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Protein

LRR receptor-like serine/threonine-protein kinase GSO1

Gene

GSO1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Together with GSO2, receptor-like serine/threonine-kinase required during the development of the epidermal surface in embryos and cotyledons (PubMed:18088309). In coordination with GSO2, regulates root growth through control of cell division and cell fate specification. Controls seedling root growth by modulating sucrose response after germination (PubMed:24123341). Receptor of the peptide hormones CIF1 and CIF2 required for contiguous Casparian strip diffusion barrier formation in roots (PubMed:28104889). Required for localizing CASP proteins into the Casparian strip following an uninterrupted, ring-like domain, to trigger endodermal differentiation and thus regulate potassium ion (K) homeostasis. Involved in the maintenance of water transport and root pressure. May also be involved in the regulation of suberin accumulation in the endodermis (PubMed:25233277).4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei979ATPPROSITE-ProRule annotation1
Active sitei1084Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi957 – 965ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

  • embryo development ending in seed dormancy Source: TAIR
  • endodermal cell differentiation Source: UniProtKB
  • establishment of protein localization Source: UniProtKB
  • plant epidermis development Source: TAIR
  • potassium ion homeostasis Source: UniProtKB
  • regulation of cell division Source: UniProtKB
  • regulation of cell fate specification Source: UniProtKB
  • regulation of endodermal cell differentiation Source: UniProtKB
  • regulation of root development Source: UniProtKB
  • regulation of root morphogenesis Source: UniProtKB
  • response to wounding Source: UniProtKB
  • specification of plant organ axis polarity Source: UniProtKB
  • water homeostasis Source: UniProtKB
  • water transport Source: UniProtKB

Keywordsi

Molecular functionDevelopmental protein, Kinase, Receptor, Serine/threonine-protein kinase, Transferase
Biological processCell wall biogenesis/degradation
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
LRR receptor-like serine/threonine-protein kinase GSO11 Publication (EC:2.7.11.1PROSITE-ProRule annotation)
Alternative name(s):
Protein GASSHO 11 Publication
Protein SCHENGEN 31 Publication
Gene namesi
Name:GSO11 Publication
Synonyms:SGN31 Publication
Ordered Locus Names:At4g20140Imported
ORF Names:F1C12.60Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRilocus:2120362. AT4G20140.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 876ExtracellularSequence analysisAdd BLAST858
Transmembranei877 – 897HelicalSequence analysisAdd BLAST21
Topological domaini898 – 1249CytoplasmicSequence analysisAdd BLAST352

GO - Cellular componenti

  • Casparian strip Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: TAIR

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Dramatic defect in endodermal barrier formation leading to altered potassium ion (K) homeostasis and hypersensitivity to low potassium conditions. Casparian strips are repeatedly interrupted, forming irregularly-sized holes of several micrometer in length, probably due to abnormal CASP proteins patterning. Suppresses the enhanced suberin production when combined to other Casparian strip-defective mutants such as esb1 and casp1 casp3. Extremely sensitive to changes in environmental conditions such as high temperatures and under long-day (LD) conditions leading to dwarf plants. Normal transpiration but altered water transport and root pressure (PubMed:25233277). No visible phenotype during embryogenesis and seedling development. Gso1 and gso2 double mutants produce slightly contorted seeds, with abnormally shaped embryos and seedlings; adhesion between cotyledons and the peripheral tissue of the endosperm, short hypocotyl, and concave cotyledons sometimes fused, with compressed epidermal cells, endosperm tissue partially adherent to the surface of the cotyledons, and a rough surface. In addition, seedlings of gso1 gso2 have also root growth and patterning defects characterized by abnormal numbers of cells in longitudinal files and radial cell layers, as well as aberrant stem cell division planes. Root growth arrest and cell divisions defects are rescued by exogenous application of sucrose, but not patterning defects (PubMed:24123341). The double mutant gso1 gso2 exhibits a repeatedly interrupted, discontinuous Casparian strip due to patch-like localization of the CASPs proteins as a result of partial fusion of individual CASP containing islands in the Casparian strip membrane domain (CSD) (PubMed:28104889).4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi160P → L in sgn3-5; altered CASP proteins localization in Casparian strips. 1 Publication1
Mutagenesisi287G → R in sgn3-8; altered CASP proteins localization in Casparian strips; when associated with R-1101. 1 Publication1
Mutagenesisi719G → R in sgn3-12; altered CASP proteins localization in Casparian strips; when associated with E-1150. 1 Publication1
Mutagenesisi1101G → R in sgn3-8; altered CASP proteins localization in Casparian strips; when associated with R-287. 1 Publication1
Mutagenesisi1150G → E in sgn3-18; altered CASP proteins localization in Casparian strips. In sgn3-12; altered CASP proteins localization in Casparian strips; when associated with R-719. 1 Publication1
Mutagenesisi1150G → R in sgn3-17; altered CASP proteins localization in Casparian strips. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000038751319 – 1249LRR receptor-like serine/threonine-protein kinase GSO1Add BLAST1231

