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Protein

Protein SCARECROW

Gene

SCR

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Transcription factor required for quiescent center cells specification and maintenance of surrounding stem cells, and for the asymmetric cell division involved in radial pattern formation in roots. Essential for cell division but not differentiation of the ground tissue. Also required for normal shoot gravitropism. Regulates the radial organization of the shoot axial organs. Binds to the promoter of MGP, NUC, RLK and SCL3. Restricts SHR movment and sequesters it into the nucleus of the endodermis.11 Publications

GO - Molecular functioni

  • DNA binding transcription factor activity Source: TAIR
  • sequence-specific DNA binding Source: TAIR

GO - Biological processi

  • asymmetric cell division Source: TAIR
  • bundle sheath cell fate specification Source: TAIR
  • gravitropism Source: TAIR
  • leaf development Source: TAIR
  • maintenance of protein location in nucleus Source: TAIR
  • radial pattern formation Source: TAIR
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionDevelopmental protein
Biological processTranscription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SCARECROW
Short name:
AtSCR
Alternative name(s):
GRAS family protein 20
Short name:
AtGRAS-20
Protein SHOOT GRAVITROPISM 1
Gene namesi
Name:SCR
Synonyms:SGR1
Ordered Locus Names:At3g54220
ORF Names:F24B22.180
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

AraportiAT3G54220
TAIRilocus:2080345 AT3G54220

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Plants have a greatly reduced root length and only a single cell layer between the epidermis and the pericycle. The sgrl-1 mutant has no gravitropic response either in inflorescence stems or in hypocotyls.4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi295 – 299LQCAE → AQCAA: Abolishes interaction with RBR1. 2 Publications5
Mutagenesisi490 – 653Missing in scr-3/sgr1-1; loss of shoot gravitropism. 1 PublicationAdd BLAST164

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003294151 – 653Protein SCARECROWAdd BLAST653

Proteomic databases

PaxDbiQ9M384

Expressioni

Tissue specificityi

Expressed in siliques, leaves and roots. Detected in the initial daughter cell before its asymmetric division and remains expressed only in the endodermal cell layer after the division. Expressed in the endodermis or starch sheath of the seedling hypocotyl, in the leaf bundle sheath cells and the root quiescent center.5 Publications

Developmental stagei

Detected in the ground tissue of late heart-stage embryos. After germination, expressed also in the L1 layer throughout the shoot apical meristem including the peripheral zone. Detected in most tissues of young leaf primordia, except in the presumptive vasculature. In mature leaves, expressed in bundle sheath cells. Detected in inflorescence stems in a single internal cell layer corresponding to the starch sheath.2 Publications

Inductioni

Up-regulated by SHR and by itself.3 Publications

Gene expression databases

ExpressionAtlasiQ9M384 baseline and differential
GenevisibleiQ9M384 AT

Interactioni

Subunit structurei

Interacts with SHR, JKD and MGP (PubMed:16640459, PubMed:17446396, PubMed:17785527, PubMed:18500650). Interacts with SIEL (PubMed:21924907). Interacts with RBR1 through its the LxCxE motif (PubMed:22921914, PubMed:24302889).7 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi9906, 7 interactors
IntActiQ9M384, 27 interactors
STRINGi3702.AT3G54220.1

Structurei

Secondary structure

1653
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi283 – 302Combined sources20
Helixi306 – 319Combined sources14
Helixi326 – 347Combined sources22
Helixi355 – 357Combined sources3
Helixi360 – 376Combined sources17
Helixi379 – 394Combined sources16
Turni395 – 397Combined sources3
Beta strandi399 – 405Combined sources7
Helixi414 – 422Combined sources9
Beta strandi430 – 436Combined sources7
Helixi440 – 457Combined sources18
Beta strandi461 – 466Combined sources6
Helixi470 – 472Combined sources3
Helixi475 – 478Combined sources4
Beta strandi485 – 491Combined sources7
Beta strandi494 – 496Combined sources3
Beta strandi499 – 501Combined sources3
Helixi502 – 512Combined sources11
Beta strandi515 – 524Combined sources10
Beta strandi526 – 528Combined sources3
Helixi530 – 551Combined sources22
Helixi557 – 565Combined sources9
Helixi567 – 575Combined sources9
Turni577 – 582Combined sources6
Helixi591 – 597Combined sources7
Beta strandi600 – 603Combined sources4
Helixi608 – 617Combined sources10
Beta strandi625 – 630Combined sources6
Beta strandi633 – 638Combined sources6
Beta strandi641 – 651Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5B3GX-ray2.00A274-653[»]
5B3HX-ray2.70A/D275-653[»]
ProteinModelPortaliQ9M384
SMRiQ9M384
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini281 – 650GRASPROSITE-ProRule annotationAdd BLAST370

