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C0LGF4 (FEI1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 49. 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·Alt products·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 FEI 1

EC=2.7.11.1
Gene names
Name:FEI1
Ordered Locus Names:At1g31420
ORF Names:T8E3.2
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the signaling pathway that regulates cell wall function, including cellulose biosynthesis, likely via an 1-aminocyclopropane-1-carboxylic acid (ACC)-mediated signal (a precursor of ethylene). Ref.4

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with the ACC synthases ACS5 and ACS9 but not ACS2, via the kinase domain. Ref.4

Subcellular location

Cell membrane; Single-pass type I membrane protein Ref.4.

Tissue specificity

Expressed in the root meristem and elongation zone, and in hypocotyls of etiolated seedlings. Ref.4

Post-translational modification

Autophosphorylated.

Disruption phenotype

No visible phenotype. Fei1 and fei2 double mutants exhibit disrupted anisotropic expansion (e.g. during hypocotyl elongation), impaired synthesis of cell wall polymers, and abnormal cellulose biosynthesis. Ref.4

Miscellaneous

'Fei' means fat in Chinese.

Sequence similarities

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

Contains 5 LRR (leucine-rich) repeats.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAG51266.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: C0LGF4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 591562LRR receptor-like serine/threonine-protein kinase FEI 1
PRO_0000387511

Regions

Topological domain30 – 238209Extracellular Potential
Transmembrane239 – 25921Helical; Potential
Topological domain260 – 591332Cytoplasmic Potential
Repeat73 – 9725LRR 1
Repeat98 – 12124LRR 2
Repeat123 – 14523LRR 3
Repeat146 – 16924LRR 4
Repeat171 – 19424LRR 5
Domain306 – 578273Protein kinase
Nucleotide binding312 – 3209ATP By similarity

Sites

Active site4291Proton acceptor By similarity
Binding site3341ATP By similarity

Amino acid modifications

Modified residue3861Phosphoserine By similarity
Modified residue4621Phosphothreonine By similarity
Modified residue4631Phosphothreonine By similarity
Modified residue4681Phosphothreonine By similarity
Modified residue4761Phosphotyrosine By similarity
Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation1201N-linked (GlcNAc...) Potential
Glycosylation1761N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis3341K → R: Loss of kinase activity, normal interaction with ACC synthases. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: EA57944B55157D91

FASTA59164,916
        10         20         30         40         50         60 
MMGICEMKSC CSWLLLISLL CSLSNESQAI SPDGEALLSF RNAVTRSDSF IHQWRPEDPD 

        70         80         90        100        110        120 
PCNWNGVTCD AKTKRVITLN LTYHKIMGPL PPDIGKLDHL RLLMLHNNAL YGAIPTALGN 

       130        140        150        160        170        180 
CTALEEIHLQ SNYFTGPIPA EMGDLPGLQK LDMSSNTLSG PIPASLGQLK KLSNFNVSNN 

       190        200        210        220        230        240 
FLVGQIPSDG VLSGFSKNSF IGNLNLCGKH VDVVCQDDSG NPSSHSQSGQ NQKKNSGKLL 

       250        260        270        280        290        300 
ISASATVGAL LLVALMCFWG CFLYKKLGKV EIKSLAKDVG GGASIVMFHG DLPYSSKDII 

       310        320        330        340        350        360 
KKLEMLNEEH IIGCGGFGTV YKLAMDDGKV FALKRILKLN EGFDRFFERE LEILGSIKHR 

       370        380        390        400        410        420 
YLVNLRGYCN SPTSKLLLYD YLPGGSLDEA LHERGEQLDW DSRVNIIIGA AKGLSYLHHD 

       430        440        450        460        470        480 
CSPRIIHRDI KSSNILLDGN LEARVSDFGL AKLLEDEESH ITTIVAGTFG YLAPEYMQSG 

       490        500        510        520        530        540 
RATEKTDVYS FGVLVLEVLS GKRPTDASFI EKGLNVVGWL KFLISEKRPR DIVDPNCEGM 

       550        560        570        580        590 
QMESLDALLS IATQCVSPSP EERPTMHRVV QLLESEVMTP CPSEFYDSSS D 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(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]"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]"Two leucine-rich repeat receptor kinases mediate signaling, linking cell wall biosynthesis and ACC synthase in Arabidopsis."
Xu S.-L., Rahman A., Baskin T.I., Kieber J.J.
Plant Cell 20:3065-3079(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-334, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, INTERACTION WITH ACS5 AND ACS9.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC027135 Genomic DNA. Translation: AAG51266.1. Different initiation.
CP002684 Genomic DNA. Translation: AEE31354.1.
FJ708643 mRNA. Translation: ACN59239.1.
PIRB86440.
RefSeqNP_001185122.1. NM_001198193.1. [C0LGF4-1]
UniGeneAt.27683.
At.67250.

3D structure databases

ProteinModelPortalC0LGF4.
SMRC0LGF4. Positions 33-208, 263-575.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G31420.1-P.

Proteomic databases

PRIDEC0LGF4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G31420.2; AT1G31420.2; AT1G31420. [C0LGF4-1]
GeneID840032.
KEGGath:AT1G31420.

Organism-specific databases

GeneFarm2555. 221.
TAIRAT1G31420.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000116554.
InParanoidQ9C867.
PhylomeDBC0LGF4.

Enzyme and pathway databases

BioCycARA:AT1G31420-MONOMER.
ARA:GQT-1631-MONOMER.

Gene expression databases

ArrayExpressC0LGF4.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR013210. LRR-contain_N2.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00560. LRR_1. 1 hit.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 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 nameFEI1_ARATH
AccessionPrimary (citable) accession number: C0LGF4
Secondary accession number(s): Q9C867
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: May 5, 2009
Last modified: June 11, 2014
This is version 49 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