TMK4_ARATH
ID TMK4_ARATH Reviewed; 928 AA.
AC Q9LK43; C0LGN6;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Receptor-like kinase TMK4 {ECO:0000303|PubMed:23613767};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=BAK1-associating receptor-like kinase 1 {ECO:0000303|PubMed:23921992};
DE AltName: Full=Leucine-rich repeat receptor-like kinases TMK4 {ECO:0000303|PubMed:23613767};
DE AltName: Full=Transmembrane kinase 4 {ECO:0000303|PubMed:23613767};
DE Flags: Precursor;
GN Name=TMK4 {ECO:0000303|PubMed:23613767};
GN Synonyms=BARK1 {ECO:0000303|PubMed:23921992};
GN OrderedLocusNames=At3g23750 {ECO:0000312|Araport:AT3G23750};
GN ORFNames=MYM9.9 {ECO:0000312|EMBL:BAB01851.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP GENE FAMILY.
RX PubMed=12972053; DOI=10.1016/s1369-5266(03)00089-x;
RA Dievart A., Clark S.E.;
RT "Using mutant alleles to determine the structure and function of leucine-
RT rich repeat receptor-like kinases.";
RL Curr. Opin. Plant Biol. 6:507-516(2003).
RN [5]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=23613767; DOI=10.1371/journal.pone.0060990;
RA Dai N., Wang W., Patterson S.E., Bleecker A.B.;
RT "The TMK subfamily of receptor-like kinases in Arabidopsis display an
RT essential role in growth and a reduced sensitivity to auxin.";
RL PLoS ONE 8:E60990-E60990(2013).
RN [6]
RP FUNCTION, INTERACTION WITH BAK1; SERK4 AND SERK5, TISSUE SPECIFICITY,
RP INDUCTION BY HORMONES, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=23921992; DOI=10.1093/pcp/pct106;
RA Kim M.H., Kim Y., Kim J.W., Lee H.S., Lee W.S., Kim S.K., Wang Z.Y.,
RA Kim S.H.;
RT "Identification of Arabidopsis BAK1-associating receptor-like kinase 1
RT (BARK1) and characterization of its gene expression and brassinosteroid-
RT regulated root phenotypes.";
RL Plant Cell Physiol. 54:1620-1634(2013).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=24578577; DOI=10.1126/science.1245125;
RA Xu T., Dai N., Chen J., Nagawa S., Cao M., Li H., Zhou Z., Chen X.,
RA De Rycke R., Rakusova H., Wang W., Jones A.M., Friml J., Patterson S.E.,
RA Bleecker A.B., Yang Z.;
RT "Cell surface ABP1-TMK auxin-sensing complex activates ROP GTPase
RT signaling.";
RL Science 343:1025-1028(2014).
CC -!- FUNCTION: Involved in auxin signal transduction and cell expansion and
CC proliferation regulation (PubMed:23613767). May be involved in
CC brassinosteroid-mediated plant growth and development via auxin
CC regulation (PubMed:23921992). May be involved in microspore and pollen
CC development (PubMed:23921992). {ECO:0000269|PubMed:23613767,
CC ECO:0000269|PubMed:23921992}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with BAK1 (via kinase domain), SERK4 and SERK5.
CC {ECO:0000269|PubMed:23921992}.
CC -!- INTERACTION:
CC Q9LK43; Q9LT96: At5g49770; NbExp=4; IntAct=EBI-20664575, EBI-17123993;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, siliques and
CC flowers (PubMed:23613767). Ubiquitous, with a high expression in mature
CC pollen grains and in the pericycle and the xylem vasculature of the
CC primary and lateral roots (PubMed:23921992).
CC {ECO:0000269|PubMed:23613767, ECO:0000269|PubMed:23921992}.
CC -!- INDUCTION: Initially up-regulated by exogenous auxin or brassinosteroid
CC but down-regulated after a prolonged treatment. Down-regulated by
CC abscisic acid, gibberellic acid or cytokinin.
CC {ECO:0000269|PubMed:23921992}.
CC -!- DOMAIN: The leucine-rich repeat (LRR) domain is disrupted by a non-LRR
CC region, resulting in the formation of two LRR solenoid structures
CC shaped like the Arabic number '7'. This is strikingly different from
CC the horseshoe structures of the canonical LRR proteins.
CC {ECO:0000250|UniProtKB:P43298}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:23613767). Tmk2 and
CC tmk4 double mutants, tmk3 and tmk4 double mutants and tmk2, tmk3 and
CC tmk4 triple mutants have no visible phenotypes (PubMed:23613767). Tmk1
CC and tmk4 double mutants, tmk1, tmk2 and tmk4 triple mutants and tmk1,
CC tmk3 and tmk4 triple mutants have a severe reduction in organ size, a
CC substantial delay in growth and development, and a decrease in
CC fertility (PubMed:23613767). Tmk1, tmk2, tmk3 and tmk4 quadruple
CC mutants are embryo lethal (PubMed:23613767, PubMed:24578577).
CC {ECO:0000269|PubMed:23613767, ECO:0000269|PubMed:24578577}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; FJ708726; ACN59321.1; -; mRNA.
DR EMBL; AP000377; BAB01851.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76809.1; -; Genomic_DNA.
DR RefSeq; NP_189017.1; NM_113279.3.
