SCR_ARATH
ID SCR_ARATH Reviewed; 653 AA.
AC Q9M384; Q96304;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein SCARECROW {ECO:0000303|PubMed:8756724};
DE Short=AtSCR {ECO:0000303|PubMed:8756724};
DE AltName: Full=GRAS family protein 20;
DE Short=AtGRAS-20;
DE AltName: Full=Protein SHOOT GRAVITROPISM 1 {ECO:0000303|PubMed:9670559};
GN Name=SCR {ECO:0000303|PubMed:8756724};
GN Synonyms=SGR1 {ECO:0000303|PubMed:9670559};
GN OrderedLocusNames=At3g54220 {ECO:0000312|Araport:AT3G54220};
GN ORFNames=F24B22.180 {ECO:0000312|EMBL:CAB70996.1};
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], DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=8756724; DOI=10.1016/s0092-8674(00)80115-4;
RA Di Laurenzio L., Wysocka-Diller J.W., Malamy J.E., Pysh L.D.,
RA Helariutta Y., Freshour G., Hahn M.G., Feldmann K.A., Benfey P.N.;
RT "The SCARECROW gene regulates an asymmetric cell division that is essential
RT for generating the radial organization of the Arabidopsis root.";
RL Cell 86:423-433(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=8819871; DOI=10.1104/pp.110.3.945;
RA Fukaki H., Fujisawa H., Tasaka M.;
RT "SGR1, SGR2, SGR3: novel genetic loci involved in shoot gravitropism in
RT Arabidopsis thaliana.";
RL Plant Physiol. 110:945-955(1996).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9375406; DOI=10.1046/j.1365-313x.1997.12040957.x;
RA Malamy J.E., Benfey P.N.;
RT "Analysis of SCARECROW expression using a rapid system for assessing
RT transgene expression in Arabidopsis roots.";
RL Plant J. 12:957-963(1997).
RN [7]
RP IDENTIFICATION, FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 490-TRP--SER-653.
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=10631180; DOI=10.1242/dev.127.3.595;
RA Wysocka-Diller J.W., Helariutta Y., Fukaki H., Malamy J.E., Benfey P.N.;
RT "Molecular analysis of SCARECROW function reveals a radial patterning
RT mechanism common to root and shoot.";
RL Development 127:595-603(2000).
RN [9]
RP INDUCTION, AND TISSUE SPECIFICITY.
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 [10]
RP INDUCTION, AND TISSUE SPECIFICITY.
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 [11]
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 [12]
RP FUNCTION.
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 [13]
RP FUNCTION, AND INDUCTION.
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 [14]
RP FUNCTION, AND INTERACTION WITH SHR.
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 [15]
RP FUNCTION, AND INTERACTION WITH SHR.
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 [16]
RP INTERACTION WITH SHR; 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 [17]
RP INTERACTION WITH SHR.
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 [18]
RP INTERACTION WITH SIEL.
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 [19]
RP FUNCTION, INTERACTION WITH RBR1, AND MUTAGENESIS OF 295-LEU--GLU-299.
RX PubMed=22921914; DOI=10.1016/j.cell.2012.07.017;
RA Cruz-Ramirez A., Diaz-Trivino S., Blilou I., Grieneisen V.A., Sozzani R.,
RA Zamioudis C., Miskolczi P., Nieuwland J., Benjamins R., Dhonukshe P.,
RA Caballero-Perez J., Horvath B., Long Y., Mahonen A.P., Zhang H., Xu J.,
RA Murray J.A., Benfey P.N., Bako L., Maree A.F., Scheres B.;
RT "A bistable circuit involving SCARECROW-RETINOBLASTOMA integrates cues to
RT inform asymmetric stem cell division.";
RL Cell 150:1002-1015(2012).
RN [20]
RP FUNCTION, INTERACTION WITH RBR1, AND MUTAGENESIS OF 295-LEU--GLU-299.
RX PubMed=24302889; DOI=10.1371/journal.pbio.1001724;
RA Cruz-Ramirez A., Diaz-Trivino S., Wachsman G., Du Y., Arteaga-Vazquez M.,
RA Zhang H., Benjamins R., Blilou I., Neef A.B., Chandler V., Scheres B.;
RT "A SCARECROW-RETINOBLASTOMA protein network controls protective quiescence
RT in the Arabidopsis root stem cell organizer.";
RL PLoS Biol. 11:E1001724-E1001724(2013).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 274-653 IN COMPLEX WITH SHR AND
RP JKD, AND INTERACTION WITH SHR.
