KNAT1_ARATH
ID KNAT1_ARATH Reviewed; 398 AA.
AC P46639; Q8S3L9; Q8S3M0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Homeobox protein knotted-1-like 1;
DE AltName: Full=Protein BREVIPEDICELLUS;
DE AltName: Full=Protein KNAT1;
GN Name=KNAT1; Synonyms=BP, BP1; OrderedLocusNames=At4g08150;
GN ORFNames=F9M13.2;
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], TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=7866029; DOI=10.2307/3869913;
RA Lincoln C., Long J., Yamaguchi J., Serikawa K.A., Hake S.;
RT "A knotted1-like homeobox gene in Arabidopsis is expressed in the
RT vegetative meristem and dramatically alters leaf morphology when
RT overexpressed in transgenic plants.";
RL Plant Cell 6:1859-1876(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta, and cv. RLD;
RX PubMed=11917137; DOI=10.1073/pnas.072626099;
RA Venglat S.P., Dumonceaux T., Rozwadowski K., Parnell L., Babic V.,
RA Keller W., Martienssen R., Selvaraj G., Datla R.;
RT "The homeobox gene BREVIPEDICELLUS is a key regulator of inflorescence
RT architecture in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4730-4735(2002).
RN [3]
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 [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].
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 INTERACTION WITH BEL1.
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 FUNCTION, AND REGULATION.
RX PubMed=11934861; DOI=10.1242/dev.129.8.1957;
RA Byrne M.E., Simorowski J., Martienssen R.A.;
RT "ASYMMETRIC LEAVES1 reveals knox gene redundancy in Arabidopsis.";
RL Development 129:1957-1965(2002).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12900451; DOI=10.1242/dev.00618;
RA Kim J.Y., Yuan Z., Jackson D.;
RT "Developmental regulation and significance of KNOX protein trafficking in
RT Arabidopsis.";
RL Development 130:4351-4362(2003).
RN [9]
RP INTERACTION WITH BLH9/PNY.
RX PubMed=12897247; DOI=10.1105/tpc.012856;
RA Smith H.M.S., Hake S.;
RT "The interaction of two homeobox genes, BREVIPEDICELLUS and PENNYWISE,
RT regulates internode patterning in the Arabidopsis inflorescence.";
RL Plant Cell 15:1717-1727(2003).
RN [10]
RP INTERACTION WITH OFP1; OFP2; OFP4; OFP6 AND OFP12.
RX PubMed=15781858; DOI=10.1073/pnas.0501181102;
RA Hackbusch J., Richter K., Muller J., Salamini F., Uhrig J.F.;
RT "A central role of Arabidopsis thaliana ovate family proteins in networking
RT and subcellular localization of 3-aa loop extension homeodomain proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4908-4912(2005).
RN [11]
RP INTERACTION WITH BLH8/PNF AND BLH9/PNY.
RX PubMed=16741748; DOI=10.1007/s00425-006-0298-9;
RA Kanrar S., Onguka O., Smith H.M.S.;
RT "Arabidopsis inflorescence architecture requires the activities of KNOX-
RT BELL homeodomain heterodimers.";
RL Planta 224:1163-1173(2006).
RN [12]
RP INTERACTION WITH BEL1 AND BLH2.
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 [13]
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 [14]
RP INTERACTION WITH CCT7 AND CCT8.
RX PubMed=21868675; DOI=10.1126/science.1205727;
RA Xu X.M., Wang J., Xuan Z., Goldshmidt A., Borrill P.G., Hariharan N.,
RA Kim J.Y., Jackson D.;
RT "Chaperonins facilitate KNOTTED1 cell-to-cell trafficking and stem cell
RT function.";
RL Science 333:1141-1144(2011).
RN [15]
RP INTERACTION WITH AGO10/PNH, AND TISSUE SPECIFICITY.
RX PubMed=26390296; DOI=10.1371/journal.pgen.1005479;
RA Ding L., Yan S., Jiang L., Zhao W., Ning K., Zhao J., Liu X., Zhang J.,
RA Wang Q., Zhang X.;
RT "HANABA TARANU (HAN) bridges meristem and organ primordia boundaries
RT through PINHEAD, JAGGED, BLADE-ON-PETIOLE2 and CYTOKININ OXIDASE 3 during
RT flower development in Arabidopsis.";
RL PLoS Genet. 11:E1005479-E1005479(2015).
RN [16]
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: May play a role in meristem function, and may be involved in
CC maintaining cells in an undifferentiated, meristematic state, and its
CC expression disappears at the same time the shoot apex undergoes the
CC transition from vegetative to reproductive development
CC (PubMed:11934861). Positive regulator of LATERAL ORGAN BOUNDARIES (LOB)
CC (PubMed:11934861). Probably binds to the DNA sequence 5'-TGAC-3'
CC (PubMed:11934861). Able to traffic from the L1 to the L2/L3 layers of
CC the meristem, presumably through plasmodesmata (PubMed:12900451).
CC {ECO:0000269|PubMed:11934861, ECO:0000269|PubMed:12900451,
CC ECO:0000269|PubMed:7866029}.
