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LysM domain receptor-like kinase 3 (LysM-containing receptor-like kinase 3) (MtLYK3) (EC 2.7.11.1) (LysM receptor kinase K1B) (Protein HAIR CURLING)

 LYK3_MEDTR              Reviewed;         620 AA.
Q6UD73; A0A072UFY4; A6H2J7; A6H2J8; A6H2K7;
08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
12-SEP-2018, entry version 114.
RecName: Full=LysM domain receptor-like kinase 3 {ECO:0000303|PubMed:12947035};
Short=LysM-containing receptor-like kinase 3 {ECO:0000305};
Short=MtLYK3 {ECO:0000303|PubMed:17586690};
EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:20971894};
AltName: Full=LysM receptor kinase K1B {ECO:0000305};
AltName: Full=Protein HAIR CURLING {ECO:0000303|PubMed:11290290};
Flags: Precursor;
Name=LYK3 {ECO:0000303|PubMed:12947035};
Synonyms=HCL {ECO:0000303|PubMed:11290290}, RLK3 {ECO:0000305};
OrderedLocusNames=MTR_5g086130 {ECO:0000312|EMBL:AES99916.1};
Medicago truncatula (Barrel medic) (Medicago tribuloides).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
50 kb inversion clade; NPAAA clade; Hologalegina; IRL clade;
Trifolieae; Medicago.
NCBI_TaxID=3880 {ECO:0000312|EMBL:AAQ73159.1};
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION,
DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
STRAIN=cv. Jemalong A17;
PubMed=12947035; DOI=10.1126/science.1090074;
Limpens E., Franken C., Smit P., Willemse J., Bisseling T., Geurts R.;
"LysM domain receptor kinases regulating rhizobial Nod factor-induced
infection.";
Science 302:630-633(2003).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] OF
121-276 (ISOFORM 1/2), FUNCTION, MUTAGENESIS OF PRO-87 AND GLY-334,
AND DISRUPTION PHENOTYPE.
TISSUE=Root;
PubMed=17586690; DOI=10.1104/pp.107.100495;
Smit P., Limpens E., Geurts R., Fedorova E., Dolgikh E., Gough C.,
Bisseling T.;
"Medicago LYK3, an entry receptor in rhizobial nodulation factor
signaling.";
Plant Physiol. 145:183-191(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Jemalong A17;
PubMed=22089132; DOI=10.1038/nature10625;
Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M.,
Cheung F., De Mita S., Krishnakumar V., Gundlach H., Zhou S.,
Mudge J., Bharti A.K., Murray J.D., Naoumkina M.A., Rosen B.,
Silverstein K.A.T., Tang H., Rombauts S., Zhao P.X., Zhou P.,
Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H.,
Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
Deshpande S., Dai X., Doyle J.J., Dudez A.-M., Farmer A.D.,
Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A.,
Humphray S.J., Jeong D.-H., Jing Y., Jocker A., Kenton S.M.,
Kim D.-J., Klee K., Lai H., Lang C., Lin S., Macmil S.L.,
Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.-H.,
Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C.,
Sallet E., Samain S., Samson N., Sanders I., Saurat O., Scarpelli C.,
Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S.,
Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B., Wang K.,
Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
"The Medicago genome provides insight into the evolution of rhizobial
symbioses.";
Nature 480:520-524(2011).
[4]
FUNCTION, MUTAGENESIS OF PRO-87 AND GLY-334, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Jemalong A17;
PubMed=11290290;
Catoira R., Timmers A.C., Maillet F., Galera C., Penmetsa R.V.,
Cook D., Denarie J., Gough C.;
"The HCL gene of Medicago truncatula controls Rhizobium-induced root
hair curling.";
Development 128:1507-1518(2001).
[5]
AUTOPHOSPHORYLATION, AND GENE FAMILY.
STRAIN=cv. Jemalong A17;
PubMed=16844829; DOI=10.1104/pp.106.084657;
Arrighi J.-F., Barre A., Ben Amor B., Bersoult A., Soriano L.C.,
Mirabella R., de Carvalho-Niebel F., Journet E.-P., Gherardi M.,
Huguet T., Geurts R., Denarie J., Rouge P., Gough C.;
"The Medicago truncatula lysin [corrected] motif-receptor-like kinase
gene family includes NFP and new nodule-expressed genes.";
Plant Physiol. 142:265-279(2006).