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 cell division but not differentiation of the ground
CC tissue. Also required for normal shoot gravitropism. Regulates the
CC radial organization of the shoot axial organs. Binds to the promoter of
CC MGP, NUC, RLK and SCL3. Restricts SHR movment and sequesters it into
CC the nucleus of the endodermis. {ECO:0000269|PubMed:10631180,
CC ECO:0000269|PubMed:12569126, ECO:0000269|PubMed:15142972,
CC ECO:0000269|PubMed:15314023, ECO:0000269|PubMed:16640459,
CC ECO:0000269|PubMed:17446396, ECO:0000269|PubMed:22921914,
CC ECO:0000269|PubMed:24302889, ECO:0000269|PubMed:8819871,
CC ECO:0000269|PubMed:9375406, ECO:0000269|PubMed:9670559}.
CC -!- SUBUNIT: Interacts with SHR, JKD and MGP (PubMed:16640459,
CC PubMed:17446396, PubMed:17785527, PubMed:18500650, PubMed:28211915).
CC Interacts with SIEL (PubMed:21924907). Interacts with RBR1 through its
CC the LxCxE motif (PubMed:22921914, PubMed:24302889).
CC {ECO:0000269|PubMed:16640459, ECO:0000269|PubMed:17446396,
CC ECO:0000269|PubMed:17785527, ECO:0000269|PubMed:18500650,
CC ECO:0000269|PubMed:21924907, ECO:0000269|PubMed:22921914,
CC ECO:0000269|PubMed:24302889, ECO:0000269|PubMed:28211915}.
CC -!- INTERACTION:
CC Q9M384; Q9C6I4: GA2OX7; NbExp=3; IntAct=EBI-1250484, EBI-25513059;
CC Q9M384; Q9ZWA6: MGP; NbExp=3; IntAct=EBI-1250484, EBI-1568600;
CC Q9M384; Q9LKZ3: RBR1; NbExp=4; IntAct=EBI-1250484, EBI-398590;
CC Q9M384; Q9SZF7: SHR; NbExp=11; IntAct=EBI-1250484, EBI-1250472;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in siliques, leaves and roots. Detected
CC in the initial daughter cell before its asymmetric division and remains
CC expressed only in the endodermal cell layer after the division.
CC Expressed in the endodermis or starch sheath of the seedling hypocotyl,
CC in the leaf bundle sheath cells and the root quiescent center.
CC {ECO:0000269|PubMed:10631180, ECO:0000269|PubMed:10850497,
CC ECO:0000269|PubMed:11565032, ECO:0000269|PubMed:8756724,
CC ECO:0000269|PubMed:9375406}.
CC -!- DEVELOPMENTAL STAGE: Detected in the ground tissue of late heart-stage
CC embryos. After germination, expressed also in the L1 layer throughout
CC the shoot apical meristem including the peripheral zone. Detected in
CC most tissues of young leaf primordia, except in the presumptive
CC vasculature. In mature leaves, expressed in bundle sheath cells.
CC Detected in inflorescence stems in a single internal cell layer
CC corresponding to the starch sheath. {ECO:0000269|PubMed:10631180,
CC ECO:0000269|PubMed:8756724}.
CC -!- INDUCTION: Up-regulated by SHR and by itself.
CC {ECO:0000269|PubMed:10850497, ECO:0000269|PubMed:11565032,
CC ECO:0000269|PubMed:15314023}.
CC -!- DISRUPTION PHENOTYPE: Plants have a greatly reduced root length and
CC only a single cell layer between the epidermis and the pericycle. The
CC sgrl-1 mutant has no gravitropic response either in inflorescence stems
CC or in hypocotyls. {ECO:0000269|PubMed:10631180,
CC ECO:0000269|PubMed:8756724, ECO:0000269|PubMed:8819871,
CC ECO:0000269|PubMed:9670559}.
CC -!- SIMILARITY: Belongs to the GRAS family. {ECO:0000255|PROSITE-
CC ProRule:PRU01191}.
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DR EMBL; U62798; AAB06318.1; -; Genomic_DNA.
DR EMBL; AL132957; CAB70996.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79200.1; -; Genomic_DNA.
DR EMBL; AY056315; AAL07164.1; -; mRNA.
DR EMBL; AY080840; AAL87315.1; -; mRNA.
DR EMBL; AY113991; AAM45039.1; -; mRNA.
DR PIR; T47581; T47581.
DR PIR; T51244; T51244.
DR RefSeq; NP_190990.1; NM_115282.4.
DR PDB; 5B3G; X-ray; 2.00 A; A=274-653.
DR PDB; 5B3H; X-ray; 2.70 A; A/D=275-653.
DR PDBsum; 5B3G; -.
DR PDBsum; 5B3H; -.
DR AlphaFoldDB; Q9M384; -.
DR SMR; Q9M384; -.
DR BioGRID; 9906; 15.
