TD1_MAIZE
ID TD1_MAIZE Reviewed; 996 AA.
AC P0DL10;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Leucine-rich repeat receptor-like kinase protein THICK TASSEL DWARF1;
DE EC=2.7.11.1;
DE AltName: Full=CLAVATA1-like protein;
DE AltName: Full=CLV1 related kinase 5;
DE Short=ZmKIN5;
DE Flags: Precursor;
GN Name=TD1; Synonyms=KIN5; ORFNames=GRMZM2G300133 {ECO:0000305};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=15716347; DOI=10.1242/dev.01671;
RA Bommert P., Lunde C., Nardmann J., Vollbrecht E., Running M., Jackson D.,
RA Hake S., Werr W.;
RT "thick tassel dwarf1 encodes a putative maize ortholog of the Arabidopsis
RT CLAVATA1 leucine-rich repeat receptor-like kinase.";
RL Development 132:1235-1245(2005).
RN [2]
RP FUNCTION.
RX PubMed=19153258; DOI=10.1534/genetics.108.098350;
RA Lunde C., Hake S.;
RT "The interaction of knotted1 and thick tassel dwarf1 in vegetative and
RT reproductive meristems of maize.";
RL Genetics 181:1693-1697(2009).
CC -!- FUNCTION: Receptor-like kinase protein that regulates meristem size
CC during inflorescence and flower development. Promotes vegetative
CC meristem growth and restricts inflorescence and floral meristem growth.
CC Based on additive and synergistic phenotypes of double mutants, it is
CC probable that unlike CLV1 and CLV2 in A.thaliana, TD1 and FAE2 do not
CC function exclusively in a single pathway. However, KN-1 and TD1 do
CC function in a linear pathway to maintain vegetative meristem
CC homeostasis, but they may interact with different partners during
CC development. {ECO:0000269|PubMed:15716347,
CC ECO:0000269|PubMed:19153258}.
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 -!- 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;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the apex of the vegetative
CC seedlings. Lower expression in young leaves, ears and tassels, embryos
CC and roots. Not expressed in the shoot meristem itself. Detected in the
CC three outermost layers of the inflorescence meristem, and on its flanks
CC at positions of prospective spikelet pair meristems. Not confined to
CC meristematic cells but also detected in primordia of glumes, lemmas and
CC stamens. {ECO:0000269|PubMed:15716347}.
CC -!- DISRUPTION PHENOTYPE: Fasciation. Flattened and wider ears with
CC irregular rows of seeds. Thicker rachis of tassels and increased floral
CC organ numbers. Reduced vegetative growth.
CC {ECO:0000269|PubMed:15716347}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR RefSeq; XP_008645089.1; XM_008646867.1.
DR AlphaFoldDB; P0DL10; -.
DR SMR; P0DL10; -.
DR STRING; 4577.GRMZM2G300133_P01; -.
DR PaxDb; P0DL10; -.
DR PRIDE; P0DL10; -.
DR EnsemblPlants; Zm00001eb228140_T001; Zm00001eb228140_P001; Zm00001eb228140.
DR GeneID; 103626458; -.
DR Gramene; Zm00001eb228140_T001; Zm00001eb228140_P001; Zm00001eb228140.
DR KEGG; zma:103626458; -.
DR MaizeGDB; 9023073; -.
DR eggNOG; ENOG502QQ4T; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR OMA; GQFMVFN; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000007305; Chromosome 5.
DR ExpressionAtlas; P0DL10; baseline and differential.
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:0033612; F:receptor serine/threonine kinase binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010080; P:regulation of floral meristem growth; IEA:EnsemblPlants.
DR GO; GO:0048833; P:specification of floral organ number; IEA:EnsemblPlants.
