Pereira A., Colombo L.,
RA Madueno F., Marsch-Martinez N., de Folter S.;
RT "Altered expression of the bZIP transcription factor DRINK ME affects
RT growth and reproductive development in Arabidopsis thaliana.";
RL Plant J. 88:437-451(2016).
CC -!- FUNCTION: Plays a major role in ovule patterning and in determination
CC of integument identity via its interaction with MADS-box factors.
CC Formation of complex with AG-SEP dimers negatively regulates the carpel
CC identity process and favors the maintenance of ovule identity. BEL1-STM
CC complex maintains the indeterminacy of the inflorescence meristem.
CC Required, with SPL, for cytokinin-induced PIN1 expression in ovules
CC (PubMed:22786869). {ECO:0000269|PubMed:12244239,
CC ECO:0000269|PubMed:17693535, ECO:0000269|PubMed:22786869}.
CC -!- SUBUNIT: May form heterodimeric complexes with TALE/KNOX proteins STM,
CC KNAT1/BP, KNAT2 and KNAT5 (PubMed:17873098). Interacts with AG-SEP1 and
CC AG-SEP3 dimers (PubMed:17693535). Interacts with KNATM, isoform KNATM-B
CC (PubMed:18398054). Interacts with BZIP30 (PubMed:27402171).
CC {ECO:0000269|PubMed:17693535, ECO:0000269|PubMed:17873098,
CC ECO:0000269|PubMed:18398054, ECO:0000269|PubMed:27402171}.
CC -!- INTERACTION:
CC Q38897; A0A178VFA3: At3g19070; NbExp=3; IntAct=EBI-1153783, EBI-15192431;
CC Q38897; Q8S307: BZR1; NbExp=3; IntAct=EBI-1153783, EBI-1803261;
CC Q38897; Q94ID6: ERF12; NbExp=3; IntAct=EBI-1153783, EBI-4446727;
CC Q38897; Q9MAI5: ERF8; NbExp=3; IntAct=EBI-1153783, EBI-2000137;
CC Q38897; Q9LQT8: GAI; NbExp=3; IntAct=EBI-1153783, EBI-963606;
CC Q38897; Q9C5X0: IAA34; NbExp=3; IntAct=EBI-1153783, EBI-3946459;
CC Q38897; P46639: KNAT1; NbExp=8; IntAct=EBI-1153783, EBI-530486;
CC Q38897; P46640: KNAT2; NbExp=3; IntAct=EBI-1153783, EBI-1153809;
CC Q38897; P48000: KNAT3; NbExp=3; IntAct=EBI-1153783, EBI-1153908;
CC Q38897; P48002: KNAT5; NbExp=3; IntAct=EBI-1153783, EBI-1153922;
CC Q38897; Q9SLH3: RGA; NbExp=3; IntAct=EBI-1153783, EBI-963624;
CC Q38897; Q8GXW1: RGL2; NbExp=3; IntAct=EBI-1153783, EBI-963665;
CC Q38897; Q38874: STM; NbExp=9; IntAct=EBI-1153783, EBI-530523;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000269|PubMed:11701881, ECO:0000269|PubMed:8521490}.
CC -!- TISSUE SPECIFICITY: Expressed in both floral and vegetative tissues.
CC {ECO:0000269|PubMed:8521490}.
CC -!- DEVELOPMENTAL STAGE: Early expression is detected in the inflorescence
CC apex of developing flowers and also in the ovule primordium and the
CC integuments. {ECO:0000269|PubMed:8521490}.
CC -!- DOMAIN: The SR/KY and BELL domains are responsive for the interaction
CC between the TALE/BELL proteins and the TALE/KNOX proteins.
CC -!- SIMILARITY: Belongs to the TALE/BELL homeobox family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK96704.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U39944; AAB05099.2; -; mRNA.
DR EMBL; AB006707; BAB08513.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94676.1; -; Genomic_DNA.
DR EMBL; AY049237; AAK83580.1; -; mRNA.
DR EMBL; AY054513; AAK96704.1; ALT_FRAME; mRNA.
DR EMBL; BT002637; AAO11553.1; -; mRNA.
DR PIR; A57632; A57632.
DR RefSeq; NP_198957.1; NM_123506.3.
DR AlphaFoldDB; Q38897; -.
DR SMR; Q38897; -.
DR BioGRID; 19394; 38.
DR IntAct; Q38897; 40.
DR STRING; 3702.AT5G41410.1; -.
DR iPTMnet; Q38897; -.
DR PaxDb; Q38897; -.
DR PRIDE; Q38897; -.
DR ProteomicsDB; 240856; -.
DR EnsemblPlants; AT5G41410.1; AT5G41410.1; AT5G41410.
DR GeneID; 834143; -.
DR Gramene; AT5G41410.1; AT5G41410.1; AT5G41410.
DR KEGG; ath:AT5G41410; -.
DR Araport; AT5G41410; -.
DR TAIR; locus:2177856; AT5G41410.
DR eggNOG; KOG0773; Eukaryota.
DR HOGENOM; CLU_011058_5_1_1; -.
DR InParanoid; Q38897; -.
DR OMA; GHYREQM; -.
DR OrthoDB; 839212at2759; -.
DR PhylomeDB; Q38897; -.
DR PRO; PR:Q38897; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38897; baseline and differential.
DR Genevisible; Q38897; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR008422; Homeobox_KN_domain.
DR InterPro; IPR006563; POX_dom.
DR Pfam; PF05920; Homeobox_KN; 1.
DR Pfam; PF07526; POX; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00574; POX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Homeobox; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..611
FT /note="Homeobox protein BEL1 homolog"
FT /id="PRO_0000315456"
FT DNA_BIND 391..453
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 63..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..213
FT /note="SR/KY domain"
FT REGION 225..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..340
FT /note="BELL domain"
FT MOTIF 275..290
FT /note="Bipartite nuclear localization"
FT /evidence="ECO:0000255"
FT COMPBIAS 225..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 113
FT /note="R -> G (in Ref. 4; AAK96704)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 69493 MW; 6C885F0B366739AD CRC64;
MARDQFYGHN NHHHQEQQHQ MINQIQGFDE TNQNPTDHHH YNHQIFGSNS NMGMMIDFSK
QQQIRMTSGS DHHHHHHQTS GGTDQNQLLE DSSSAMRLCN VNNDFPSEVN DERPPQRPSQ
GLSLSLSSSN PTSISLQSFE LRPQQQQQQG YSGNKSTQHQ NLQHTQMMMM MMNSHHQNNN
NNNHQHHNHH QFQIGSSKYL SPAQELLSEF CSLGVKESDE EVMMMKHKKK QKGKQQEEWD
TSHHSNNDQH DQSATTSSKK HVPPLHSLEF MELQKRKAKL LSMLEELKRR YGHYREQMRV
AAAAFEAAVG LGGAEIYTAL ASRAMSRHFR CLKDGLVGQI QATSQALGER EEDNRAVSIA
ARGETPRLRL LDQALRQQKS YRQMTLVDAH PWRPQRGLPE RAVTTLRAWL FEHFLHPYPS
DVDKHILARQ TGLSRSQVSN WFINARVRLW KPMIEEMYCE ETRSEQMEIT NPMMIDTKPD
PDQLIRVEPE SLSSIVTNPT SKSGHNSTHG TMSLGSTFDF SLYGNQAVTY AGEGGPRGDV
SLTLGLQRND GNGGVSLALS PVTAQGGQLF YGRDHIEEGP VQYSASMLDD DQVQNLPYRN
LMGAQLLHDI V