DR IntAct; Q9M384; 28.
DR STRING; 3702.AT3G54220.1; -.
DR PaxDb; Q9M384; -.
DR PRIDE; Q9M384; -.
DR ProteomicsDB; 232886; -.
DR EnsemblPlants; AT3G54220.1; AT3G54220.1; AT3G54220.
DR GeneID; 824589; -.
DR Gramene; AT3G54220.1; AT3G54220.1; AT3G54220.
DR KEGG; ath:AT3G54220; -.
DR Araport; AT3G54220; -.
DR TAIR; locus:2080345; AT3G54220.
DR eggNOG; ENOG502QTMY; Eukaryota.
DR HOGENOM; CLU_011924_7_1_1; -.
DR InParanoid; Q9M384; -.
DR OMA; MEIQTGA; -.
DR OrthoDB; 772613at2759; -.
DR PhylomeDB; Q9M384; -.
DR PRO; PR:Q9M384; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M384; baseline and differential.
DR Genevisible; Q9M384; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0008356; P:asymmetric cell division; IMP:TAIR.
DR GO; GO:0090610; P:bundle sheath cell fate specification; IMP:TAIR.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:TAIR.
DR GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IGI:TAIR.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IMP:TAIR.
DR GO; GO:0009956; P:radial pattern formation; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0048364; P:root development; IGI:TAIR.
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; Developmental protein; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..653
FT /note="Protein SCARECROW"
FT /id="PRO_0000329415"
FT DOMAIN 281..650
FT /note="GRAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..351
FT /note="Leucine repeat I (LRI)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 370..435
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 445..477
FT /note="Leucine repeat II (LRII)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 486..573
FT /note="PFYRE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 576..650
FT /note="SAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 295..299
FT /note="LxCxE motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 401..405
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT COMPBIAS 14..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 295..299
FT /note="LQCAE->AQCAA: Abolishes interaction with RBR1."
FT /evidence="ECO:0000269|PubMed:22921914,
FT ECO:0000269|PubMed:24302889"
FT MUTAGEN 490..653
FT /note="Missing: In scr-3/sgr1-1; loss of shoot
FT gravitropism."
FT /evidence="ECO:0000269|PubMed:9670559"
FT CONFLICT 454
FT /note="A -> T (in Ref. 1; AAB06318)"
FT /evidence="ECO:0000305"
FT HELIX 283..302
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 326..347
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 360..376
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 379..394
FT /evidence="ECO:0007829|PDB:5B3G"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 399..405
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 430..436
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 440..457
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 485..491
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 502..512
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 515..524
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 530..551
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 557..565
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 567..575
FT /evidence="ECO:0007829|PDB:5B3G"
FT TURN 577..582
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 591..597
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 600..603
FT /evidence="ECO:0007829|PDB:5B3G"
FT HELIX 608..617
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 625..630
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 633..638
FT /evidence="ECO:0007829|PDB:5B3G"
FT STRAND 641..651
FT /evidence="ECO:0007829|PDB:5B3G"
SQ SEQUENCE 653 AA; 71506 MW; 009A4C48C6DA0616 CRC64;
MAESGDFNGG QPPPHSPLRT TSSGSSSSNN RGPPPPPPPP LVMVRKRLAS EMSSNPDYNN
SSRPPRRVSH LLDSNYNTVT PQQPPSLTAA ATVSSQPNPP LSVCGFSGLP VFPSDRGGRN
VMMSVQPMDQ DSSSSSASPT VWVDAIIRDL IHSSTSVSIP QLIQNVRDII FPCNPNLGAL
LEYRLRSLML LDPSSSSDPS PQTFEPLYQI SNNPSPPQQQ QQHQQQQQQH KPPPPPIQQQ
ERENSSTDAP PQPETVTATV PAVQTNTAEA LRERKEEIKR QKQDEEGLHL LTLLLQCAEA
VSADNLEEAN KLLLEISQLS TPYGTSAQRV AAYFSEAMSA RLLNSCLGIY AALPSRWMPQ
THSLKMVSAF QVFNGISPLV KFSHFTANQA IQEAFEKEDS VHIIDLDIMQ GLQWPGLFHI
LASRPGGPPH VRLTGLGTSM EALQATGKRL SDFADKLGLP FEFCPLAEKV GNLDTERLNV
RKREAVAVHW LQHSLYDVTG SDAHTLWLLQ RLAPKVVTVV EQDLSHAGSF LGRFVEAIHY
YSALFDSLGA SYGEESEERH VVEQQLLSKE IRNVLAVGGP SRSGEVKFES WREKMQQCGF
KGISLAGNAA TQATLLLGMF PSDGYTLVDD NGTLKLGWKD LSLLTASAWT PRS
