SHR_ARATH
ID SHR_ARATH Reviewed; 531 AA.
AC Q9SZF7; B3DNN8; Q8RU28;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein SHORT-ROOT {ECO:0000303|PubMed:10850497};
DE Short=AtSHR {ECO:0000303|PubMed:10850497};
DE AltName: Full=GRAS family protein 26;
DE Short=AtGRAS-26;
DE AltName: Full=Protein SHOOT GRAVITROPISM 7 {ECO:0000303|PubMed:9670559};
GN Name=SHR {ECO:0000303|PubMed:10850497};
GN Synonyms=SGR7 {ECO:0000303|PubMed:9670559};
GN OrderedLocusNames=At4g37650 {ECO:0000312|Araport:AT4G37650};
GN ORFNames=F19F18.140 {ECO:0000312|EMBL:CAB38304.1};
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=10850497; DOI=10.1016/s0092-8674(00)80865-x;
RA Helariutta Y., Fukaki H., Wysocka-Diller J.W., Nakajima K., Jung J.,
RA Sena G., Hauser M.-T., Benfey P.N.;
RT "The SHORT-ROOT gene controls radial patterning of the Arabidopsis root
RT through radial signaling.";
RL Cell 101:555-567(2000).
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 De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-531.
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 IDENTIFICATION, AND FUNCTION.
RX PubMed=9670559; DOI=10.1046/j.1365-313x.1998.00137.x;
RA Fukaki H., Wysocka-Diller J.W., Kato T., Fujisawa H., Benfey P.N.,
RA Tasaka M.;
RT "Genetic evidence that the endodermis is essential for shoot gravitropism
RT in Arabidopsis thaliana.";
RL Plant J. 14:425-430(1998).
RN [7]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND TRANSLOCATION.
RX PubMed=11565032; DOI=10.1038/35095061;
RA Nakajima K., Sena G., Nawy T., Benfey P.N.;
RT "Intercellular movement of the putative transcription factor SHR in root
RT patterning.";
RL Nature 413:307-311(2001).
RN [8]
RP FUNCTION.
RX PubMed=12569126; DOI=10.1101/gad.252503;
RA Sabatini S., Heidstra R., Wildwater M., Scheres B.;
RT "SCARECROW is involved in positioning the stem cell niche in the
RT Arabidopsis root meristem.";
RL Genes Dev. 17:354-358(2003).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15314023; DOI=10.1101/gad.305504;
RA Heidstra R., Welch D., Scheres B.;
RT "Mosaic analyses using marked activation and deletion clones dissect
RT Arabidopsis SCARECROW action in asymmetric cell division.";
RL Genes Dev. 18:1964-1969(2004).
RN [10]
RP TISSUE SPECIFICITY, AND TRANSLOCATION.
RX PubMed=15142972; DOI=10.1242/dev.01144;
RA Sena G., Jung J.W., Benfey P.N.;
RT "A broad competence to respond to SHORT ROOT revealed by tissue-specific
RT ectopic expression.";
RL Development 131:2817-2826(2004).
RN [11]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-289.
RX PubMed=15498493; DOI=10.1016/j.cub.2004.09.081;
RA Gallagher K.L., Paquette A.J., Nakajima K., Benfey P.N.;
RT "Mechanisms regulating SHORT-ROOT intercellular movement.";
RL Curr. Biol. 14:1847-1851(2004).
RN [12]
RP FUNCTION, AND INTERACTION WITH SCR.
RX PubMed=16640459; DOI=10.1371/journal.pbio.0040143;
RA Levesque M.P., Vernoux T., Busch W., Cui H., Wang J.Y., Blilou I.,
RA Hassan H., Nakajima K., Matsumoto N., Lohmann J.U., Scheres B.,
RA Benfey P.N.;
RT "Whole-genome analysis of the SHORT-ROOT developmental pathway in
RT Arabidopsis.";
RL PLoS Biol. 4:739-752(2006).
RN [13]
RP FUNCTION, AND INTERACTION WITH SCR.
RX PubMed=17446396; DOI=10.1126/science.1139531;
RA Cui H., Levesque M.P., Vernoux T., Jung J.W., Paquette A.J.,
RA Gallagher K.L., Wang J.Y., Blilou I., Scheres B., Benfey P.N.;
RT "An evolutionarily conserved mechanism delimiting SHR movement defines a
RT single layer of endodermis in plants.";
RL Science 316:421-425(2007).
RN [14]
RP INTERACTION WITH JKD AND MGP.