[6]
FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PUB1, SUBCELLULAR
LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
AUTOPHOSPHORYLATION, AND CATALYTIC ACTIVITY.
STRAIN=cv. Jemalong A17;
PubMed=20971894; DOI=10.1105/tpc.110.075861;
Mbengue M., Camut S., de Carvalho-Niebel F., Deslandes L.,
Froidure S., Klaus-Heisen D., Moreau S., Rivas S., Timmers T.,
Herve C., Cullimore J., Lefebvre B.;
"The Medicago truncatula E3 ubiquitin ligase PUB1 interacts with the
LYK3 symbiotic receptor and negatively regulates infection and
nodulation.";
Plant Cell 22:3474-3488(2010).
[7]
DISRUPTION PHENOTYPE.
PubMed=23432463; DOI=10.1111/nph.12198;
Rey T., Nars A., Bonhomme M., Bottin A., Huguet S., Balzergue S.,
Jardinaud M.-F., Bono J.-J., Cullimore J., Dumas B., Gough C.,
Jacquet C.;
"NFP, a LysM protein controlling Nod factor perception, also
intervenes in Medicago truncatula resistance to pathogens.";
New Phytol. 198:875-886(2013).
[8]
FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=cv. Jemalong A17;
PubMed=25351493; DOI=10.1105/tpc.114.129502;
Moling S., Pietraszewska-Bogiel A., Postma M., Fedorova E., Hink M.A.,
Limpens E., Gadella T.W.J., Bisseling T.;
"Nod factor receptors form heteromeric complexes and are essential for
intracellular infection in medicago nodules.";
Plant Cell 26:4188-4199(2014).
-!- FUNCTION: Putative receptor for S.meliloti Nod factor signals
essential for the establishment of the nitrogen-fixing, root
nodule symbiosis with S.meliloti (PubMed:20971894,
PubMed:12947035, PubMed:17586690, PubMed:25351493). Involved in
the control of root hair curling after S.meliloti infection,
probably by modulating the reorganization of the microtubular
cytoskeleton in epidermal and cortical cells (PubMed:17586690,
PubMed:11290290). Regulates a subset of Nod factor-induced genes
(PubMed:17586690). {ECO:0000269|PubMed:11290290,
ECO:0000269|PubMed:12947035, ECO:0000269|PubMed:17586690,
ECO:0000269|PubMed:20971894, ECO:0000269|PubMed:25351493}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:20971894}.
-!- SUBUNIT: Forms homodimers and homooligomers (By similarity). Forms
heteromeric complexes with NFP at the cell periphery in nodules
(PubMed:25351493). Interacts with PUB1 (PubMed:20971894).
{ECO:0000250|UniProtKB:A8R7E6, ECO:0000269|PubMed:20971894,
ECO:0000269|PubMed:25351493}.
-!- INTERACTION:
G7KAT5:11409451; NbExp=6; IntAct=EBI-12551665, EBI-12551650;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20971894,
ECO:0000269|PubMed:25351493}; Single-pass membrane protein
{ECO:0000255}. Vacuole lumen {ECO:0000269|PubMed:25351493}.
Note=Removed from the plasma membrane upon the release of rhizobia
into the host cytoplasm. Vacuolar localization is observed in
cells undergoing breakdown of the receptors.
{ECO:0000269|PubMed:25351493}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6UD73-1; Sequence=Displayed;
Name=2;
IsoId=Q6UD73-2; Sequence=VSP_058382;
Note=No experimental confirmation available.
{ECO:0000312|EMBL:KEH28326.1};
-!- TISSUE SPECIFICITY: Expressed in the epidermal and root hair cells
of the developing root hair zone during nonsymbiotic growth.
Accumulates in roots and nodules during symbiotic growth with
rhizobia (PubMed:12947035, PubMed:20971894). Localized at the cell
periphery in a narrow zone of about two cell layers (e.g. L1/L2
zone) at the nodule apex upon infection by rhizobia, from the
meristem to the infection zone (at protein level)
(PubMed:25351493). {ECO:0000269|PubMed:12947035,
ECO:0000269|PubMed:20971894, ECO:0000269|PubMed:25351493}.