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi77N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi117N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi213N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi228N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi248N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi298N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi309N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi334N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi369N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi393N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi406N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi454N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi537N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi553N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi558N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi565N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi693N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi708N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi779N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi822N-linked (GlcNAc...)PROSITE-ProRule annotation1
Modified residuei948PhosphothreonineBy similarity1
Modified residuei1027PhosphotyrosineBy similarity1
Modified residuei1071PhosphotyrosineBy similarity1
Modified residuei1129PhosphotyrosineBy similarity1
Modified residuei1136PhosphotyrosineBy similarity1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiC0LGQ5.

Expressioni

Tissue specificityi

Mostly expressed in siliques, seeds, developing embryos and seedlings, detected in flower buds and roots, but not in leaves or stems.1 Publication

Developmental stagei

In flower buds, localized in filaments and stigmas. During embryogenesis, uniform expression from the globular embryo to the mature cotyledonary embryo. After germination, detected in whole cotyledons and in the hypocotyl. During the 6 first days after germination (DAG), highly expressed in roots throughout the elongation zone (EZ) and differentiation zone, but restricted to the endodermis and vasculature. Accumulates progressively in the quiescent center (QC). Down-regulated at sites of lateral root primordia (LRP) initiation. Absent at sites of deliberate wounding in the root. Mostly observed in the inner layers of the mature root, the QC and shoot apical meristem (SAM) (PubMed:24123341). Expressed early during endodermal differentiation, shortly after the onset of endodermal cells elongation (PubMed:25233277).3 Publications

Inductioni

Repressed by wounding.1 Publication

Gene expression databases

GenevisibleiC0LGQ5. AT.

Interactioni

Subunit structurei

Interacts with CIF1 and CIF2.1 Publication

Protein-protein interaction databases

BioGridi13052. 12 interactors.
STRINGi3702.AT4G20140.1.

Structurei

3D structure databases

ProteinModelPortaliC0LGQ5.
SMRiC0LGQ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati94 – 118LRR 1Sequence analysisAdd BLAST25
Repeati119 – 142LRR 2Sequence analysisAdd BLAST24
Repeati144 – 166LRR 3Sequence analysisAdd BLAST23
Repeati168 – 190LRR 4Sequence analysisAdd BLAST23
Repeati191 – 214LRR 5Sequence analysisAdd BLAST24
Repeati216 – 238LRR 6Sequence analysisAdd BLAST23
Repeati239 – 262LRR 7Sequence analysisAdd BLAST24
Repeati264 – 285LRR 8Sequence analysisAdd BLAST22
Repeati286 – 310LRR 9Sequence analysisAdd BLAST25
Repeati312 – 334LRR 10Sequence analysisAdd BLAST23
Repeati336 – 359LRR 11Sequence analysisAdd BLAST24
Repeati360 – 383LRR 12Sequence analysisAdd BLAST24
Repeati385 – 407LRR 13Sequence analysisAdd BLAST23
Repeati408 – 431LRR 14Sequence analysisAdd BLAST24
Repeati433 – 455LRR 15Sequence analysisAdd BLAST23
Repeati457 – 479LRR 16Sequence analysisAdd BLAST23
Repeati480 – 503LRR 17Sequence analysisAdd BLAST24
Repeati505 – 527LRR 18Sequence analysisAdd BLAST23
Repeati528 – 551LRR 19Sequence analysisAdd BLAST24
Repeati553 – 574LRR 20Sequence analysisAdd BLAST22
Repeati576 – 598LRR 21Sequence analysisAdd BLAST23
Repeati599 – 622LRR 22Sequence analysisAdd BLAST24
Repeati623 – 646LRR 23Sequence analysisAdd BLAST24
Repeati648 – 670LRR 24Sequence analysisAdd BLAST23
Repeati671 – 694LRR 25Sequence analysisAdd BLAST24
Repeati696 – 718LRR 26Sequence analysisAdd BLAST23
Repeati719 – 742LRR 27Sequence analysisAdd BLAST24
Repeati744 – 766LRR 28Sequence analysisAdd BLAST23
Repeati767 – 791LRR 29Sequence analysisAdd BLAST25
Repeati792 – 815LRR 30Sequence analysisAdd BLAST24
Repeati817 – 838LRR 31Sequence analysisAdd BLAST22
Domaini951 – 1240Protein kinasePROSITE-ProRule annotationAdd BLAST290

