HAR1_LOTJA
ID HAR1_LOTJA Reviewed; 986 AA.
AC Q8GRU6;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Leucine-rich repeat receptor-like kinase protein HAR1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein HYPERNODULATION ABERRANT ROOT FORMATION 1 {ECO:0000303|PubMed:12442172};
DE Flags: Precursor;
GN Name=HAR1 {ECO:0000303|PubMed:12442172};
GN ORFNames=CM0216.560.nc {ECO:0000312|EMBL:BAF98590.1};
OS Lotus japonicus (Lotus corniculatus var. japonicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=12442170; DOI=10.1038/nature01207;
RA Krusell L., Madsen L.H., Sato S., Aubert G., Genua A., Szczyglowski K.,
RA Duc G., Kaneko T., Tabata S., de Bruijn F., Pajuelo E., Sandal N.,
RA Stougaard J.;
RT "Shoot control of root development and nodulation is mediated by a
RT receptor-like kinase.";
RL Nature 420:422-426(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-740.
RX PubMed=12442172; DOI=10.1038/nature01231;
RA Nishimura R., Hayashi M., Wu G.-J., Kouchi H., Imaizumi-Anraku H.,
RA Murakami Y., Kawasaki S., Akao S., Ohmori M., Nagasawa M., Harada K.,
RA Kawaguchi M.;
RT "HAR1 mediates systemic regulation of symbiotic organ development.";
RL Nature 420:426-429(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Miyakojima MG-20;
RX PubMed=18511435; DOI=10.1093/dnares/dsn008;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Kato T., Nakao M.,
RA Sasamoto S., Watanabe A., Ono A., Kawashima K., Fujishiro T., Katoh M.,
RA Kohara M., Kishida Y., Minami C., Nakayama S., Nakazaki N., Shimizu Y.,
RA Shinpo S., Takahashi C., Wada T., Yamada M., Ohmido N., Hayashi M.,
RA Fukui K., Baba T., Nakamichi T., Mori H., Tabata S.;
RT "Genome structure of the legume, Lotus japonicus.";
RL DNA Res. 15:227-239(2008).
CC -!- FUNCTION: LRR receptor kinase involved in the regulation of root and
CC shoot growth, and root nodule organogenesis (PubMed:12442170,
CC PubMed:12442172). Involved in long distance nodulation signaling events
CC (PubMed:12442170, PubMed:12442172). Involved in the autoregulation of
CC nodulation (AON), a long distance systemic signaling from root to shoot
CC and back again, which allows legumes to limit the number of root
CC nodules formed based on available nitrogen and previous rhizobial
CC colonization (PubMed:12442170, PubMed:12442172). Acts from shoot to
CC root to control AON (PubMed:12442170, PubMed:12442172). Involved in the
CC regulation of root colonization by arbuscular mycorrhizal (AM) fungi
CC (PubMed:12442170, PubMed:12442172). {ECO:0000269|PubMed:12442170,
CC ECO:0000269|PubMed:12442172}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:12442172}.
CC -!- DISRUPTION PHENOTYPE: Increased number of root nodules when inoculated
CC with Mesorhizobium loti (PubMed:12442170, PubMed:12442172). Inhibition
CC of shoot and root growth (PubMed:12442170, PubMed:12442172). Increase
CC in arbuscular mycorrhizal (AM) fungus colonization intensity in roots
CC (enhanced mycorrhizal phenotype) when inoculated with AM fungi
CC (PubMed:12442170, PubMed:12442172). {ECO:0000269|PubMed:12442170,
CC ECO:0000269|PubMed:12442172}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AJ495843; CAD42335.1; -; Genomic_DNA.
DR EMBL; AJ495844; CAD42336.1; -; mRNA.
DR EMBL; AJ580824; CAE45593.1; -; Genomic_DNA.
DR EMBL; AB092809; BAC41327.1; -; Genomic_DNA.
DR EMBL; AB092810; BAC41331.1; -; mRNA.
DR EMBL; AP005667; BAF98590.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GRU6; -.
DR SMR; Q8GRU6; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 5.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Differentiation; Glycoprotein;
KW Growth regulation; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Receptor; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..986
FT /note="Leucine-rich repeat receptor-like kinase protein
FT HAR1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000448629"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 71..97
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 98..121
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 123..145
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 146..170
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 171..196
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 198..218
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 243..267
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 268..291
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 293..314
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 316..339
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 340..363
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 365..387
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 388..411
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 412..435
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 437..458
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 459..482
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 483..506
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 508..530
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 531..554
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 555..578
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 579..603
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT DOMAIN 695..971
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 820
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 701..709
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 723
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 740
FT /note="E->K: In har1-5; increased number of root nodules
FT when inoculated with Mesorhizobium loti; inhibition of
FT shoot and root growth; increase in arbuscular mycorrhizal
FT (AM) fungus colonization intensity in roots (enhanced
FT mycorrhizal phenotype) when inoculated with AM fungi."
FT /evidence="ECO:0000269|PubMed:12442172"
SQ SEQUENCE 986 AA; 108457 MW; B93C31BCBE71FF27 CRC64;
MRIRVSYLLV LCFTLIWFRW TVVYSSFSDL DALLKLKESM KGAKAKHHAL EDWKFSTSLS
AHCSFSGVTC DQNLRVVALN VTLVPLFGHL PPEIGLLEKL ENLTISMNNL TDQLPSDLAS
LTSLKVLNIS HNLFSGQFPG NITVGMTELE ALDAYDNSFS GPLPEEIVKL EKLKYLHLAG
NYFSGTIPES YSEFQSLEFL GLNANSLTGR VPESLAKLKT LKELHLGYSN AYEGGIPPAF
GSMENLRLLE MANCNLTGEI PPSLGNLTKL HSLFVQMNNL TGTIPPELSS MMSLMSLDLS
INDLTGEIPE SFSKLKNLTL MNFFQNKFRG SLPSFIGDLP NLETLQVWEN NFSFVLPHNL
GGNGRFLYFD VTKNHLTGLI PPDLCKSGRL KTFIITDNFF RGPIPKGIGE CRSLTKIRVA
NNFLDGPVPP GVFQLPSVTI TELSNNRLNG ELPSVISGES LGTLTLSNNL FTGKIPAAMK
NLRALQSLSL DANEFIGEIP GGVFEIPMLT KVNISGNNLT GPIPTTITHR ASLTAVDLSR
NNLAGEVPKG MKNLMDLSIL NLSRNEISGP VPDEIRFMTS LTTLDLSSNN FTGTVPTGGQ
FLVFNYDKTF AGNPNLCFPH RASCPSVLYD SLRKTRAKTA RVRAIVIGIA LATAVLLVAV
TVHVVRKRRL HRAQAWKLTA FQRLEIKAED VVECLKEENI IGKGGAGIVY RGSMPNGTDV
AIKRLVGQGS GRNDYGFRAE IETLGKIRHR NIMRLLGYVS NKDTNLLLYE YMPNGSLGEW
LHGAKGGHLR WEMRYKIAVE AARGLCYMHH DCSPLIIHRD VKSNNILLDA DFEAHVADFG
LAKFLYDPGA SQSMSSIAGS YGYIAPEYAY TLKVDEKSDV YSFGVVLLEL IIGRKPVGEF
GDGVDIVGWV NKTMSELSQP SDTALVLAVV DPRLSGYPLT SVIHMFNIAM MCVKEMGPAR
PTMREVVHML TNPPQSNTST QDLINL
