TMKL1_ARATH
ID TMKL1_ARATH Reviewed; 674 AA.
AC P33543;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Putative kinase-like protein TMKL1;
DE Flags: Precursor;
GN Name=TMKL1; OrderedLocusNames=At3g24660; ORFNames=MSD24.3;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=8219075; DOI=10.1007/bf00029017;
RA Valon C., Smalle J., Goodman H.M., Giraudat J.;
RT "Characterization of an Arabidopsis thaliana gene (TMKL1) encoding a
RT putative transmembrane protein with an unusual kinase-like domain.";
RL Plant Mol. Biol. 23:415-421(1993).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: Does not seem to have conserved a kinase activity.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; X72863; CAA51385.1; -; mRNA.
DR EMBL; AP000740; BAB01215.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76934.1; -; Genomic_DNA.
DR EMBL; AY090945; AAM13993.1; -; mRNA.
DR PIR; S39476; S39476.
DR RefSeq; NP_189109.1; NM_113377.4.
DR AlphaFoldDB; P33543; -.
DR SMR; P33543; -.
DR BioGRID; 7393; 49.
DR STRING; 3702.AT3G24660.1; -.
DR iPTMnet; P33543; -.
DR PaxDb; P33543; -.
DR PRIDE; P33543; -.
DR ProteomicsDB; 232646; -.
DR EnsemblPlants; AT3G24660.1; AT3G24660.1; AT3G24660.
DR GeneID; 822062; -.
DR Gramene; AT3G24660.1; AT3G24660.1; AT3G24660.
DR KEGG; ath:AT3G24660; -.
DR Araport; AT3G24660; -.
DR TAIR; locus:2093121; AT3G24660.
DR eggNOG; ENOG502QVB6; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; P33543; -.
DR OMA; FFGESKF; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P33543; -.
DR PRO; PR:P33543; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P33543; baseline and differential.
DR Genevisible; P33543; AT.
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:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Leucine-rich repeat; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..674
FT /note="Putative kinase-like protein TMKL1"
FT /id="PRO_0000024389"
FT TOPO_DOM 26..295
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..674
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 100..122
FT /note="LRR 1"
FT REPEAT 124..146
FT /note="LRR 2"
FT REPEAT 148..169
FT /note="LRR 3"
FT REPEAT 173..194
FT /note="LRR 4"
FT REPEAT 200..222
FT /note="LRR 5"
FT REPEAT 224..244
FT /note="LRR 6"
FT REPEAT 247..269
FT /note="LRR 7"
FT DOMAIN 373..674
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 331..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 375
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 674 AA; 73353 MW; 533D0A8D8767E253 CRC64;
MGMEALRFLH VIFFFVLILH CHCGTSLSGS SDVKLLLGKI KSSLQGNSES LLLSSWNSSV
PVCQWRGVKW VFSNGSPLQC SDLSSPQWTN TSLFNDSSLH LLSLQLPSAN LTGSLPREIG
EFSMLQSVFL NINSLSGSIP LELGYTSSLS DVDLSGNALA GVLPPSIWNL CDKLVSFKIH
GNNLSGVLPE PALPNSTCGN LQVLDLGGNK FSGEFPEFIT RFKGVKSLDL SSNVFEGLVP
EGLGVLELES LNLSHNNFSG MLPDFGESKF GAESFEGNSP SLCGLPLKPC LGSSRLSPGA
VAGLVIGLMS GAVVVASLLI GYLQNKKRKS SIESEDDLEE GDEEDEIGEK EGGEGKLVVF
QGGENLTLDD VLNATGQVME KTSYGTVYKA KLSDGGNIAL RLLREGTCKD RSSCLPVIRQ
LGRIRHENLV PLRAFYQGKR GEKLLIYDYL PNISLHDLLH ESKPRKPALN WARRHKIALG
IARGLAYLHT GQEVPIIHGN IRSKNVLVDD FFFARLTEFG LDKIMVQAVA DEIVSQAKSD
GYKAPELHKM KKCNPRSDVY AFGILLLEIL MGKKPGKSGR NGNEFVDLPS LVKAAVLEET
TMEVFDLEAM KGIRSPMEEG LVHALKLAMG CCAPVTTVRP SMEEVVKQLE ENRPRNRSAL
YSPTETRSDA ETPF