DR AlphaFoldDB; Q9LK43; -.
DR SMR; Q9LK43; -.
DR IntAct; Q9LK43; 18.
DR STRING; 3702.AT3G23750.1; -.
DR iPTMnet; Q9LK43; -.
DR PaxDb; Q9LK43; -.
DR PRIDE; Q9LK43; -.
DR ProteomicsDB; 228453; -.
DR EnsemblPlants; AT3G23750.1; AT3G23750.1; AT3G23750.
DR GeneID; 821957; -.
DR Gramene; AT3G23750.1; AT3G23750.1; AT3G23750.
DR KEGG; ath:AT3G23750; -.
DR Araport; AT3G23750; -.
DR TAIR; locus:2095188; AT3G23750.
DR eggNOG; ENOG502QPZR; Eukaryota.
DR HOGENOM; CLU_000288_114_6_1; -.
DR InParanoid; Q9LK43; -.
DR OMA; FDWQENG; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LK43; -.
DR PRO; PR:Q9LK43; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK43; baseline and differential.
DR Genevisible; Q9LK43; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Disulfide bond; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..928
FT /note="Receptor-like kinase TMK4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433432"
FT TOPO_DOM 25..472
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..928
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 61..84
FT /note="LRR 1"
FT /evidence="ECO:0000305"
FT REPEAT 85..107
FT /note="LRR 2"
FT /evidence="ECO:0000305"
FT REPEAT 108..130
FT /note="LRR 3"
FT /evidence="ECO:0000305"
FT REPEAT 132..157
FT /note="LRR 4"
FT /evidence="ECO:0000305"
FT REPEAT 158..180
FT /note="LRR 5"
FT /evidence="ECO:0000305"
FT REPEAT 181..205
FT /note="LRR 6"
FT /evidence="ECO:0000305"
FT REPEAT 207..229
FT /note="LRR 7"
FT /evidence="ECO:0000305"
FT REPEAT 230..251
FT /note="LRR 8"
FT /evidence="ECO:0000305"
FT REPEAT 252..276
FT /note="LRR 9"
FT /evidence="ECO:0000305"
FT REPEAT 278..298
FT /note="LRR 10"
FT /evidence="ECO:0000305"
FT REPEAT 360..383
FT /note="LRR 11"
FT /evidence="ECO:0000305"
FT REPEAT 384..407
FT /note="LRR 12"
FT /evidence="ECO:0000305"
FT REPEAT 408..435
FT /note="LRR 13"
FT /evidence="ECO:0000305"
FT DOMAIN 578..858
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 445..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 707
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 584..592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 51..58
FT /evidence="ECO:0000250|UniProtKB:P43298"
FT DISULFID 310..318
FT /evidence="ECO:0000250|UniProtKB:P43298"
FT DISULFID 348..356
FT /evidence="ECO:0000250|UniProtKB:P43298"
FT CONFLICT 607
FT /note="R -> G (in Ref. 1; ACN59321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 928 AA; 99964 MW; 13BB63639060B412 CRC64;
MEAPTPLLLL VLLTTITFFT TSVADDQTAM LALAKSFNPP PSDWSSTTDF CKWSGVRCTG
GRVTTISLAD KSLTGFIAPE ISTLSELKSV SIQRNKLSGT IPSFAKLSSL QEIYMDENNF
VGVETGAFAG LTSLQILSLS DNNNITTWSF PSELVDSTSL TTIYLDNTNI AGVLPDIFDS
LASLQNLRLS YNNITGVLPP SLGKSSIQNL WINNQDLGMS GTIEVLSSMT SLSQAWLHKN
HFFGPIPDLS KSENLFDLQL RDNDLTGIVP PTLLTLASLK NISLDNNKFQ GPLPLFSPEV
KVTIDHNVFC TTKAGQSCSP QVMTLLAVAG GLGYPSMLAE SWQGDDACSG WAYVSCDSAG
KNVVTLNLGK HGFTGFISPA IANLTSLKSL YLNGNDLTGV IPKELTFMTS LQLIDVSNNN
LRGEIPKFPA TVKFSYKPGN ALLGTNGGDG SSPGTGGASG GPGGSSGGGG SKVGVIVGVI
VAVLVFLAIL GFVVYKFVMK RKYGRFNRTD PEKVGKILVS DAVSNGGSGN GGYANGHGAN
NFNALNSPSS GDNSDRFLLE GGSVTIPMEV LRQVTNNFSE DNILGRGGFG VVYAGELHDG
TKTAVKRMEC AAMGNKGMSE FQAEIAVLTK VRHRHLVALL GYCVNGNERL LVYEYMPQGN
LGQHLFEWSE LGYSPLTWKQ RVSIALDVAR GVEYLHSLAQ QSFIHRDLKP SNILLGDDMR
AKVADFGLVK NAPDGKYSVE TRLAGTFGYL APEYAATGRV TTKVDVYAFG VVLMEILTGR
KALDDSLPDE RSHLVTWFRR ILINKENIPK ALDQTLEADE ETMESIYRVA ELAGHCTARE
PQQRPDMGHA VNVLGPLVEK WKPSCQEEEE SFGIDVNMSL PQALQRWQNE GTSSSTMFHG
DFSYSQTQSS IPPKASGFPN TFDSADGR
