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C0LGT1 (Y5129_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 48. 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

Names and origin

Protein namesRecommended name:
Probable LRR receptor-like serine/threonine-protein kinase At5g10290

EC=2.7.11.1
Gene names
Ordered Locus Names:At5g10290
ORF Names:F18D22.60
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length613 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subcellular location

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

Sequence similarities

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

Contains 4 LRR (leucine-rich) repeats.

Contains 1 protein kinase domain.

Sequence caution

The sequence CAB96685.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 613582Probable LRR receptor-like serine/threonine-protein kinase At5g10290
PRO_0000387560

Regions

Topological domain32 – 225194Extracellular Potential
Transmembrane226 – 24621Helical; Potential
Topological domain247 – 613367Cytoplasmic Potential
Repeat95 – 11723LRR 1
Repeat119 – 14123LRR 2
Repeat143 – 16624LRR 3
Repeat167 – 18923LRR 4
Domain290 – 569280Protein kinase
Nucleotide binding296 – 3049ATP By similarity

Sites

Active site4171Proton acceptor By similarity
Binding site3181ATP By similarity

Amino acid modifications

Modified residue2871Phosphothreonine By similarity
Modified residue3131Phosphothreonine By similarity
Modified residue3711Phosphoserine By similarity
Modified residue3901Phosphothreonine By similarity
Modified residue4501Phosphothreonine By similarity
Modified residue4511Phosphothreonine By similarity
Modified residue4561Phosphothreonine By similarity
Modified residue4641Phosphotyrosine By similarity
Modified residue4661Phosphoserine By similarity
Modified residue4671Phosphothreonine By similarity
Modified residue4711Phosphoserine By similarity
Modified residue5471Phosphothreonine By similarity
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1551N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict5371E → G in AAM13028. Ref.3

Sequences

Sequence LengthMass (Da)Tools
C0LGT1 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: B71BE8151BA387B7

FASTA61368,659
        10         20         30         40         50         60 
MRMFSLQKMA MAFTLLFFAC LCSFVSPDAQ GDALFALRIS LRALPNQLSD WNQNQVNPCT 

        70         80         90        100        110        120 
WSQVICDDKN FVTSLTLSDM NFSGTLSSRV GILENLKTLT LKGNGITGEI PEDFGNLTSL 

       130        140        150        160        170        180 
TSLDLEDNQL TGRIPSTIGN LKKLQFLTLS RNKLNGTIPE SLTGLPNLLN LLLDSNSLSG 

       190        200        210        220        230        240 
QIPQSLFEIP KYNFTSNNLN CGGRQPHPCV SAVAHSGDSS KPKTGIIAGV VAGVTVVLFG 

       250        260        270        280        290        300 
ILLFLFCKDR HKGYRRDVFV DVAGEVDRRI AFGQLKRFAW RELQLATDNF SEKNVLGQGG 

       310        320        330        340        350        360 
FGKVYKGVLP DNTKVAVKRL TDFESPGGDA AFQREVEMIS VAVHRNLLRL IGFCTTQTER 

       370        380        390        400        410        420 
LLVYPFMQNL SLAHRLREIK AGDPVLDWET RKRIALGAAR GFEYLHEHCN PKIIHRDVKA 

       430        440        450        460        470        480 
ANVLLDEDFE AVVGDFGLAK LVDVRRTNVT TQVRGTMGHI APEYLSTGKS SERTDVFGYG 

       490        500        510        520        530        540 
IMLLELVTGQ RAIDFSRLEE EDDVLLLDHV KKLEREKRLG AIVDKNLDGE YIKEEVEMMI 

       550        560        570        580        590        600 
QVALLCTQGS PEDRPVMSEV VRMLEGEGLA ERWEEWQNVE VTRRHEFERL QRRFDWGEDS 

       610 
MHNQDAIELS GGR 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [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]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL360334 Genomic DNA. Translation: CAB96685.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED91517.1.
AY093029 mRNA. Translation: AAM13028.1.
FJ708775 mRNA. Translation: ACN59366.1.
PIRT50817.
RefSeqNP_196591.2. NM_121067.3.
UniGeneAt.6000.

3D structure databases

ProteinModelPortalC0LGT1.
SMRC0LGT1. Positions 28-183, 238-580.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid16171. 1 interaction.

Proteomic databases

PaxDbC0LGT1.
PRIDEC0LGT1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G10290.1; AT5G10290.1; AT5G10290.
GeneID830893.
KEGGath:AT5G10290.

Organism-specific databases

GeneFarm507. 46.
TAIRAT5G10290.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000116554.
InParanoidQ8RWK7.
OMAREFKPGE.
PhylomeDBC0LGT1.
ProtClustDBCLSN2690145.

Enzyme and pathway databases

BioCycARA:AT5G10290-MONOMER.

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_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00560. LRR_1. 1 hit.
PF12799. LRR_4. 1 hit.
PF08263. LRRNT_2. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 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 nameY5129_ARATH
AccessionPrimary (citable) accession number: C0LGT1
Secondary accession number(s): Q8RWK7, Q9LFT7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 48 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