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni288 – 351Leucine repeat I (LRI)PROSITE-ProRule annotationAdd BLAST64
Regioni370 – 435VHIIDPROSITE-ProRule annotationAdd BLAST66
Regioni445 – 477Leucine repeat II (LRII)PROSITE-ProRule annotationAdd BLAST33
Regioni486 – 573PFYREPROSITE-ProRule annotationAdd BLAST88
Regioni576 – 650SAWPROSITE-ProRule annotationAdd BLAST75

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili262 – 289Sequence analysisAdd BLAST28

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi295 – 299LxCxE motifPROSITE-ProRule annotation2 Publications5
Motifi401 – 405VHIIDPROSITE-ProRule annotation5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi12 – 40Pro-richAdd BLAST29
Compositional biasi22 – 28Poly-Ser7
Compositional biasi132 – 138Poly-Ser7
Compositional biasi194 – 197Poly-Ser4
Compositional biasi218 – 240Gln-richAdd BLAST23
Compositional biasi232 – 236Poly-Pro5

Sequence similaritiesi

Belongs to the GRAS family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IIRY Eukaryota
ENOG4110TCK LUCA
HOGENOMiHOG000238577
InParanoidiQ9M384
OMAiTAWIDSI
OrthoDBiEOG09360409
PhylomeDBiQ9M384

Family and domain databases

InterProiView protein in InterPro
IPR005202 TF_GRAS
PfamiView protein in Pfam
PF03514 GRAS, 1 hit
PROSITEiView protein in PROSITE
PS50985 GRAS, 1 hit

Sequencei

Sequence statusi: Complete.

Q9M384-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAESGDFNGG QPPPHSPLRT TSSGSSSSNN RGPPPPPPPP LVMVRKRLAS
60 70 80 90 100
EMSSNPDYNN SSRPPRRVSH LLDSNYNTVT PQQPPSLTAA ATVSSQPNPP
110 120 130 140 150
LSVCGFSGLP VFPSDRGGRN VMMSVQPMDQ DSSSSSASPT VWVDAIIRDL
160 170 180 190 200
IHSSTSVSIP QLIQNVRDII FPCNPNLGAL LEYRLRSLML LDPSSSSDPS
210 220 230 240 250
PQTFEPLYQI SNNPSPPQQQ QQHQQQQQQH KPPPPPIQQQ ERENSSTDAP
260 270 280 290 300
PQPETVTATV PAVQTNTAEA LRERKEEIKR QKQDEEGLHL LTLLLQCAEA
310 320 330 340 350
VSADNLEEAN KLLLEISQLS TPYGTSAQRV AAYFSEAMSA RLLNSCLGIY
360 370 380 390 400
AALPSRWMPQ THSLKMVSAF QVFNGISPLV KFSHFTANQA IQEAFEKEDS
410 420 430 440 450
VHIIDLDIMQ GLQWPGLFHI LASRPGGPPH VRLTGLGTSM EALQATGKRL
460 470 480 490 500
SDFADKLGLP FEFCPLAEKV GNLDTERLNV RKREAVAVHW LQHSLYDVTG
510 520 530 540 550
SDAHTLWLLQ RLAPKVVTVV EQDLSHAGSF LGRFVEAIHY YSALFDSLGA
560 570 580 590 600
SYGEESEERH VVEQQLLSKE IRNVLAVGGP SRSGEVKFES WREKMQQCGF
610 620 630 640 650
KGISLAGNAA TQATLLLGMF PSDGYTLVDD NGTLKLGWKD LSLLTASAWT

PRS
Length:653
Mass (Da):71,506
Last modified:October 1, 2000 - v1
Checksum:i009A4C48C6DA0616
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti454A → T in AAB06318 (PubMed:8756724).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62798 Genomic DNA Translation: AAB06318.1
AL132957 Genomic DNA Translation: CAB70996.1
CP002686 Genomic DNA Translation: AEE79200.1
AY056315 mRNA Translation: AAL07164.1
AY080840 mRNA Translation: AAL87315.1
AY113991 mRNA Translation: AAM45039.1
PIRiT47581
T51244
RefSeqiNP_190990.1, NM_115282.4
UniGeneiAt.71814
At.932

Genome annotation databases

EnsemblPlantsiAT3G54220.1; AT3G54220.1; AT3G54220
GeneIDi824589
GrameneiAT3G54220.1; AT3G54220.1; AT3G54220
KEGGiath:AT3G54220

Similar proteinsi

Entry informationi

Entry nameiSCR_ARATH
AccessioniPrimary (citable) accession number: Q9M384
Secondary accession number(s): Q96304
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: October 1, 2000
Last modified: April 25, 2018
This is version 110 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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