TMK3_ARATH
ID TMK3_ARATH Reviewed; 943 AA.
AC Q9SIT1;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Receptor-like kinase TMK3 {ECO:0000303|PubMed:23613767};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=BARK1-like kinase 2 {ECO:0000303|PubMed:23921992};
DE AltName: Full=Leucine-rich repeat receptor-like kinases TMK3 {ECO:0000303|PubMed:23613767};
DE AltName: Full=Transmembrane kinase 3 {ECO:0000303|PubMed:23613767};
DE Flags: Precursor;
GN Name=TMK3 {ECO:0000303|PubMed:23613767};
GN Synonyms=BLK2 {ECO:0000303|PubMed:23921992};
GN OrderedLocusNames=At2g01820 {ECO:0000312|Araport:AT2G01820};
GN ORFNames=T23K3.1 {ECO:0000312|EMBL:AAD21776.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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).
CC {ECO:0000269|PubMed:23613767}.
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 -!- INTERACTION:
CC Q9SIT1; Q9M9S4: At1g14390; NbExp=2; IntAct=EBI-16896864, EBI-16954682;
CC Q9SIT1; Q9SHI2: At1g17230; NbExp=4; IntAct=EBI-16896864, EBI-20651261;
CC Q9SIT1; Q9SH71: At1g64210; NbExp=2; IntAct=EBI-16896864, EBI-20651385;
CC Q9SIT1; Q9M9C5: At1g68400; NbExp=4; IntAct=EBI-16896864, EBI-1238661;
CC Q9SIT1; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-16896864, EBI-20651541;
CC Q9SIT1; Q8W4S5: At5g63710; NbExp=3; IntAct=EBI-16896864, EBI-16934827;
CC Q9SIT1; Q9LJY0: PRK4; NbExp=2; IntAct=EBI-16896864, EBI-16914444;
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. {ECO:0000269|PubMed:23613767}.
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). Tmk1 and
CC tmk3 double mutants, tmk2 and tmk3 double mutants, tmk3 and tmk4 double
CC mutants, tmk1, tmk2 and tmk3 triple mutants and tmk2, tmk3 and tmk4
CC triple mutants have no visible phenotypes (PubMed:23613767). Tmk1, tmk3
CC 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; FJ708686; ACN59281.1; -; mRNA.
DR EMBL; AC007069; AAD21776.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05504.1; -; Genomic_DNA.
DR PIR; E84429; E84429.
DR RefSeq; NP_178291.1; NM_126243.4.
DR PDB; 7BRC; X-ray; 2.06 A; A=25-482.
DR PDBsum; 7BRC; -.
DR AlphaFoldDB; Q9SIT1; -.
DR SMR; Q9SIT1; -.
DR IntAct; Q9SIT1; 35.
DR STRING; 3702.AT2G01820.1; -.
DR iPTMnet; Q9SIT1; -.
DR SwissPalm; Q9SIT1; -.
DR PaxDb; Q9SIT1; -.
DR PRIDE; Q9SIT1; -.
DR ProteomicsDB; 232607; -.
DR EnsemblPlants; AT2G01820.1; AT2G01820.1; AT2G01820.
DR GeneID; 814713; -.
DR Gramene; AT2G01820.1; AT2G01820.1; AT2G01820.
DR KEGG; ath:AT2G01820; -.
DR Araport; AT2G01820; -.
DR TAIR; locus:2059703; AT2G01820.
DR eggNOG; ENOG502QPQ4; Eukaryota.
DR HOGENOM; CLU_000288_114_6_1; -.
DR OMA; DMAHIVN; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9SIT1; -.
DR PRO; PR:Q9SIT1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIT1; baseline and differential.
DR Genevisible; Q9SIT1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
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:0009555; P:pollen development; IMP:TAIR.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 2.
DR Pfam; PF00069; Pkinase; 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 3D-structure; ATP-binding; Disulfide bond; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..943
FT /note="Receptor-like kinase TMK3"
FT /id="PRO_0000433431"
FT TOPO_DOM 25..482
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..943
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 64..88
FT /note="LRR 1"
FT /evidence="ECO:0000305"
FT REPEAT 89..111
FT /note="LRR 2"
FT /evidence="ECO:0000305"
FT REPEAT 112..134
FT /note="LRR 3"
FT /evidence="ECO:0000305"
FT REPEAT 136..160
FT /note="LRR 4"
FT /evidence="ECO:0000305"
FT REPEAT 162..183
FT /note="LRR 5"
FT /evidence="ECO:0000305"
FT REPEAT 186..210
FT /note="LRR 6"
FT /evidence="ECO:0000305"
FT REPEAT 212..232
FT /note="LRR 7"
FT /evidence="ECO:0000305"
FT REPEAT 233..254
FT /note="LRR 8"
FT /evidence="ECO:0000305"
FT REPEAT 255..279
FT /note="LRR 9"
FT /evidence="ECO:0000305"
FT REPEAT 281..301
FT /note="LRR 10"
FT /evidence="ECO:0000305"
FT REPEAT 363..386
FT /note="LRR 11"
FT /evidence="ECO:0000305"
FT REPEAT 387..410
FT /note="LRR 12"
FT /evidence="ECO:0000305"
FT REPEAT 411..438
FT /note="LRR 13"
FT /evidence="ECO:0000305"
FT DOMAIN 585..866
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 441..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 714
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 591..599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 54..61
FT /evidence="ECO:0000250|UniProtKB:P43298"
FT DISULFID 315..323
FT /evidence="ECO:0000250|UniProtKB:P43298"
FT DISULFID 353..361
FT /evidence="ECO:0000250|UniProtKB:P43298"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:7BRC"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:7BRC"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:7BRC"
FT TURN 129..134
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:7BRC"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:7BRC"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:7BRC"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:7BRC"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:7BRC"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:7BRC"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:7BRC"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:7BRC"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:7BRC"
FT HELIX 382..386
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 397..402
FT /evidence="ECO:0007829|PDB:7BRC"
FT HELIX 406..410
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:7BRC"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:7BRC"
SQ SEQUENCE 943 AA; 101959 MW; EBD1CC31F4C9BB68 CRC64;
MSNSHLGTLC FIISLLGLAN FSLSQTGLDD STMQSLKSSL NLTSDVDWSN PNPCKWQSVQ
CDGSNRVTKI QLKQKGIRGT LPTNLQSLSE LVILELFLNR ISGPIPDLSG LSRLQTLNLH
DNLFTSVPKN LFSGMSSLQE MYLENNPFDP WVIPDTVKEA TSLQNLTLSN CSIIGKIPDF
FGSQSLPSLT NLKLSQNGLE GELPMSFAGT SIQSLFLNGQ KLNGSISVLG NMTSLVEVSL
QGNQFSGPIP DLSGLVSLRV FNVRENQLTG VVPQSLVSLS SLTTVNLTNN YLQGPTPLFG
KSVGVDIVNN MNSFCTNVAG EACDPRVDTL VSVAESFGYP VKLAESWKGN NPCVNWVGIT
CSGGNITVVN MRKQDLSGTI SPSLAKLTSL ETINLADNKL SGHIPDELTT LSKLRLLDVS
NNDFYGIPPK FRDTVTLVTE GNANMGKNGP NKTSDAPGAS PGSKPSGGSD GSETSKKSSN
VKIIVPVVGG VVGALCLVGL GVCLYAKKRK RPARVQSPSS NMVIHPHHSG DNDDIKLTVA
ASSLNSGGGS DSYSHSGSAA SDIHVVEAGN LVISIQVLRN VTNNFSEENI LGRGGFGTVY
KGELHDGTKI AVKRMESSVV SDKGLTEFKS EITVLTKMRH RHLVALLGYC LDGNERLLVY
EYMPQGTLSQ HLFHWKEEGR KPLDWTRRLA IALDVARGVE YLHTLAHQSF IHRDLKPSNI
LLGDDMRAKV SDFGLVRLAP DGKYSIETRV AGTFGYLAPE YAVTGRVTTK VDIFSLGVIL
MELITGRKAL DETQPEDSVH LVTWFRRVAA SKDENAFKNA IDPNISLDDD TVASIEKVWE
LAGHCCAREP YQRPDMAHIV NVLSSLTVQW KPTETDPDDV YGIDYDMPLP QVLKKWQAFE
GLSQTADDSG SSSSAYGSKD NTQTSIPTRP SGFADSFTSV DGR
