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C0LGQ5 (GSO1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
LRR receptor-like serine/threonine-protein kinase GSO1
EC=2.7.11.1
Alternative name(s):
Protein GASSHO 1
Gene names
Name:GSO1
Ordered Locus Names:At4g20140
ORF Names:F1C12.60
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length1249 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Together with GSO2, receptor-like serine/threonine-kinase required during the development of the epidermal surface in embryos and cotyledons. Ref.4

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Mostly expressed in siliques, seeds, developing embryos and seedlings, detected in flower buds and roots, but not in leaves or stems. Ref.4

Developmental stage

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. Ref.4

Disruption phenotype

No visible effect on embryogenesis and seedling development. Double mutants gso1/gso2 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. Ref.4

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 31 LRR (leucine-rich) repeats.

Contains 1 protein kinase domain.

Sequence caution

The sequence CAA18239.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB79014.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 12491231LRR receptor-like serine/threonine-protein kinase GSO1
PRO_0000387513

Regions

Topological domain19 – 876858Extracellular Potential
Transmembrane877 – 89721Helical; Potential
Topological domain898 – 1249352Cytoplasmic Potential
Repeat94 – 11825LRR 1
Repeat119 – 14224LRR 2
Repeat144 – 16623LRR 3
Repeat168 – 19023LRR 4
Repeat191 – 21424LRR 5
Repeat216 – 23823LRR 6
Repeat239 – 26224LRR 7
Repeat264 – 28522LRR 8
Repeat286 – 31025LRR 9
Repeat312 – 33423LRR 10
Repeat336 – 35924LRR 11
Repeat360 – 38324LRR 12
Repeat385 – 40723LRR 13
Repeat408 – 43124LRR 14
Repeat433 – 45523LRR 15
Repeat457 – 47923LRR 16
Repeat480 – 50324LRR 17
Repeat505 – 52723LRR 18
Repeat528 – 55124LRR 19
Repeat553 – 57422LRR 20
Repeat576 – 59823LRR 21
Repeat599 – 62224LRR 22
Repeat623 – 64624LRR 23
Repeat648 – 67023LRR 24
Repeat671 – 69424LRR 25
Repeat696 – 71823LRR 26
Repeat719 – 74224LRR 27
Repeat744 – 76623LRR 28
Repeat767 – 79125LRR 29
Repeat792 – 81524LRR 30
Repeat817 – 83822LRR 31
Domain951 – 1240290Protein kinase
Nucleotide binding957 – 9659ATP By similarity

Sites

Active site10841Proton acceptor By similarity
Binding site9791ATP By similarity

Amino acid modifications

Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Glycosylation2481N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...) Potential
Glycosylation3091N-linked (GlcNAc...) Potential
Glycosylation3341N-linked (GlcNAc...) Potential
Glycosylation3691N-linked (GlcNAc...) Potential
Glycosylation3931N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation4541N-linked (GlcNAc...) Potential
Glycosylation5371N-linked (GlcNAc...) Potential
Glycosylation5531N-linked (GlcNAc...) Potential
Glycosylation5581N-linked (GlcNAc...) Potential
Glycosylation5651N-linked (GlcNAc...) Potential
Glycosylation6931N-linked (GlcNAc...) Potential
Glycosylation7081N-linked (GlcNAc...) Potential
Glycosylation7791N-linked (GlcNAc...) Potential
Glycosylation8221N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
C0LGQ5 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 9B4C4928C8A10E95

FASTA1,249137,288
        10         20         30         40         50         60 
MQPLVLLLLF ILCFSGLGQP GIINNDLQTL LEVKKSLVTN PQEDDPLRQW NSDNINYCSW 

        70         80         90        100        110        120 
TGVTCDNTGL FRVIALNLTG LGLTGSISPW FGRFDNLIHL DLSSNNLVGP IPTALSNLTS 

       130        140        150        160        170        180 
LESLFLFSNQ LTGEIPSQLG SLVNIRSLRI GDNELVGDIP ETLGNLVNLQ MLALASCRLT 

       190        200        210        220        230        240 
GPIPSQLGRL VRVQSLILQD NYLEGPIPAE LGNCSDLTVF TAAENMLNGT IPAELGRLEN 

       250        260        270        280        290        300 
LEILNLANNS LTGEIPSQLG EMSQLQYLSL MANQLQGLIP KSLADLGNLQ TLDLSANNLT 

