NORK_MEDTR
ID NORK_MEDTR Reviewed; 925 AA.
AC Q8L4H4; Q8L6K4; Q8L6K5; Q8L6K6; Q8LKZ0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Nodulation receptor kinase;
DE EC=2.7.11.1 {ECO:0000269|PubMed:26839127};
DE AltName: Full=Does not make infections protein 2;
DE AltName: Full=MtSYMRK;
DE AltName: Full=Symbiosis receptor-like kinase;
DE Flags: Precursor;
GN Name=NORK; Synonyms=DMI2, SYMRK;
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND MUTAGENESIS OF
RP 343-ASN--ARG-925; 436-LEU--SER-458 AND GLY-795.
RC STRAIN=cv. Jemalong A17;
RX PubMed=12087406; DOI=10.1038/nature00842;
RA Endre G., Kereszt A.A., Kevei Z., Mihacea S., Kalo P., Kiss G.B.;
RT "A receptor kinase gene regulating symbiotic nodule development.";
RL Nature 417:962-966(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=12087405; DOI=10.1038/nature00841;
RA Stracke S., Kistner C., Yoshida S., Mulder L., Sato S., Kaneko T.,
RA Tabata S., Sandal N., Stougaard J., Szczyglowski K., Parniske M.;
RT "A plant receptor-like kinase required for both bacterial and fungal
RT symbiosis.";
RL Nature 417:959-962(2002).
RN [3]
RP INTERACTION WITH PUB1, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=26839127; DOI=10.1104/pp.15.01694;
RA Vernie T., Camut S., Camps C., Rembliere C., de Carvalho-Niebel F.,
RA Mbengue M., Timmers T., Gasciolli V., Thompson R.D., Lesignor C.,
RA Lefebvre B., Cullimore J.V., Herve C.;
RT "PUB1 interacts with the receptor kinase DMI2 and negatively regulates
RT rhizobial and arbuscular mycorrhizal symbioses through its ubiquitination
RT activity in Medicago truncatula.";
RL Plant Physiol. 170:2312-2324(2016).
CC -!- FUNCTION: Involved in the perception of symbiotic fungi and bacteria.
CC Part of the perception/transduction system leading to nodulation or
CC mycorrhizal infection (PubMed:12087406, PubMed:12087405).
CC Phosphorylates PUB1 (PubMed:26839127). {ECO:0000269|PubMed:12087405,
CC ECO:0000269|PubMed:12087406, ECO:0000269|PubMed:26839127}.
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:0000269|PubMed:26839127};
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:0000269|PubMed:26839127};
CC -!- SUBUNIT: Binds to PUB1. {ECO:0000269|PubMed:26839127}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed constitutively in the entire root system,
CC except in root meristems. {ECO:0000269|PubMed:26839127}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:26839127}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD10808.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD10809.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD10810.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD10814.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ418369; CAD10808.1; ALT_INIT; mRNA.
DR EMBL; AJ418370; CAD10809.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ418371; CAD10810.1; ALT_INIT; mRNA.
DR EMBL; AJ418374; CAD10814.1; ALT_INIT; mRNA.
DR EMBL; AJ418373; CAD10811.1; -; mRNA.
DR EMBL; AF491998; AAM76685.1; -; mRNA.
DR RefSeq; XP_003612951.2; XM_003612903.2.
DR AlphaFoldDB; Q8L4H4; -.
DR SMR; Q8L4H4; -.
DR STRING; 3880.AES95909; -.
DR PRIDE; Q8L4H4; -.
DR EnsemblPlants; AES95909; AES95909; MTR_5g030920.
DR GeneID; 11407326; -.
DR Gramene; AES95909; AES95909; MTR_5g030920.
DR eggNOG; ENOG502QRK1; Eukaryota.
DR OrthoDB; 684563at2759; -.
DR ExpressionAtlas; Q8L4H4; 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:0004672; F:protein kinase activity; IDA:UniProtKB.