-!- DEVELOPMENTAL STAGE: Following inoculation with S.meliloti,
accumulates strongly in the nodule primordia. In young nodules,
expressed in a broad apical region and in the vasculature. In
mature nodules, predominantly observed in the apical part of the
nodule encompassing the pre-infection and infection zones
(PubMed:20971894). Localized on infection threads before rhizobia
are released (PubMed:25351493). {ECO:0000269|PubMed:20971894,
ECO:0000269|PubMed:25351493}.
-!- PTM: Autophosphorylated. {ECO:0000269|PubMed:16844829,
ECO:0000269|PubMed:20971894}.
-!- DISRUPTION PHENOTYPE: In the lyk3-4 mutant, increased nodulation
in plants infected by S.meliloti, mostly resulting in tubular
infection threads, and, to a lower extent, in sac-like structures
(PubMed:20971894, PubMed:12947035). The weak hcl-4 mutant is
unable to form curled root hairs, a step preceding infection
thread formation upon infection by S.meliloti and leading to
nodulation. In the hcl-2 mutant, S.meliloti induces extensive root
hair deformation and continuous curling, but is unable to induce
the formation of tight root hair curls and the subsequent
infection threads (PubMed:17586690). In the hcl-2 mutant, there is
reduced S. meliloti Nod factor-mediated induction of cortical cell
division foci. Impaired asymmetric microtubule network formation
in curled root hairs, and failure of activated cortical cells to
become polarised and to exhibit the microtubular cytoplasmic
bridges characteristic of the pre-infection threads induced by
rhizobia (PubMed:11290290). Increased infection threads in nodules
due to a slower release of bacteria into the cytoplasm
(PubMed:25351493). Normal susceptibility to the root oomycete
A.euteiches and to the fungus C.trifolii (PubMed:23432463).
{ECO:0000269|PubMed:11290290, ECO:0000269|PubMed:12947035,
ECO:0000269|PubMed:17586690, ECO:0000269|PubMed:20971894,
ECO:0000269|PubMed:23432463, ECO:0000269|PubMed:25351493}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
URL="http://plantsp.genomics.purdue.edu/family/class.html";
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EMBL; AY372402; AAQ73155.1; -; Genomic_DNA.
EMBL; AY372406; AAQ73159.1; -; mRNA.
EMBL; AM420448; CAM06620.1; -; Genomic_DNA.
EMBL; AM420450; CAM06621.1; -; Genomic_DNA.
EMBL; AM420451; CAM06622.1; -; Genomic_DNA.
EMBL; AM420459; CAM06630.1; -; mRNA.
EMBL; CM001221; AES99916.1; -; Genomic_DNA.
EMBL; CM001221; KEH28326.1; -; Genomic_DNA.
RefSeq; XP_003616958.1; XM_003616910.2. [Q6UD73-1]
RefSeq; XP_013454295.1; XM_013598841.1. [Q6UD73-2]
ProteinModelPortal; Q6UD73; -.
SMR; Q6UD73; -.
IntAct; Q6UD73; 1.
MINT; Q6UD73; -.
EnsemblPlants; AES99916; AES99916; MTR_5g086130. [Q6UD73-1]
EnsemblPlants; KEH28326; KEH28326; MTR_5g086130. [Q6UD73-2]
Gramene; AES99916; AES99916; MTR_5g086130. [Q6UD73-1]
Gramene; KEH28326; KEH28326; MTR_5g086130. [Q6UD73-2]
KEGG; mtr:MTR_5g086130; -.
KO; K13429; -.
OMA; ARRCTHQ; -.
OrthoDB; EOG093604SX; -.
Proteomes; UP000002051; Chromosome 5.
Proteomes; UP000002051; Unassembled WGS sequence.
ExpressionAtlas; Q6UD73; differential.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005775; C:vacuolar lumen; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0009877; P:nodulation; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0009609; P:response to symbiotic bacterium; IMP:UniProtKB.
Gene3D; 3.10.350.10; -; 2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR036779; LysM_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Kinase; Membrane; Nodulation;
Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
Transmembrane helix; Vacuole.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 620 LysM domain receptor-like kinase 3.
{ECO:0000255}.
/FTId=PRO_5006746948.
TOPO_DOM 24 231 Extracellular. {ECO:0000305}.
TRANSMEM 232 252 Helical. {ECO:0000255}.