CC -!- SUBUNIT: May form heterodimeric complex with the TALE/BELL proteins
CC BEL1, BLH2, BLH8/PNF and BLH9/PNY (PubMed:11701881, PubMed:12897247,
CC PubMed:16741748, PubMed:17873098). Interacts with OFP1, OFP2, OFP4,
CC OFP6 and OFP12 (PubMed:15781858). Interacts with CCT7 and CCT8
CC (PubMed:21868675). Interacts with KNATM-B (PubMed:18398054). Binds to
CC AGO10/PNH (PubMed:26390296). Interacts with BZIP30 (PubMed:27402171).
CC {ECO:0000269|PubMed:11701881, ECO:0000269|PubMed:12897247,
CC ECO:0000269|PubMed:15781858, ECO:0000269|PubMed:16741748,
CC ECO:0000269|PubMed:17873098, ECO:0000269|PubMed:18398054,
CC ECO:0000269|PubMed:21868675, ECO:0000269|PubMed:26390296,
CC ECO:0000269|PubMed:27402171}.
CC -!- INTERACTION:
CC P46639; A0A384KCR8: At1g05860; NbExp=3; IntAct=EBI-530486, EBI-25518310;
CC P46639; F4HZI8: At1g15200; NbExp=3; IntAct=EBI-530486, EBI-25516058;
CC P46639; Q9SXE5: At1g62520; NbExp=3; IntAct=EBI-530486, EBI-4426262;
CC P46639; A0A178VY90: At2g32840; NbExp=3; IntAct=EBI-530486, EBI-25510857;
CC P46639; A0A1I9LTW1: At3g54390; NbExp=3; IntAct=EBI-530486, EBI-15191983;
CC P46639; Q9LYL6: At3g56270; NbExp=3; IntAct=EBI-530486, EBI-1238139;
CC P46639; P48731: ATH1; NbExp=6; IntAct=EBI-530486, EBI-912904;
CC P46639; Q38897: BEL1; NbExp=8; IntAct=EBI-530486, EBI-1153783;
CC P46639; Q9SK91: BHLH94; NbExp=3; IntAct=EBI-530486, EBI-15192173;
CC P46639; Q94KL5: BLH4; NbExp=3; IntAct=EBI-530486, EBI-1153797;
CC P46639; O65685: BLH6; NbExp=4; IntAct=EBI-530486, EBI-1153881;
CC P46639; Q9SIW1: BLH7; NbExp=5; IntAct=EBI-530486, EBI-1153967;
CC P46639; Q9LZM8: BLH9; NbExp=7; IntAct=EBI-530486, EBI-530473;
CC P46639; Q8L5Y6: CAND1; NbExp=4; IntAct=EBI-530486, EBI-602912;
CC P46639; Q84K25: COG8; NbExp=3; IntAct=EBI-530486, EBI-4425470;
CC P46639; Q84Y18: CXIP4; NbExp=3; IntAct=EBI-530486, EBI-25522794;
CC P46639; Q9SKK0: EBF1; NbExp=3; IntAct=EBI-530486, EBI-401198;
CC P46639; O80654: ERF037; NbExp=4; IntAct=EBI-530486, EBI-25511744;
CC P46639; Q9FN91: EXO70H7; NbExp=3; IntAct=EBI-530486, EBI-25516131;
CC P46639; Q9SQI2: GI; NbExp=3; IntAct=EBI-530486, EBI-446380;
CC P46639; Q8RXD6: HUB1; NbExp=5; IntAct=EBI-530486, EBI-2012188;
CC P46639; P46639: KNAT1; NbExp=5; IntAct=EBI-530486, EBI-530486;
CC P46639; O80397: MKK4; NbExp=3; IntAct=EBI-530486, EBI-2358409;
CC P46639; Q8GWP0: MYB39; NbExp=3; IntAct=EBI-530486, EBI-4440057;
CC P46639; Q9FX36: MYB54; NbExp=5; IntAct=EBI-530486, EBI-25511270;
CC P46639; Q84JP1: NFYA7; NbExp=3; IntAct=EBI-530486, EBI-4444640;
CC P46639; Q9SGW3: RPN12A; NbExp=3; IntAct=EBI-530486, EBI-594133;
CC P46639; Q9LUF3: SAE1B-1; NbExp=4; IntAct=EBI-530486, EBI-4456124;
CC P46639; Q9ZU90: SKIP28; NbExp=3; IntAct=EBI-530486, EBI-604427;
CC P46639; Q84JG2: SWI3B; NbExp=6; IntAct=EBI-530486, EBI-1102271;
CC P46639; Q9LEZ9: TCP17; NbExp=3; IntAct=EBI-530486, EBI-15192327;
CC P46639; Q9LT89: TCP19; NbExp=3; IntAct=EBI-530486, EBI-4426178;
CC P46639; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-530486, EBI-15192297;
CC P46639; Q84MB2: TIFY8; NbExp=5; IntAct=EBI-530486, EBI-4426557;
CC P46639; Q9LVG2: TOE2; NbExp=3; IntAct=EBI-530486, EBI-4424568;
CC P46639; O22768: UNE12; NbExp=3; IntAct=EBI-530486, EBI-3133156;
CC P46639; Q5CCK4: VAL2; NbExp=3; IntAct=EBI-530486, EBI-15193683;
CC P46639; Q93WU9: WRKY51; NbExp=3; IntAct=EBI-530486, EBI-15214372;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the vegetative meristem. Present in
CC the base of flower primordia (PubMed:26390296).