       310        320        330        340        350        360 
GEIPEEFWNM SQLLDLVLAN NHLSGSLPKS ICSNNTNLEQ LVLSGTQLSG EIPVELSKCQ 

       370        380        390        400        410        420 
SLKQLDLSNN SLAGSIPEAL FELVELTDLY LHNNTLEGTL SPSISNLTNL QWLVLYHNNL 

       430        440        450        460        470        480 
EGKLPKEISA LRKLEVLFLY ENRFSGEIPQ EIGNCTSLKM IDMFGNHFEG EIPPSIGRLK 

       490        500        510        520        530        540 
ELNLLHLRQN ELVGGLPASL GNCHQLNILD LADNQLSGSI PSSFGFLKGL EQLMLYNNSL 

       550        560        570        580        590        600 
QGNLPDSLIS LRNLTRINLS HNRLNGTIHP LCGSSSYLSF DVTNNGFEDE IPLELGNSQN 

       610        620        630        640        650        660 
LDRLRLGKNQ LTGKIPWTLG KIRELSLLDM SSNALTGTIP LQLVLCKKLT HIDLNNNFLS 

       670        680        690        700        710        720 
GPIPPWLGKL SQLGELKLSS NQFVESLPTE LFNCTKLLVL SLDGNSLNGS IPQEIGNLGA 

       730        740        750        760        770        780 
LNVLNLDKNQ FSGSLPQAMG KLSKLYELRL SRNSLTGEIP VEIGQLQDLQ SALDLSYNNF 

       790        800        810        820        830        840 
TGDIPSTIGT LSKLETLDLS HNQLTGEVPG SVGDMKSLGY LNVSFNNLGG KLKKQFSRWP 

       850        860        870        880        890        900 
ADSFLGNTGL CGSPLSRCNR VRSNNKQQGL SARSVVIISA ISALTAIGLM ILVIALFFKQ 

       910        920        930        940        950        960 
RHDFFKKVGH GSTAYTSSSS SSQATHKPLF RNGASKSDIR WEDIMEATHN LSEEFMIGSG 

       970        980        990       1000       1010       1020 
GSGKVYKAEL ENGETVAVKK ILWKDDLMSN KSFSREVKTL GRIRHRHLVK LMGYCSSKSE 

      1030       1040       1050       1060       1070       1080 
GLNLLIYEYM KNGSIWDWLH EDKPVLEKKK KLLDWEARLR IAVGLAQGVE YLHHDCVPPI 

      1090       1100       1110       1120       1130       1140 
VHRDIKSSNV LLDSNMEAHL GDFGLAKVLT ENCDTNTDSN TWFACSYGYI APEYAYSLKA 

      1150       1160       1170       1180       1190       1200 
TEKSDVYSMG IVLMEIVTGK MPTDSVFGAE MDMVRWVETH LEVAGSARDK LIDPKLKPLL 

      1210       1220       1230       1240 
PFEEDAACQV LEIALQCTKT SPQERPSSRQ ACDSLLHVYN NRTAGYKKL

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-like protein kinase genes in Arabidopsis thaliana."
Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.
BMC Genomics 11:19-19(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"GASSHO1 and GASSHO2 encoding a putative leucine-rich repeat transmembrane-type receptor kinase are essential for the normal development of the epidermal surface in Arabidopsis embryos."
Tsuwamoto R., Fukuoka H., Takahata Y.
Plant J. 54:30-42(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00535203.
PIRT05322.
RefSeqNP_193747.2. NM_118133.2.
UniGeneAt.2179.
At.22288.

3D structure databases

ProteinModelPortalC0LGQ5.
SMRC0LGQ5. Positions 26-859, 903-1227.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT4G20140.1-P.

Proteomic databases

PaxDbC0LGQ5.
PRIDEC0LGQ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G20140.1; AT4G20140.1; AT4G20140.
GeneID827760.
KEGGath:AT4G20140.

Organism-specific databases

GeneFarm663. 55.
TAIRAt4g20140.

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000116551.
InParanoidQ9SN91.
OMAEDIMEAT.
PhylomeDBC0LGQ5.
ProtClustDBCLSN2687271.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR013320. ConA-like_subgrp.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00560. LRR_1. 2 hits.
PF12799. LRR_4. 1 hit.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSO1_ARATH
AccessionPrimary (citable) accession number: C0LGQ5
Secondary accession number(s): Q9SN91
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: May 5, 2009
Last modified: May 1, 2013
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents