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Protein

Receptor protein kinase TMK1

Gene

TMK1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Transmembrane kinase receptor (PubMed:1332795). Phosphorylates only serine and threonine residues (PubMed:8224199). Involved in auxin signal transduction and cell expansion and proliferation regulation (PubMed:23613767). Forms with ABP1 a cell surface auxin perception complex that activates ROP signaling pathways (PubMed:24578577). Required for auxin promotion of pavement cell interdigitation (PubMed:24578577). Auxin promotes the formation of the ABP1-TMK1 protein complex (PubMed:24578577).1 Publication3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Cofactori

Mn2+1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei616ATPPROSITE-ProRule annotation1
Active sitei717Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi594 – 602ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • transmembrane receptor protein serine/threonine kinase activity Source: TAIR

GO - Biological processi

  • signal transduction Source: TAIR

Keywordsi

Molecular functionKinase, Receptor, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor protein kinase TMK11 Publication (EC:2.7.11.11 Publication)
Alternative name(s):
BARK1-like kinase 11 Publication
Transmembrane kinase 11 Publication
Gene namesi
Name:TMK11 Publication
Synonyms:BLK11 Publication
Ordered Locus Names:At1g66150Imported
ORF Names:F15E12.4Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

AraportiAT1G66150
TAIRilocus:2013825 AT1G66150

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini24 – 482ExtracellularSequence analysisAdd BLAST459
Transmembranei483 – 503HelicalSequence analysisAdd BLAST21
Topological domaini504 – 942CytoplasmicSequence analysisAdd BLAST439

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype (PubMed:23613767). Tmk1 and tmk2 double mutants, tmk1 and tmk3 double mutants and tmk1, tmk2 and tmk3 triple mutants have no visible phenotypes (PubMed:23613767). Tmk1 and tmk4 double mutants, tmk1, tmk2 and tmk4 triple mutants and tmk1, tmk3 and tmk4 triple mutants have a severe reduction in organ size, a substantial delay in growth and development, and a decrease in fertility (PubMed:23613767). Tmk1, tmk2, tmk3 and tmk4 quadruple mutants are embryo lethal (PubMed:23613767, PubMed:24578577).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000002438824 – 942Receptor protein kinase TMK1Add BLAST919

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi53 ↔ 601 Publication
Glycosylationi86N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi99N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi158N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi164N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi171N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi230N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi285N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi314 ↔ 3211 Publication
Disulfide bondi351 ↔ 3591 Publication
Glycosylationi363N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi397N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Autophosphorylated on serine and threonine residues.1 Publication
Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP43298
PRIDEiP43298

PTM databases

iPTMnetiP43298

Expressioni

Tissue specificityi

Expressed in roots, leaves, stems, siliques and flowers.2 Publications

Gene expression databases

ExpressionAtlasiP43298 baseline and differential
GenevisibleiP43298 AT

Interactioni

Subunit structurei

Interacts (via extracellular domain) with ABP1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ERABP1P334873EBI-2023970,EBI-16094614

Protein-protein interaction databases

BioGridi28151, 3 interactors
DIPiDIP-46512N
IntActiP43298, 4 interactors
STRINGi3702.AT1G66150.1

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4HQ1X-ray1.55A1-469[»]
ProteinModelPortaliP43298
SMRiP43298
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati63 – 87LRR 1CuratedAdd BLAST25
Repeati88 – 110LRR 2CuratedAdd BLAST23
Repeati111 – 133LRR 3CuratedAdd BLAST23
Repeati135 – 159LRR 4CuratedAdd BLAST25
Repeati161 – 182LRR 5CuratedAdd BLAST22
Repeati185 – 209LRR 6CuratedAdd BLAST25
Repeati211 – 231LRR 7CuratedAdd BLAST21
Repeati232 – 253LRR 8CuratedAdd BLAST22
Repeati254 – 278LRR 9CuratedAdd BLAST25
Repeati280 – 300LRR 10CuratedAdd BLAST21
Repeati361 – 384LRR 11CuratedAdd BLAST24
Repeati385 – 408LRR 12CuratedAdd BLAST24
Repeati409 – 436LRR 13CuratedAdd BLAST28
Domaini588 – 869Protein kinasePROSITE-ProRule annotationAdd BLAST282

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi448 – 464Ser-richPROSITE-ProRule annotationAdd BLAST17

Domaini

The leucine-rich repeat (LRR) domain is disrupted by a non-LRR region, resulting in the formation of two LRR solenoid structures shaped like the Arabic number "7". This is strikingly different from the horseshoe structures of the canonical LRR proteins.1 Publication

Sequence similaritiesi

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410IIW7 Eukaryota
ENOG41102Z7 LUCA
HOGENOMiHOG000240631
InParanoidiP43298
KOiK00924
OMAiITVINLE
OrthoDBiEOG093601IK
PhylomeDBiP43298

Family and domain databases

Gene3Di3.80.10.10, 2 hits
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR001611 Leu-rich_rpt
IPR003591 Leu-rich_rpt_typical-subtyp
IPR032675 LRR_dom_sf
IPR013210 LRR_N_plant-typ
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF13855 LRR_8, 1 hit
PF08263 LRRNT_2, 2 hits
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00369 LRR_TYP, 5 hits
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51450 LRR, 7 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequencei

Sequence statusi: Complete.

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

P43298-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKRRTFLLF SFTFLLLLSL SKADSDGDLS AMLSLKKSLN PPSSFGWSDP
60 70 80 90 100
DPCKWTHIVC TGTKRVTRIQ IGHSGLQGTL SPDLRNLSEL ERLELQWNNI
110 120 130 140 150
SGPVPSLSGL ASLQVLMLSN NNFDSIPSDV FQGLTSLQSV EIDNNPFKSW
160 170 180 190 200
EIPESLRNAS ALQNFSANSA NVSGSLPGFL GPDEFPGLSI LHLAFNNLEG
210 220 230 240 250
ELPMSLAGSQ VQSLWLNGQK LTGDITVLQN MTGLKEVWLH SNKFSGPLPD
260 270 280 290 300
FSGLKELESL SLRDNSFTGP VPASLLSLES LKVVNLTNNH LQGPVPVFKS
310 320 330 340 350
SVSVDLDKDS NSFCLSSPGE CDPRVKSLLL IASSFDYPPR LAESWKGNDP
360 370 380 390 400
CTNWIGIACS NGNITVISLE KMELTGTISP EFGAIKSLQR IILGINNLTG
410 420 430 440 450
MIPQELTTLP NLKTLDVSSN KLFGKVPGFR SNVVVNTNGN PDIGKDKSSL
460 470 480 490 500
SSPGSSSPSG GSGSGINGDK DRRGMKSSTF IGIIVGSVLG GLLSIFLIGL
510 520 530 540 550
LVFCWYKKRQ KRFSGSESSN AVVVHPRHSG SDNESVKITV AGSSVSVGGI
560 570 580 590 600
SDTYTLPGTS EVGDNIQMVE AGNMLISIQV LRSVTNNFSS DNILGSGGFG
610 620 630 640 650
VVYKGELHDG TKIAVKRMEN GVIAGKGFAE FKSEIAVLTK VRHRHLVTLL
660 670 680 690 700
GYCLDGNEKL LVYEYMPQGT LSRHLFEWSE EGLKPLLWKQ RLTLALDVAR
710 720 730 740 750
GVEYLHGLAH QSFIHRDLKP SNILLGDDMR AKVADFGLVR LAPEGKGSIE
760 770 780 790 800
TRIAGTFGYL APEYAVTGRV TTKVDVYSFG VILMELITGR KSLDESQPEE
810 820 830 840 850
SIHLVSWFKR MYINKEASFK KAIDTTIDLD EETLASVHTV AELAGHCCAR
860 870 880 890 900
EPYQRPDMGH AVNILSSLVE LWKPSDQNPE DIYGIDLDMS LPQALKKWQA
910 920 930 940
YEGRSDLESS TSSLLPSLDN TQMSIPTRPY GFAESFTSVD GR
Length:942
Mass (Da):102,388
Last modified:November 1, 1995 - v1
Checksum:i93E300B52FF549DE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti849A → S in BAF00566 (PubMed:11130712).Curated1
Sequence conflicti849A → S in AAP04161 (PubMed:14593172).Curated1
Sequence conflicti905S → G in ACN59264 (PubMed:20064227).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00670 Genomic DNA Translation: AAA32876.1
FJ708669 mRNA Translation: ACN59264.1
AC026480 Genomic DNA Translation: AAG51302.1
CP002684 Genomic DNA Translation: AEE34468.1
BT006178 mRNA Translation: AAP04161.1
AK228659 mRNA Translation: BAF00566.1
PIRiJQ1674
RefSeqiNP_176789.1, NM_105286.4
UniGeneiAt.28076

Genome annotation databases

EnsemblPlantsiAT1G66150.1; AT1G66150.1; AT1G66150
GeneIDi842930
GrameneiAT1G66150.1; AT1G66150.1; AT1G66150
KEGGiath:AT1G66150

Similar proteinsi

Entry informationi

Entry nameiTMK1_ARATH
AccessioniPrimary (citable) accession number: P43298
Secondary accession number(s): C0LGH9, Q84R13
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 154 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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