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:0009877; P:nodulation; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR024788; Malectin-like_Carb-bd_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
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; Coiled coil; Kinase; Leucine-rich repeat; Membrane;
KW Nodulation; Nucleotide-binding; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..925
FT /note="Nodulation receptor kinase"
FT /id="PRO_0000024364"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 408..430
FT /note="LRR 1"
FT REPEAT 432..454
FT /note="LRR 2"
FT REPEAT 455..476
FT /note="LRR 3"
FT REPEAT 479..500
FT /note="LRR 4"
FT DOMAIN 596..873
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT COILED 362..384
FT /evidence="ECO:0000255"
FT ACT_SITE 722
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 602..610
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 624
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 343..367
FT /note="NAYEILQARSWIEETNQKDLEVIQK->KPMKSCRHGRGLKRPTKKIWKLFRR
FT : In dmi2-1/DMI2/TR25; loss of nodulation and mycorrhizal
FT infection."
FT MUTAGEN 368..925
FT /note="Missing: In dmi2-1/DMI2/TR25; loss of nodulation and
FT mycorrhizal infection."
FT MUTAGEN 436..458
FT /note="Missing: In dmi2-3/P1; loss of nodulation and
FT mycorrhizal infection."
FT /evidence="ECO:0000269|PubMed:12087406"
FT MUTAGEN 795
FT /note="G->E: In dmi2-4/NN1/R38; loss of nodulation, but no
FT effect on mycorrhizal infection."
FT /evidence="ECO:0000269|PubMed:12087406"
SQ SEQUENCE 925 AA; 104181 MW; 25057428D2204A42 CRC64;
MMELQVIRIF RLVVAFVLCL CIFIRSASSA TKGFESIACC ADSNYTDPKT TLTYTTDHIW
FSDKRSCRQI PEILFSHRSN KNVRKFEIYE GKRCYNLPTV KDQVYLIRGI FPFDSLNSSF
YVSIGVTELG ELRSSRLEDL EIEGVFRATK DYIDFCLLKE DVNPFISQIE LRPLPEEYLH
GFGTSVLKLI SRNNLGDTND DIRFPDDQND RIWKRKETST PTSALPLSFN VSNVDLKDSV
TPPLQVLQTA LTHPERLEFV HDGLETDDYE YSVFLHFLEL NGTVRAGQRV FDIYLNNEIK
KEKFDVLAGG SKNSYTALNI SANGSLNITL VKASGSEFGP LLNAYEILQA RSWIEETNQK
DLEVIQKMRE ELLLHNQENE ALESWSGDPC MIFPWKGITC DDSTGSSIIT KLDLSSNNLK
GAIPSIVTKM TNLQILNLSH NQFDMLFPSF PPSSLLISLD LSYNDLSGWL PESIISLPHL
KSLYFGCNPS MSDEDTTKLN SSLINTDYGR CKAKKPKFGQ VFVIGAITSG SLLITLAVGI
LFFCRYRHKS ITLEGFGKTY PMATNIIFSL PSKDDFFIKS VSVKPFTLEY IEQATEQYKT
LIGEGGFGSV YRGTLDDGQE VAVKVRSSTS TQGTREFDNE LNLLSAIQHE NLVPLLGYCN
EYDQQILVYP FMSNGSLLDR LYGEASKRKI LDWPTRLSIA LGAARGLAYL HTFPGRSVIH
RDVKSSNILL DQSMCAKVAD FGFSKYAPQE GDSYVSLEVR GTAGYLDPEY YKTQQLSEKS
DVFSFGVVLL EIVSGREPLN IKRPRIEWSL VEWAKPYIRA SKVDEIVDPG IKGGYHAEAL
WRVVEVALQC LEPYSTYRPC MVDIVRELED ALIIENNASE YMKSIDSLGG SNRYSIVMDK
RALPSTTSTA ESTITTQTLS HPQPR