CC {ECO:0000269|PubMed:12900451, ECO:0000269|PubMed:26390296,
CC ECO:0000269|PubMed:7866029}.
CC -!- INDUCTION: Negatively regulated by ASYMMETRIC LEAVES1 (AS1) and
CC ASYMMETRIC LEAVES2 (AS2).
CC -!- SIMILARITY: Belongs to the TALE/KNOX homeobox family.
CC {ECO:0000255|PROSITE-ProRule:PRU00559}.
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DR EMBL; U14174; AAA67881.1; -; Genomic_DNA.
DR EMBL; AF482994; AAM03026.1; -; mRNA.
DR EMBL; AF482995; AAM03027.1; -; mRNA.
DR EMBL; AC006267; AAD27897.1; -; Genomic_DNA.
DR EMBL; AL161510; CAB81151.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82597.1; -; Genomic_DNA.
DR EMBL; AY080834; AAL87309.1; -; mRNA.
DR EMBL; AY113982; AAM45030.1; -; mRNA.
DR PIR; D85080; D85080.
DR RefSeq; NP_192555.1; NM_116884.4.
DR AlphaFoldDB; P46639; -.
DR SMR; P46639; -.
DR BioGRID; 11664; 110.
DR IntAct; P46639; 106.
DR STRING; 3702.AT4G08150.1; -.
DR PaxDb; P46639; -.
DR PRIDE; P46639; -.
DR ProteomicsDB; 237044; -.
DR EnsemblPlants; AT4G08150.1; AT4G08150.1; AT4G08150.
DR GeneID; 826364; -.
DR Gramene; AT4G08150.1; AT4G08150.1; AT4G08150.
DR KEGG; ath:AT4G08150; -.
DR Araport; AT4G08150; -.
DR TAIR; locus:2128828; AT4G08150.
DR eggNOG; KOG0773; Eukaryota.
DR HOGENOM; CLU_040111_0_0_1; -.
DR InParanoid; P46639; -.
DR OMA; TQEANNN; -.
DR OrthoDB; 1171537at2759; -.
DR PhylomeDB; P46639; -.
DR PRO; PR:P46639; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P46639; baseline and differential.
DR Genevisible; P46639; AT.
DR GO; GO:0005634; C:nucleus; ISS: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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0045165; P:cell fate commitment; IMP:TAIR.
DR GO; GO:0001708; P:cell fate specification; IMP:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010051; P:xylem and phloem pattern formation; IMP:TAIR.
DR GO; GO:0010089; P:xylem development; IMP:TAIR.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR005539; ELK_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR008422; Homeobox_KN_domain.
DR InterPro; IPR005540; KNOX1.
DR InterPro; IPR005541; KNOX2.
DR Pfam; PF03789; ELK; 1.
DR Pfam; PF05920; Homeobox_KN; 1.
DR Pfam; PF03790; KNOX1; 1.
DR Pfam; PF03791; KNOX2; 1.
DR SMART; SM01188; ELK; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM01255; KNOX1; 1.
DR SMART; SM01256; KNOX2; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51213; ELK; 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.
FT CHAIN 1..398
FT /note="Homeobox protein knotted-1-like 1"
FT /id="PRO_0000048957"
FT DOMAIN 279..299
FT /note="ELK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00559"
FT DNA_BIND 300..363
FT /note="Homeobox; TALE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 20..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 10
FT /note="T -> S (in Ref. 2; AAM03027/AAM03026)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="E -> D (in Ref. 2; AAM03026)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="N -> NN (in Ref. 2; AAM03027/AAM03026)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="N -> NN (in Ref. 2; AAM03027/AAM03026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 45836 MW; 815A22786589A316 CRC64;
MEEYQHDNST TPQRVSFLYS PISSSNKNDN TSDTNNNNNN NNSSNYGPGY NNTNNNNHHH
QHMLFPHMSS LLPQTTENCF RSDHDQPNNN NNPSVKSEAS SSRINHYSML MRAIHNTQEA
NNNNNDNVSD VEAMKAKIIA HPHYSTLLQA YLDCQKIGAP PDVVDRITAA RQDFEARQQR
STPSVSASSR DPELDQFMEA YCDMLVKYRE ELTRPIQEAM EFIRRIESQL SMLCQSPIHI
LNNPDGKSDN MGSSDEEQEN NSGGETELPE IDPRAEDREL KNHLLKKYSG YLSSLKQELS
KKKKKGKLPK EARQKLLTWW ELHYKWPYPS ESEKVALAES TGLDQKQINN WFINQRKRHW
KPSEDMQFMV MDGLQHPHHA ALYMDGHYMG DGPYRLGP
