TMK2_ARATH
ID TMK2_ARATH Reviewed; 886 AA.
AC Q9FYK0; Q9FXJ6;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Receptor-like kinase TMK2 {ECO:0000303|PubMed:23613767};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=BARK1-like kinase 3 {ECO:0000303|PubMed:23921992};
DE AltName: Full=Leucine-rich repeat receptor-like kinases TMK2 {ECO:0000303|PubMed:23613767};
DE AltName: Full=Transmembrane kinase 2 {ECO:0000303|PubMed:23613767};
DE Flags: Precursor;
GN Name=TMK2 {ECO:0000303|PubMed:23613767};
GN Synonyms=BLK3 {ECO:0000303|PubMed:23921992};
GN OrderedLocusNames=At1g24650 {ECO:0000312|Araport:AT1G24650};
GN ORFNames=F21J9.31 {ECO:0000312|EMBL:AAF97970.1},
GN F5A9.23 {ECO:0000312|EMBL:AAG03120.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 Q9FYK0; Q9SHI2: At1g17230; NbExp=4; IntAct=EBI-20652836, EBI-20651261;
CC Q9FYK0; Q9FZB8-2: At1g51810; NbExp=2; IntAct=EBI-20652836, EBI-20653376;
CC Q9FYK0; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-20652836, EBI-20651541;
CC Q9FYK0; A0A178UFM8: AXX17_At5g50380; NbExp=3; IntAct=EBI-20652836, EBI-20653342;
CC Q9FYK0; O65440-2: BAM3; NbExp=3; IntAct=EBI-20652836, EBI-20653325;
CC Q9FYK0; Q9LP77: RKL1; NbExp=3; IntAct=EBI-20652836, EBI-1544507;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques and flowers.
CC {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 tmk2 double mutants, tmk2 and tmk3 double mutants, tmk1, tmk2 and tmk3
CC triple mutants and tmk2, tmk3 and tmk4 triple mutants have no visible
CC phenotypes (PubMed:23613767). Tmk1, tmk2 and tmk4 triple mutants have a
CC severe reduction in organ size, a substantial delay in growth and
CC development, and a decrease in fertility (PubMed:23613767). Tmk1, tmk2,
CC tmk3 and tmk4 quadruple mutants are embryo lethal (PubMed:23613767,
CC PubMed:24578577). {ECO:0000269|PubMed:23613767,
CC ECO:0000269|PubMed:24578577}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG03120.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; FJ708636; ACN59232.1; -; mRNA.
DR EMBL; AC000103; AAF97970.1; -; Genomic_DNA.
DR EMBL; AC004133; AAG03120.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30556.1; -; Genomic_DNA.
DR RefSeq; NP_173869.1; NM_102307.1.
DR AlphaFoldDB; Q9FYK0; -.
DR SMR; Q9FYK0; -.
DR IntAct; Q9FYK0; 35.
DR STRING; 3702.AT1G24650.1; -.
DR PaxDb; Q9FYK0; -.
DR PRIDE; Q9FYK0; -.
DR EnsemblPlants; AT1G24650.1; AT1G24650.1; AT1G24650.
DR GeneID; 839079; -.
DR Gramene; AT1G24650.1; AT1G24650.1; AT1G24650.
DR KEGG; ath:AT1G24650; -.
DR Araport; AT1G24650; -.
DR TAIR; locus:2024016; AT1G24650.
DR eggNOG; ENOG502QPQ4; Eukaryota.
DR HOGENOM; CLU_000288_114_6_1; -.
DR OMA; ANQCSSR; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9FYK0; -.
DR PRO; PR:Q9FYK0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FYK0; baseline and differential.
DR Genevisible; Q9FYK0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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; 4.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..886
FT /note="Receptor-like kinase TMK2"
FT /id="PRO_0000433430"
FT TOPO_DOM 21..460
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..886
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 59..83
FT /note="LRR 1"
FT /evidence="ECO:0000305"
FT REPEAT 84..106
FT /note="LRR 2"
FT /evidence="ECO:0000305"
FT REPEAT 107..129
FT /note="LRR 3"
FT /evidence="ECO:0000305"
FT REPEAT 131..155
FT /note="LRR 4"
FT /evidence="ECO:0000305"
FT REPEAT 157..179
FT /note="LRR 5"
FT /evidence="ECO:0000305"
FT REPEAT 182..206
FT /note="LRR 6"
FT /evidence="ECO:0000305"
FT REPEAT 208..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..302
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 547..827
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 676
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 553..561
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 575
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 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 48..56
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"
SQ SEQUENCE 886 AA; 97406 MW; D3E232BD84F0E8FF CRC64;
MIAKNFLLLL CFIALVNVES SPDEAVMIAL RDSLKLSGNP NWSGSDPCKW SMFIKCDASN
RVTAIQIGDR GISGKLPPDL GKLTSLTKFE VMRNRLTGPI PSLAGLKSLV TVYANDNDFT
SVPEDFFSGL SSLQHVSLDN NPFDSWVIPP SLENATSLVD FSAVNCNLSG KIPDYLFEGK
DFSSLTTLKL SYNSLVCEFP MNFSDSRVQV LMLNGQKGRE KLHGSISFLQ KMTSLTNVTL
QGNSFSGPLP DFSGLVSLKS FNVRENQLSG LVPSSLFELQ SLSDVALGNN LLQGPTPNFT
APDIKPDLNG LNSFCLDTPG TSCDPRVNTL LSIVEAFGYP VNFAEKWKGN DPCSGWVGIT
CTGTDITVIN FKNLGLNGTI SPRFADFASL RVINLSQNNL NGTIPQELAK LSNLKTLDVS
KNRLCGEVPR FNTTIVNTTG NFEDCPNGNA GKKASSNAGK IVGSVIGILL ALLLIGVAIF
FLVKKKMQYH KMHPQQQSSD QDAFKITIEN LCTGVSESGF SGNDAHLGEA GNIVISIQVL
RDATYNFDEK NILGRGGFGI VYKGELHDGT KIAVKRMESS IISGKGLDEF KSEIAVLTRV
RHRNLVVLHG YCLEGNERLL VYQYMPQGTL SRHIFYWKEE GLRPLEWTRR LIIALDVARG
VEYLHTLAHQ SFIHRDLKPS NILLGDDMHA KVADFGLVRL APEGTQSIET KIAGTFGYLA
PEYAVTGRVT TKVDVYSFGV ILMELLTGRK ALDVARSEEE VHLATWFRRM FINKGSFPKA
IDEAMEVNEE TLRSINIVAE LANQCSSREP RDRPDMNHVV NVLVSLVVQW KPTERSSDSE
DIYGIDYDTP LPQLILDSCF FGDNTLTSIP SRPSELESTF KSGQGR