DR Gene3D; 3.80.10.10; -; 4.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Developmental protein; Differentiation; 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..996
FT /note="Leucine-rich repeat receptor-like kinase protein
FT THICK TASSEL DWARF1"
FT /id="PRO_0000422040"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 78..103
FT /note="LRR 1"
FT REPEAT 104..127
FT /note="LRR 2"
FT REPEAT 128..151
FT /note="LRR 3"
FT REPEAT 153..178
FT /note="LRR 4"
FT REPEAT 180..201
FT /note="LRR 5"
FT REPEAT 202..226
FT /note="LRR 6"
FT REPEAT 251..275
FT /note="LRR 7"
FT REPEAT 276..299
FT /note="LRR 8"
FT REPEAT 300..323
FT /note="LRR 9"
FT REPEAT 325..349
FT /note="LRR 10"
FT REPEAT 351..371
FT /note="LRR 11"
FT REPEAT 372..395
FT /note="LRR 12"
FT REPEAT 397..419
FT /note="LRR 13"
FT REPEAT 420..443
FT /note="LRR 14"
FT REPEAT 445..466
FT /note="LRR 15"
FT REPEAT 467..490
FT /note="LRR 16"
FT REPEAT 491..514
FT /note="LRR 17"
FT REPEAT 516..538
FT /note="LRR 18"
FT REPEAT 539..562
FT /note="LRR 19"
FT REPEAT 563..586
FT /note="LRR 20"
FT REPEAT 587..611
FT /note="LRR 21"
FT DOMAIN 703..978
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 828
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 709..717
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 731
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 996 AA; 105988 MW; BA94FF17A43864CF CRC64;
MPPPTFLLGL LLLLLLAAAA PAPASATPER DAYALSRLKA SLVPSATNST SAPLSDWDPA
ATPPAHCAFT GVTCDAATSR VVAINLTAVP LHGGALPPEV ALLDALASLT VANCYLRGRL
PPALASMPAL RHLNLSNNNL SGPFPPPPPA AYFPALEIVD VYNNNLSGPL PPLGAPHARS
LRYLHLGGNY FNGSIPDTFG DLAALEYLGL NGNALSGRVP PSLSRLSRLR EMYVGYYNQY
SGGVPREFGA LQSLVRLDMS SCTLTGPIPP ELARLSRLDT LFLALNQLTG EIPPELGALT
SLRSLDLSIN DLAGEIPASF AALTNLKLLN LFRNHLRGEI PAFLGDFPFL EVLQVWDNNL
TGPLPPALGR NGRLKTLDVT SNHLTGTIPP DLCAGRNLQL LVLMDNGFFG SIPESLGDCK
TLTRVRLGKN FLTGPVPAGL FDLPQANMLE LTDNMLTGEL PDVIAGDKIG MLMLGNNRIG
GRIPAAIGNL PALQTLSLES NNFSGPLPPE IGRLRNLTRL NASGNALTGG IPRELMGCAS
LGAVDLSRNG LTGEIPDTVT SLKILCTLNV SRNRLSGELP AAMANMTSLT TLDVSYNQLS
GPVPMQGQFL VFNESSFVGN PGLCSACPPS SGGARSPFSL RRWDSKKLLV WLVVLLTLLV
LAVLGARKAH EAWREAARRR SGAWKMTAFQ KLDFSADDVV ECLKEDNIIG KGGAGIVYHG
VTRGGAELAI KRLVGRGCGD HDRGFTAEVT TLGRIRHRNI VRLLGFVSNR EANLLLYEYM
PNGSLGEMLH GGKGGHLGWE ARARVAAEAA RGLCYLHHDC APRIIHRDVK SNNILLDSAF
EAHVADFGLA KFLGGGGATS ECMSAIAGSY GYIAPEYAYT LRVDEKSDVY SFGVVLLELI
TGRRPVGSFG DGVDIVHWVR KVTADAAAAE EPVLLVADRR LAPEPVPLLA DLYRVAMACV
EEASTARPTM REVVHMLSTS AAAQPDVPHA LCKVVD