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IJJK. Eukaryota.
COG0515. LUCA.
COG4886. LUCA.
HOGENOMiHOG000116551.
InParanoidiC0LGQ5.
OMAiEVNCTAF.
OrthoDBiEOG093600QC.
PhylomeDBiC0LGQ5.

Family and domain databases

Gene3Di3.80.10.10. 6 hits.
InterProiView protein in InterPro
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR013210. LRR_N_plant-typ.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF00560. LRR_1. 2 hits.
PF13855. LRR_8. 4 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
SMARTiView protein in SMART
SM00369. LRR_TYP. 16 hits.
SM00220. S_TKc. 1 hit.
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

C0LGQ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPLVLLLLF ILCFSGLGQP GIINNDLQTL LEVKKSLVTN PQEDDPLRQW
60 70 80 90 100
NSDNINYCSW TGVTCDNTGL FRVIALNLTG LGLTGSISPW FGRFDNLIHL
110 120 130 140 150
DLSSNNLVGP IPTALSNLTS LESLFLFSNQ LTGEIPSQLG SLVNIRSLRI
160 170 180 190 200
GDNELVGDIP ETLGNLVNLQ MLALASCRLT GPIPSQLGRL VRVQSLILQD
210 220 230 240 250
NYLEGPIPAE LGNCSDLTVF TAAENMLNGT IPAELGRLEN LEILNLANNS
260 270 280 290 300
LTGEIPSQLG EMSQLQYLSL MANQLQGLIP KSLADLGNLQ TLDLSANNLT
310 320 330 340 350
GEIPEEFWNM SQLLDLVLAN NHLSGSLPKS ICSNNTNLEQ LVLSGTQLSG
360 370 380 390 400
EIPVELSKCQ SLKQLDLSNN SLAGSIPEAL FELVELTDLY LHNNTLEGTL
410 420 430 440 450
SPSISNLTNL QWLVLYHNNL EGKLPKEISA LRKLEVLFLY ENRFSGEIPQ
460 470 480 490 500
EIGNCTSLKM IDMFGNHFEG EIPPSIGRLK ELNLLHLRQN ELVGGLPASL
510 520 530 540 550
GNCHQLNILD LADNQLSGSI PSSFGFLKGL EQLMLYNNSL QGNLPDSLIS
560 570 580 590 600
LRNLTRINLS HNRLNGTIHP LCGSSSYLSF DVTNNGFEDE IPLELGNSQN
610 620 630 640 650
LDRLRLGKNQ LTGKIPWTLG KIRELSLLDM SSNALTGTIP LQLVLCKKLT
660 670 680 690 700
HIDLNNNFLS GPIPPWLGKL SQLGELKLSS NQFVESLPTE LFNCTKLLVL
710 720 730 740 750
SLDGNSLNGS IPQEIGNLGA LNVLNLDKNQ FSGSLPQAMG KLSKLYELRL
760 770 780 790 800
SRNSLTGEIP VEIGQLQDLQ SALDLSYNNF TGDIPSTIGT LSKLETLDLS
810 820 830 840 850
HNQLTGEVPG SVGDMKSLGY LNVSFNNLGG KLKKQFSRWP ADSFLGNTGL
860 870 880 890 900
CGSPLSRCNR VRSNNKQQGL SARSVVIISA ISALTAIGLM ILVIALFFKQ
910 920 930 940 950
RHDFFKKVGH GSTAYTSSSS SSQATHKPLF RNGASKSDIR WEDIMEATHN
960 970 980 990 1000
LSEEFMIGSG GSGKVYKAEL ENGETVAVKK ILWKDDLMSN KSFSREVKTL
1010 1020 1030 1040 1050
GRIRHRHLVK LMGYCSSKSE GLNLLIYEYM KNGSIWDWLH EDKPVLEKKK
1060 1070 1080 1090 1100
KLLDWEARLR IAVGLAQGVE YLHHDCVPPI VHRDIKSSNV LLDSNMEAHL
1110 1120 1130 1140 1150
GDFGLAKVLT ENCDTNTDSN TWFACSYGYI APEYAYSLKA TEKSDVYSMG
1160 1170 1180 1190 1200
IVLMEIVTGK MPTDSVFGAE MDMVRWVETH LEVAGSARDK LIDPKLKPLL
1210 1220 1230 1240
PFEEDAACQV LEIALQCTKT SPQERPSSRQ ACDSLLHVYN NRTAGYKKL
Length:1,249
Mass (Da):137,288
Last modified:May 5, 2009 - v1
Checksum:i9B4C4928C8A10E95
GO