RX PubMed=17785527; DOI=10.1101/gad.440307;
RA Welch D., Hassan H., Blilou I., Immink R., Heidstra R., Scheres B.;
RT "Arabidopsis JACKDAW and MAGPIE zinc finger proteins delimit asymmetric
RT cell division and stabilize tissue boundaries by restricting SHORT-ROOT
RT action.";
RL Genes Dev. 21:2196-2204(2007).
RN [15]
RP INTERACTION WITH SCR AND SCL23.
RX PubMed=18500650; DOI=10.1007/s11103-008-9345-1;
RA Lee M.-H., Kim B., Song S.-K., Heo J.-O., Yu N.-I., Lee S.A., Kim M.,
RA Kim D.G., Sohn S.O., Lim C.E., Chang K.S., Lee M.M., Lim J.;
RT "Large-scale analysis of the GRAS gene family in Arabidopsis thaliana.";
RL Plant Mol. Biol. 67:659-670(2008).
RN [16]
RP MUTAGENESIS OF 342-LEU--VAL-347, AND MISCELLANEOUS.
RX PubMed=19000160; DOI=10.1111/j.1365-313x.2008.03735.x;
RA Gallagher K.L., Benfey P.N.;
RT "Both the conserved GRAS domain and nuclear localization are required for
RT SHORT-ROOT movement.";
RL Plant J. 57:785-797(2009).
RN [17]
RP INTERACTION WITH SIEL, AND MISCELLANEOUS.
RX PubMed=21924907; DOI=10.1016/j.cub.2011.08.013;
RA Koizumi K., Wu S., MacRae-Crerar A., Gallagher K.L.;
RT "An essential protein that interacts with endosomes and promotes movement
RT of the SHORT-ROOT transcription factor.";
RL Curr. Biol. 21:1559-1564(2011).
RN [18]
RP MISCELLANEOUS.
RX PubMed=23294290; DOI=10.1111/tpj.12112;
RA Wu S., Gallagher K.L.;
RT "Intact microtubules are required for the intercellular movement of the
RT SHORT-ROOT transcription factor.";
RL Plant J. 74:148-159(2013).
RN [19]
RP SUBCELLULAR LOCATION.
RX PubMed=25124761; DOI=10.1111/tpj.12640;
RA Wu S., Gallagher K.L.;
RT "The movement of the non-cell-autonomous transcription factor, SHORT-ROOT
RT relies on the endomembrane system.";
RL Plant J. 80:396-409(2014).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 59-531 IN COMPLEX WITH SCR AND
RP JKD, INTERACTION WITH SCR, AND MUTAGENESIS OF LEU-166; TRP-167; ASN-170;
RP GLU-171; TYR-176; ARG-436 AND ARG-441.
RX PubMed=28211915; DOI=10.1038/nplants.2017.10;
RA Hirano Y., Nakagawa M., Suyama T., Murase K., Shirakawa M., Takayama S.,
RA Sun T.-P., Hakoshima T.;
RT "Structure of the SHR-SCR heterodimer bound to the BIRD/IDD transcriptional
RT factor JKD.";
RL Nat. Plants 3:17010-17010(2017).
CC -!- FUNCTION: Transcription factor required for quiescent center cells
CC specification and maintenance of surrounding stem cells, and for the
CC asymmetric cell division involved in radial pattern formation in roots.
CC Essential for both cell division and cell specification. Regulates the
CC radial organization of the shoot axial organs and is required for
CC normal shoot gravitropism. Directly controls the transcription of SCR,
CC and when associated with SCR, of MGP, RLK, TRI, NUC and SCL3.
CC {ECO:0000269|PubMed:10850497, ECO:0000269|PubMed:12569126,
CC ECO:0000269|PubMed:15314023, ECO:0000269|PubMed:16640459,
CC ECO:0000269|PubMed:17446396, ECO:0000269|PubMed:9670559}.
CC -!- SUBUNIT: Interacts with SCR, SCL23, JKD and MGP (PubMed:16640459,
CC PubMed:17446396, PubMed:17785527, PubMed:18500650, PubMed:28211915).
CC Interacts with SIEL (PubMed:21924907). Association to endosomes and
CC intercellular movement of SHR rely on the interaction with SIEL
CC (PubMed:25124761). {ECO:0000269|PubMed:16640459,
CC ECO:0000269|PubMed:17446396, ECO:0000269|PubMed:17785527,
CC ECO:0000269|PubMed:18500650, ECO:0000269|PubMed:21924907,
CC ECO:0000269|PubMed:25124761, ECO:0000269|PubMed:28211915}.
