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C0LGS3

- Y4372_ARATH

UniProt

C0LGS3 - Y4372_ARATH

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Protein

Probable LRR receptor-like serine/threonine-protein kinase At4g37250

Gene

At4g37250

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G37250-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable LRR receptor-like serine/threonine-protein kinase At4g37250 (EC:2.7.11.1)
Gene namesi
Ordered Locus Names:At4g37250
ORF Names:AP22.22, C7A10.110
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G37250.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 768747Probable LRR receptor-like serine/threonine-protein kinase At4g37250PRO_0000387558Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi212 – 2121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
Modified residuei451 – 4511PhosphoserineBy similarity
Modified residuei531 – 5311PhosphoserineBy similarity
Modified residuei553 – 5531PhosphothreonineBy similarity
Modified residuei662 – 6621PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiC0LGS3.

Interactioni

Protein-protein interaction databases

BioGridi15160. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliC0LGS3.
SMRiC0LGS3. Positions 22-322, 428-750.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 328307ExtracellularSequence AnalysisAdd
BLAST
Topological domaini350 – 768419CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei329 – 34921HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati67 – 9024LRR 1Add
BLAST
Repeati91 – 11222LRR 2Add
BLAST
Repeati115 – 13723LRR 3Add
BLAST
Repeati139 – 16224LRR 4Add
BLAST
Repeati163 – 18321LRR 5Add
BLAST
Repeati184 – 20623LRR 6Add
BLAST
Repeati207 – 22923LRR 7Add
BLAST
Repeati232 – 25423LRR 8Add
BLAST
Domaini449 – 756308Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 8 LRR (leucine-rich) repeats.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000116554.
InParanoidiC0LGS3.
OMAiYSEVELC.
PhylomeDBiC0LGS3.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_dom.
[Graphical view]
PfamiPF00560. LRR_1. 3 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

C0LGS3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRMELISVIF FFFCSVLSSS ALNSDGLVLM KFKSSVLVDP LSLLQTWNYK
60 70 80 90 100
HESPCSWRGI SCNNDSKVLT LSLPNSQLLG SIPSDLGSLL TLQSLDLSNN
110 120 130 140 150
SFNGPLPVSF FNARELRFLD LSSNMISGEI PSAIGDLHNL LTLNLSDNAL
160 170 180 190 200
AGKLPTNLAS LRNLTVVSLE NNYFSGEIPG GWRVVEFLDL SSNLINGSLP
210 220 230 240 250
PDFGGYSLQY LNVSFNQISG EIPPEIGVNF PRNVTVDLSF NNLTGPIPDS
260 270 280 290 300
PVFLNQESNF FSGNPGLCGE PTRNPCLIPS SPSIVSEADV PTSTPAIAAI
310 320 330 340 350
PNTIGSNPVT DPNSQQTDPN PRTGLRPGVI IGIVVGDIAG IGILAVIFLY
360 370 380 390 400
IYRCKKNKIV DNNNNDKQRT ETDTITLSTF SSSSSSPEES RRFRKWSCLR
410 420 430 440 450
KDPETTPSEE EDEDDEDEES GYNANQRSGD NKLVTVDGEK EMEIETLLKA
460 470 480 490 500
SAYILGATGS SIMYKAVLED GRVFAVRRLG ENGLSQRRFK DFEPHIRAIG
510 520 530 540 550
KLVHPNLVRL CGFYWGTDEK LVIYDFVPNG SLVNPRYRKG GGSSSPYHLP
560 570 580 590 600
WETRLKIAKG IARGLAYLHE KKHVHGNLKP SNILLGHDME PKIGDFGLER
610 620 630 640 650
LLTGETSYIR AGGSSRIFSS KRYTTSSREF SSIGPTPSPS PSSVGAMSPY
660 670 680 690 700
CAPESFRSLK PSPKWDVYGF GVILLELLTG KIVSVEEIVL GNGLTVEDGH
710 720 730 740 750
RAVRMADVAI RGELDGKQEF LLDCFKLGYS CASPVPQKRP TMKESLAVLE
760
RFHPNSSVIK SSSFHYGH
Length:768
Mass (Da):84,063
Last modified:May 5, 2009 - v1
Checksum:i03057CD65F6A364B
GO

Sequence cautioni

The sequence CAB16774.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAB80391.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti361 – 3611D → Y in AAN72248. (PubMed:14593172)Curated
Sequence conflicti361 – 3611D → Y in AAL57701. (PubMed:14593172)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z99707 Genomic DNA. Translation: CAB16774.1. Different initiation.
AL161591 Genomic DNA. Translation: CAB80391.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE86773.1.
AY065068 mRNA. Translation: AAL57701.1.
BT002237 mRNA. Translation: AAN72248.1.
FJ708765 mRNA. Translation: ACN59358.1.
AK317633 mRNA. Translation: BAH20295.1.
PIRiB85440.
RefSeqiNP_195442.2. NM_119888.2.
UniGeneiAt.27846.

Genome annotation databases

EnsemblPlantsiAT4G37250.1; AT4G37250.1; AT4G37250.
GeneIDi829879.
KEGGiath:AT4G37250.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z99707 Genomic DNA. Translation: CAB16774.1 . Different initiation.
AL161591 Genomic DNA. Translation: CAB80391.1 . Different initiation.
CP002687 Genomic DNA. Translation: AEE86773.1 .
AY065068 mRNA. Translation: AAL57701.1 .
BT002237 mRNA. Translation: AAN72248.1 .
FJ708765 mRNA. Translation: ACN59358.1 .
AK317633 mRNA. Translation: BAH20295.1 .
PIRi B85440.
RefSeqi NP_195442.2. NM_119888.2.
UniGenei At.27846.

3D structure databases

ProteinModelPortali C0LGS3.
SMRi C0LGS3. Positions 22-322, 428-750.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 15160. 1 interaction.

Proteomic databases

PRIDEi C0LGS3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G37250.1 ; AT4G37250.1 ; AT4G37250 .
GeneIDi 829879.
KEGGi ath:AT4G37250.

Organism-specific databases

GeneFarmi 596. 47.
TAIRi AT4G37250.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000116554.
InParanoidi C0LGS3.
OMAi YSEVELC.
PhylomeDBi C0LGS3.

Enzyme and pathway databases

BioCyci ARA:AT4G37250-MONOMER.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_dom.
[Graphical view ]
Pfami PF00560. LRR_1. 3 hits.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
    Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.
    , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
    Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. "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.
    , 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.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
    , 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.
  5. "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.
  6. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 71-768.
    Tissue: Root.

Entry informationi

Entry nameiY4372_ARATH
AccessioniPrimary (citable) accession number: C0LGS3
Secondary accession number(s): B9DHS8, O23161, Q8VZC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: May 5, 2009
Last modified: October 29, 2014
This is version 47 of the entry and version 1 of the sequence. [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

External Data

Dasty 3