ID IND_ARATH Reviewed; 198 AA.
AC O81313; A0JQ73;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 27-MAR-2024, entry version 142.
DE RecName: Full=Transcription factor IND;
DE AltName: Full=Basic helix-loop-helix protein 40;
DE Short=AtbHLH40;
DE Short=bHLH 40;
DE AltName: Full=Protein INDEHISCENT;
DE AltName: Full=Transcription factor EN 120;
DE AltName: Full=bHLH transcription factor bHLH040;
GN Name=IND; Synonyms=BHLH40, EN120; OrderedLocusNames=At4g00120;
GN ORFNames=F6N15.18;
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP MUTANTS IND-1 AND IND-3.
RX PubMed=15035986; DOI=10.1016/s0092-8674(04)00217-x;
RA Liljegren S.J., Roeder A.H.K., Kempin S.A., Gremski K., Ostergaard L.,
RA Guimil S., Reyes D.K., Yanofsky M.F.;
RT "Control of fruit patterning in Arabidopsis by INDEHISCENT.";
RL Cell 116:843-853(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-198, TISSUE SPECIFICITY, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia;
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 [6]
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 [7]
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).
CC -!- FUNCTION: Transcription regulator required for seed dispersal. Involved
CC in the differentiation of all three cell types required for fruit
CC dehiscence. Acts as the key regulator in a network including SHP and
CC ALC that controls specification of the valve margin. Works with ALC,
CC SHP, and FUL to allow differentiation of the lignified valve layer, the
CC spring-loaded mechanism of fruit that promotes opening. Regulates the
CC expression of the YJ80 marker. {ECO:0000269|PubMed:15035986}.
CC -!- SUBUNIT: Homodimer (Probable). Heterodimer; possibly with ALC.
CC {ECO:0000305}.
CC -!- INTERACTION:
CC O81313; Q8L9Y3: ARR14; NbExp=4; IntAct=EBI-4446992, EBI-1100737;
CC O81313; Q9LML3: At1g07210; NbExp=3; IntAct=EBI-4446992, EBI-25516668;
CC O81313; Q84K51: At1g77770; NbExp=3; IntAct=EBI-4446992, EBI-25520665;
CC O81313; A0A178VY90: At2g32840; NbExp=3; IntAct=EBI-4446992, EBI-25510857;
CC O81313; A0A178W6S0: AXX17_At1g45290; NbExp=3; IntAct=EBI-4446992, EBI-25518185;
CC O81313; A0A178UA35: AXX17_At5g50880; NbExp=3; IntAct=EBI-4446992, EBI-25520727;
CC O81313; Q8H7F6: GRXS16; NbExp=4; IntAct=EBI-4446992, EBI-4424482;
CC O81313; Q9SND4: HEC2; NbExp=4; IntAct=EBI-4446992, EBI-1536720;
CC O81313; Q84J88: HIPP36; NbExp=3; IntAct=EBI-4446992, EBI-4458346;
CC O81313; Q9FWY7: IMPA6; NbExp=3; IntAct=EBI-4446992, EBI-4431755;
CC O81313; Q9FNP4: PIA2; NbExp=3; IntAct=EBI-4446992, EBI-4435148;
CC O81313; Q9FUA4: SPT; NbExp=7; IntAct=EBI-4446992, EBI-1536703;
CC O81313; Q9FLP5: SUMO3; NbExp=3; IntAct=EBI-4446992, EBI-25512645;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: After fertilization, it is expressed in stripes
CC about four cells wide at the margins of developing wild-type fruit.
CC Also expressed in the inner valve layer, which becomes lignified later
CC in fruit development. Detected in roots. {ECO:0000269|PubMed:12679534,
CC ECO:0000269|PubMed:15035986}.
CC -!- INDUCTION: By FUL, which restrict its expression to the margins.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF069299; AAC19297.1; -; Genomic_DNA.
DR EMBL; AL161471; CAB80770.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE81825.1; -; Genomic_DNA.
DR EMBL; BT029443; ABK59672.1; -; mRNA.
DR EMBL; AF488578; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T01340; T01340.
DR RefSeq; NP_191923.1; NM_116229.2.
DR AlphaFoldDB; O81313; -.
DR SMR; O81313; -.
DR BioGRID; 13202; 15.
DR IntAct; O81313; 30.
DR STRING; 3702.O81313; -.
DR PaxDb; 3702-AT4G00120-1; -.
DR ProteomicsDB; 228850; -.
DR EnsemblPlants; AT4G00120.1; AT4G00120.1; AT4G00120.
DR GeneID; 827911; -.
DR Gramene; AT4G00120.1; AT4G00120.1; AT4G00120.
DR KEGG; ath:AT4G00120; -.
DR Araport; AT4G00120; -.
DR TAIR; AT4G00120; IND.
DR eggNOG; ENOG502RZ93; Eukaryota.
DR HOGENOM; CLU_1398124_0_0_1; -.
DR InParanoid; O81313; -.
DR OMA; AMKEMQY; -.
DR OrthoDB; 1220854at2759; -.
DR PhylomeDB; O81313; -.
DR PRO; PR:O81313; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81313; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0010197; P:polar nucleus fusion; IMP:TAIR.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:TAIR.
DR CDD; cd11454; bHLH_AtIND_like; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR045843; IND-like.
DR PANTHER; PTHR45914; TRANSCRIPTION FACTOR HEC3-RELATED; 1.
DR PANTHER; PTHR45914:SF64; TRANSCRIPTION FACTOR IND; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..198
FT /note="Transcription factor IND"
FT /id="PRO_0000127252"
FT DOMAIN 118..167
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 128
FT /note="R->H: In ind-3; defects in margin definition,
FT especially at the fruit base."
FT MUTAGEN 141
FT /note="L->F: In ind-1; defects in margin definition,
FT especially at the fruit base."
SQ SEQUENCE 198 AA; 22949 MW; 5A84F2EE23825EBF CRC64;
MENGMYKKKG VCDSCVSSKS RSNHSPKRSM MEPQPHHLLM DWNKANDLLT QEHAAFLNDP
HHLMLDPPPE TLIHLDEDEE YDEDMDAMKE MQYMIAVMQP VDIDPATVPK PNRRNVRISD
DPQTVVARRR RERISEKIRI LKRIVPGGAK MDTASMLDEA IRYTKFLKRQ VRILQPHSQI
GAPMANPSYL CYYHNSQP
//