TOPO_DOM 253 620 Cytoplasmic. {ECO:0000305}.
DOMAIN 46 72 LysM 1; degenerate.
{ECO:0000250|UniProtKB:A8R7E6}.
DOMAIN 102 148 LysM 2. {ECO:0000255|PROSITE-
ProRule:PRU01118}.
DOMAIN 167 210 LysM 3. {ECO:0000255|PROSITE-
ProRule:PRU01118}.
DOMAIN 322 595 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 328 336 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 108 114 Chitin-binding.
{ECO:0000250|UniProtKB:A8R7E6}.
REGION 136 142 Chitin-binding.
{ECO:0000250|UniProtKB:A8R7E6}.
ACT_SITE 441 441 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 349 349 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 269 269 Phosphoserine.
{ECO:0000250|UniProtKB:A8R7E6}.
MOD_RES 273 273 Phosphoserine.
{ECO:0000250|UniProtKB:A8R7E6}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 25 92 {ECO:0000250|UniProtKB:A8R7E6}.
DISULFID 29 154 {ECO:0000250|UniProtKB:A8R7E6}.
DISULFID 90 152 {ECO:0000250|UniProtKB:A8R7E6}.
VAR_SEQ 277 278 Missing (in isoform 2).
/FTId=VSP_058382.
MUTAGEN 87 87 P->S: In hcl-3; S.meliloti induces
extensive root hair deformation and
continuous curling, but is unable to
induce the formation of tight root hair
curls and the subsequent infection
threads. {ECO:0000269|PubMed:11290290,
ECO:0000269|PubMed:17586690}.
MUTAGEN 334 334 G->E: In hcl-1; S.meliloti induces
extensive root hair deformation and
continuous curling, but is unable to
induce the formation of tight root hair
curls and the subsequent infection
threads. {ECO:0000269|PubMed:11290290,
ECO:0000269|PubMed:17586690}.
CONFLICT 87 87 P -> S (in Ref. 2; CAM06621).
{ECO:0000305}.
CONFLICT 334 334 G -> E (in Ref. 2; CAM06620).
{ECO:0000305}.
SEQUENCE 620 AA; 68580 MW; 884D5593B8FEB66E CRC64;
MNLKNGLLLF ILFLDCVFFK VESKCVKGCD VALASYYIIP SIQLRNISNF MQSKIVLTNS
FDVIMSYNRD VVFDKSGLIS YTRINVPFPC ECIGGEFLGH VFEYTTKEGD DYDLIANTYY
ASLTTVELLK KFNSYDPNHI PVKAKINVTV ICSCGNSQIS KDYGLFVTYP LRSDDTLAKI
ATKAGLDEGL IQNFNQDANF SIGSGIVFIP GRDQNGHFFP LYSRTGIAKG SAVGIAMAGI
FGLLLFVIYI YAKYFQKKEE EKTKLPQTSR AFSTQDASGS AEYETSGSSG HATGSAAGLT
GIMVAKSTEF TYQELAKATN NFSLDNKIGQ GGFGAVYYAE LRGEKTAIKK MDVQASSEFL
CELKVLTHVH HLNLVRLIGY CVEGSLFLVY EHIDNGNLGQ YLHGIGTEPL PWSSRVQIAL
DSARGLEYIH EHTVPVYIHR DVKSANILID KNLRGKVADF GLTKLIEVGN STLHTRLVGT
FGYMPPEYAQ YGDVSPKIDV YAFGVVLYEL ITAKNAVLKT GESVAESKGL VQLFEEALHR
MDPLEGLRKL VDPRLKENYP IDSVLKMAQL GRACTRDNPL LRPSMRSIVV ALMTLSSPTE
DCDDDSSYEN QSLINLLSTR


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10-782-55028 Discoidin domain-containing receptor 2 - EC 2.7.10.1; Discoidin domain receptor 2; Receptor protein-tyrosine kinase TKT; Tyrosine-protein kinase TYRO 10; Neurotrophic tyrosine kinase. receptor-related 0.01 mg
10-782-55028 Discoidin domain-containing receptor 2 - EC 2.7.10.1; Discoidin domain receptor 2; Receptor protein-tyrosine kinase TKT; Tyrosine-protein kinase TYRO 10; Neurotrophic tyrosine kinase. receptor-related 0.001 mg


 

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