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C0LGQ9 (Y4294_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable LRR receptor-like serine/threonine-protein kinase At4g20940

EC=2.7.11.1
Gene names
Ordered Locus Names:At4g20940
ORF Names:T13K14.100
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1037 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Domain

The protein kinase domain is predicted to be catalytically inactive.

Sequence similarities

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

Contains 21 LRR (leucine-rich) repeats.

Contains 1 protein kinase domain.

Sequence caution

The sequence AEE84378.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB45889.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB79094.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 10371036Probable LRR receptor-like serine/threonine-protein kinase At4g20940
PRO_0000387555

Regions

Topological domain2 – 614613Extracellular Potential
Transmembrane615 – 63521Helical; Potential
Topological domain636 – 1037402Cytoplasmic Potential
Repeat57 – 7721LRR 1
Repeat78 – 10326LRR 2
Repeat105 – 12521LRR 3
Repeat126 – 14924LRR 4
Repeat150 – 17324LRR 5
Repeat175 – 19622LRR 6
Repeat197 – 22125LRR 7
Repeat223 – 24422LRR 8
Repeat246 – 26924LRR 9
Repeat270 – 29324LRR 10
Repeat294 – 31724LRR 11
Repeat319 – 34123LRR 12
Repeat342 – 36827LRR 13
Repeat385 – 40925LRR 14
Repeat410 – 43324LRR 15
Repeat434 – 45825LRR 16
Repeat460 – 48223LRR 17
Repeat483 – 50523LRR 18
Repeat506 – 53025LRR 19
Repeat532 – 55423LRR 20
Repeat556 – 57621LRR 21
Domain754 – 1037284Protein kinase
Nucleotide binding760 – 7689ATP By similarity

Sites

Binding site7821ATP By similarity

Amino acid modifications

Modified residue6881Phosphoserine Ref.4
Lipidation21N-myristoyl glycine Potential
Glycosylation761N-linked (GlcNAc...) Potential
Glycosylation871N-linked (GlcNAc...) Potential
Glycosylation1301N-linked (GlcNAc...) Potential
Glycosylation1371N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential
Glycosylation4161N-linked (GlcNAc...) Potential
Glycosylation5181N-linked (GlcNAc...) Potential
Glycosylation5501N-linked (GlcNAc...) Potential
Glycosylation5591N-linked (GlcNAc...) Potential
Glycosylation6051N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
C0LGQ9 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 20E81BFD1A605F7C

FASTA1,037112,042
        10         20         30         40         50         60 
MGQLPSQDIM ALLEFKKGIK HDPTGFVLNS WNDESIDFNG CPSSWNGIVC NGGNVAGVVL 

        70         80         90        100        110        120 
DNLGLTADAD FSLFSNLTKL VKLSMSNNSL SGVLPNDLGS FKSLQFLDLS DNLFSSSLPK 

       130        140        150        160        170        180 
EIGRSVSLRN LSLSGNNFSG EIPESMGGLI SLQSLDMSSN SLSGPLPKSL TRLNDLLYLN 

       190        200        210        220        230        240 
LSSNGFTGKM PRGFELISSL EVLDLHGNSI DGNLDGEFFL LTNASYVDIS GNRLVTTSGK 

       250        260        270        280        290        300 
LLPGVSESIK HLNLSHNQLE GSLTSGFQLF QNLKVLDLSY NMLSGELPGF NYVYDLEVLK 

       310        320        330        340        350        360 
LSNNRFSGSL PNNLLKGDSL LLTTLDLSGN NLSGPVSSIM STTLHTLDLS SNSLTGELPL 

       370        380        390        400        410        420 
LTGGCVLLDL SNNQFEGNLT RWSKWENIEY LDLSQNHFTG SFPDATPQLL RANHLNLSYN 

       430        440        450        460        470        480 
KLTGSLPERI PTHYPKLRVL DISSNSLEGP IPGALLSMPT LEEIHLQNNG MTGNIGPLPS 

       490        500        510        520        530        540 
SGSRIRLLDL SHNRFDGDLP GVFGSLTNLQ VLNLAANNLS GSLPSSMNDI VSLSSLDVSQ 

       550        560        570        580        590        600 
NHFTGPLPSN LSSNIMAFNV SYNDLSGTVP ENLKNFPPPS FYPGNSKLVL PAGSPGSSAS 

       610        620        630        640        650        660 
EASKNKSTNK LVKVVIIVSC AVALIILILV AILLFCICKS RRREERSITG KETNRRAQTI 

       670        680        690        700        710        720 
PSGSGGGMVV SAEDLVASRK GSSSEILSPD EKLAVATGFS PSKTSNLSWS PGSGDSFPAD 

       730        740        750        760        770        780 
QQLARLDVRS PDRLVGELHF LDDSIKLTPE ELSRAPAEVL GRSSHGTSYR ATLDNGVFLT 

       790        800        810        820        830        840 
VKWLREGVAK QRKEFAKEVK KFSNIRHPNV VTLRGYYWGP TQHEKLILSD YISPGSLASF 

       850        860        870        880        890        900 
LYDRPGRKGP PLAWTQRLKI AVDVARGLNY LHFDRAVPHG NLKATNILLD GAELNARVAD 

       910        920        930        940        950        960 
YCLHRLMTQA GTVEQILDAG ILGYRAPELA ASRKPLPSFK SDVYAFGVIL LEILTGRCAG 

       970        980        990       1000       1010       1020 
DVITGEQEGV DLTDWVRLRV AEGRGAECFD SVLTQEMGSD PVTEKGMKEV LGIALRCIRS 

      1030 
VSERPGIKTI YEDLSSI 

« 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]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL080282 Genomic DNA. Translation: CAB45889.1. Sequence problems.
AL161554 Genomic DNA. Translation: CAB79094.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84378.1. Sequence problems.
FJ708750 mRNA. Translation: ACN59344.1.
PIRT10636.
RefSeqNP_193826.2. NM_118212.2.
UniGeneAt.32683.
At.75578.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G20940.1-P.

Proteomic databases

PaxDbC0LGQ9.
PRIDEC0LGQ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID827842.
KEGGath:AT4G20940.

Organism-specific databases

GeneFarm2329. 47.
TAIRAT4G20940.

Phylogenomic databases

eggNOGNOG256848.
InParanoidQ9SUB9.
PhylomeDBC0LGQ9.

Enzyme and pathway databases

BioCycARA:AT4G20940-MONOMER.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamPF00560. LRR_1. 8 hits.
PF13855. LRR_8. 2 hits.
PF08263. LRRNT_2. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameY4294_ARATH
AccessionPrimary (citable) accession number: C0LGQ9
Secondary accession number(s): F4JIJ5, Q9SUB9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: May 5, 2009
Last modified: May 14, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names