CC -!- INTERACTION:
CC Q9SZF7; Q9M384: SCR; NbExp=11; IntAct=EBI-1250472, EBI-1250484;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11565032,
CC ECO:0000269|PubMed:15498493, ECO:0000269|PubMed:25124761}. Nucleus
CC {ECO:0000269|PubMed:11565032, ECO:0000269|PubMed:15498493,
CC ECO:0000269|PubMed:25124761}. Early endosome
CC {ECO:0000269|PubMed:25124761}. Late endosome
CC {ECO:0000269|PubMed:25124761}. Recycling endosome
CC {ECO:0000269|PubMed:25124761}. Note=Cytoplasm and nucleus in the stele
CC (PubMed:11565032, PubMed:15498493). Restricted to the nucleus in
CC adjacent cells (PubMed:11565032, PubMed:15498493). Localization to
CC endosomes promotes the intercellular movement of SHR (PubMed:25124761).
CC {ECO:0000269|PubMed:11565032, ECO:0000269|PubMed:15498493,
CC ECO:0000269|PubMed:25124761}.
CC -!- TISSUE SPECIFICITY: Expressed in the stele and the quiescent center.
CC Not detected in the ground tissue cell lineage. The SHR protein moves
CC from the stele to a single layer of adjacent cells, where it enters the
CC nucleus. {ECO:0000269|PubMed:10850497, ECO:0000269|PubMed:11565032,
CC ECO:0000269|PubMed:15142972, ECO:0000269|PubMed:15314023}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the procambium during embryogenesis.
CC {ECO:0000269|PubMed:10850497}.
CC -!- MISCELLANEOUS: Moves via plasmodesmata from the stele into the adjacent
CC cell layer where it locates in the nucleus to controls SCR
CC transcription and endodermis specification. Intact microtubules are
CC required for cell-to-cell trafficking of SHR (PubMed:23294290). This
CC intercellular movement is dependent upon the endosome localized protein
CC SIEL (PubMed:21924907). It is necessary for normal patterning of the
CC root (PubMed:19000160). {ECO:0000269|PubMed:19000160,
CC ECO:0000269|PubMed:21924907, ECO:0000269|PubMed:23294290}.
CC -!- SIMILARITY: Belongs to the GRAS family. {ECO:0000255|PROSITE-
CC ProRule:PRU01191}.
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DR EMBL; AF233752; AAF75234.1; -; Genomic_DNA.
DR EMBL; AL035605; CAB38304.1; -; Genomic_DNA.
DR EMBL; AL161591; CAB80430.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86820.1; -; Genomic_DNA.
DR EMBL; BT033026; ACE62894.1; -; mRNA.
DR EMBL; AY074547; AAL69513.1; -; mRNA.
DR PIR; T04722; T04722.
DR RefSeq; NP_195480.1; NM_119928.3.
DR PDB; 5B3G; X-ray; 2.00 A; B=59-531.
DR PDB; 5B3H; X-ray; 2.70 A; B/E=112-531.
DR PDBsum; 5B3G; -.
DR PDBsum; 5B3H; -.
DR AlphaFoldDB; Q9SZF7; -.
DR SMR; Q9SZF7; -.
DR BioGRID; 15200; 3.
DR IntAct; Q9SZF7; 6.
DR STRING; 3702.AT4G37650.1; -.
DR PaxDb; Q9SZF7; -.
DR PRIDE; Q9SZF7; -.
DR ProteomicsDB; 232977; -.
DR EnsemblPlants; AT4G37650.1; AT4G37650.1; AT4G37650.
DR GeneID; 829919; -.
DR Gramene; AT4G37650.1; AT4G37650.1; AT4G37650.
DR KEGG; ath:AT4G37650; -.
DR Araport; AT4G37650; -.
DR TAIR; locus:2120106; AT4G37650.
DR eggNOG; ENOG502QQN4; Eukaryota.
DR HOGENOM; CLU_011924_5_1_1; -.
DR InParanoid; Q9SZF7; -.
DR OMA; HRMMKEI; -.
DR OrthoDB; 709637at2759; -.
DR PhylomeDB; Q9SZF7; -.
DR PRO; PR:Q9SZF7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZF7; baseline and differential.
DR Genevisible; Q9SZF7; AT.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0008356; P:asymmetric cell division; IMP:TAIR.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IMP:TAIR.
DR GO; GO:0009956; P:radial pattern formation; IMP:TAIR.
DR GO; GO:0032350; P:regulation of hormone metabolic process; NAS:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR005202; TF_GRAS.
DR PANTHER; PTHR31636; PTHR31636; 1.
DR Pfam; PF03514; GRAS; 1.
DR PROSITE; PS50985; GRAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; Endosome; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..531
FT /note="Protein SHORT-ROOT"
FT /id="PRO_0000329423"
FT DOMAIN 134..529
FT /note="GRAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 14..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..206
FT /note="Leucine repeat I (LRI)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 225..290
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 310..343
FT /note="Leucine repeat II (LRII)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 353..449
FT /note="PFYRE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 452..529
FT /note="SAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 256..260
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT COMPBIAS 71..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 166
FT /note="L->G: Impaired SCR binding (10 percent); when
FT associated with G-167."
FT /evidence="ECO:0000269|PubMed:28211915"
FT MUTAGEN 167
FT /note="W->G: Reduced SCR binding (30 percent). Impaired SCR
FT binding (5-10 percent); when associated with A-176 or G-
FT 166."
FT /evidence="ECO:0000269|PubMed:28211915"
FT MUTAGEN 170
FT /note="N->A: Reduced SCR binding (50 percent); when
FT associated with A-171."
FT /evidence="ECO:0000269|PubMed:28211915"
FT MUTAGEN 171
FT /note="E->A: Reduced SCR binding (55 percent). Reduced SCR
FT binding (50 percent); when associated with A-170."
FT /evidence="ECO:0000269|PubMed:28211915"
FT MUTAGEN 176
FT /note="Y->A: Reduced SCR binding (50 percent). Impaired SCR
FT binding (5 percent); when associated with G-167."
FT /evidence="ECO:0000269|PubMed:28211915"
FT MUTAGEN 289
FT /note="T->I,E: Loss of both export from the stele and
FT activity."
FT /evidence="ECO:0000269|PubMed:15498493"
FT MUTAGEN 342..347
FT /note="LNELDV->AAA: No effect on activity, but loss of
FT movment into the endodermis and reduction in the nuclear
FT localization in the stele."
FT /evidence="ECO:0000269|PubMed:19000160"
FT MUTAGEN 436
FT /note="R->A: Reduced SCR binding (50 percent); when
FT associated with A-441."
FT /evidence="ECO:0000269|PubMed:28211915"
FT MUTAGEN 441
FT /note="R->A: Reduced SCR binding (75 percent). Reduced SCR
FT binding (50 percent); when associated with A-436."
FT /evidence="ECO:0000269|PubMed:28211915"
FT CONFLICT 233
FT /note="P -> S (in Ref. 4; AAL69513)"
FT /evidence="ECO:0000305"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 142..156
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 159..172
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 179..195
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 216..231
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:5B3G"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 285..294
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 301..322
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 326..335
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 370..380
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 405..428
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 434..452
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 465..474
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 484..494
FT /evidence="ECO:0007829|PDB:5B3G"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 508..517
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 520..530
FT /evidence="ECO:0007829|PDB:5B3G"
SQ SEQUENCE 531 AA; 59462 MW; F43EEC5F7AA0CA1C CRC64;
MDTLFRLVSL QQQQQSDSII TNQSSLSRTS TTTTGSPQTA YHYNFPQNDV VEECFNFFMD
EEDLSSSSSH HNHHNHNNPN TYYSPFTTPT QYHPATSSTP SSTAAAAALA SPYSSSGHHN
DPSAFSIPQT PPSFDFSANA KWADSVLLEA ARAFSDKDTA RAQQILWTLN ELSSPYGDTE
QKLASYFLQA LFNRMTGSGE RCYRTMVTAA ATEKTCSFES TRKTVLKFQE VSPWATFGHV
AANGAILEAV DGEAKIHIVD ISSTFCTQWP TLLEALATRS DDTPHLRLTT VVVANKFVND
QTASHRMMKE IGNRMEKFAR LMGVPFKFNI IHHVGDLSEF DLNELDVKPD EVLAINCVGA
MHGIASRGSP RDAVISSFRR LRPRIVTVVE EEADLVGEEE GGFDDEFLRG FGECLRWFRV
CFESWEESFP RTSNERLMLE RAAGRAIVDL VACEPSDSTE RRETARKWSR RMRNSGFGAV
GYSDEVADDV RALLRRYKEG VWSMVQCPDA AGIFLCWRDQ PVVWASAWRP T