Sequence cautioni

The sequence CAA18239 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAB79014 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL022224 Genomic DNA. Translation: CAA18239.1. Sequence problems.
AL161552 Genomic DNA. Translation: CAB79014.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84279.1.
FJ708746 mRNA. Translation: ACN59340.1.
PIRiT05322.
RefSeqiNP_193747.2. NM_118133.3.
UniGeneiAt.2179.
At.22288.

Genome annotation databases

EnsemblPlantsiAT4G20140.1; AT4G20140.1; AT4G20140.
GeneIDi827760.
GrameneiAT4G20140.1; AT4G20140.1; AT4G20140.
KEGGiath:AT4G20140.

Cross-referencesi

Web resourcesi

PlantP kinase Classification PPC

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL022224 Genomic DNA. Translation: CAA18239.1. Sequence problems.
AL161552 Genomic DNA. Translation: CAB79014.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84279.1.
FJ708746 mRNA. Translation: ACN59340.1.
PIRiT05322.
RefSeqiNP_193747.2. NM_118133.3.
UniGeneiAt.2179.
At.22288.

3D structure databases

ProteinModelPortaliC0LGQ5.
SMRiC0LGQ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi13052. 12 interactors.
STRINGi3702.AT4G20140.1.

Proteomic databases

PaxDbiC0LGQ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G20140.1; AT4G20140.1; AT4G20140.
GeneIDi827760.
GrameneiAT4G20140.1; AT4G20140.1; AT4G20140.
KEGGiath:AT4G20140.

Organism-specific databases

AraportiAT4G20140.
TAIRilocus:2120362. AT4G20140.

Phylogenomic databases

eggNOGiENOG410IJJK. Eukaryota.
COG0515. LUCA.
COG4886. LUCA.
HOGENOMiHOG000116551.
InParanoidiC0LGQ5.
OMAiEVNCTAF.
OrthoDBiEOG093600QC.
PhylomeDBiC0LGQ5.

Miscellaneous databases

PROiPR:C0LGQ5.

Gene expression databases

GenevisibleiC0LGQ5. AT.

Family and domain databases

Gene3Di3.80.10.10. 6 hits.
InterProiView protein in InterPro
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR013210. LRR_N_plant-typ.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF00560. LRR_1. 2 hits.
PF13855. LRR_8. 4 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
SMARTiView protein in SMART
SM00369. LRR_TYP. 16 hits.
SM00220. S_TKc. 1 hit.
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGSO1_ARATH
AccessioniPrimary (citable) accession number: C0LGQ5
Secondary accession number(s): Q9SN91
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: May 5, 2009
Last modified: April 12, 2017
This is version 70 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.