NORK_PEA
ID NORK_PEA Reviewed; 924 AA.
AC Q8LKZ1; Q8L6F1; Q8L6F2; Q8L6F3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Nodulation receptor kinase;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=NORK; Synonyms=SYM19;
OS Pisum sativum (Garden pea).
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; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Frisson;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF GLY-604 AND ASP-739.
RC STRAIN=cv. Frisson;
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 [3]
RP FUNCTION.
RX PubMed=11078515; DOI=10.1073/pnas.230440097;
RA Walker S.A., Viprey V., Downie J.A.;
RT "Dissection of nodulation signaling using pea mutants defective for calcium
RT spiking induced by nod factors and chitin oligomers.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13413-13418(2000).
CC -!- FUNCTION: Involved in the perception of symbiotic fungi and bacteria
CC and required for the calcium spiking. Part of the
CC perception/transduction system leading to nodulation or mycorrhizal
CC infection. {ECO:0000269|PubMed:11078515}.
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 -!- PTM: May be phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD10806.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD10812.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD10813.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF491997; AAM76684.1; -; mRNA.
DR EMBL; AJ418375; CAD10812.1; ALT_INIT; mRNA.
DR EMBL; AJ418367; CAD10806.1; ALT_INIT; mRNA.
DR EMBL; AJ418376; CAD10813.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q8LKZ1; -.
DR SMR; Q8LKZ1; -.
DR PRIDE; Q8LKZ1; -.
DR EnsemblPlants; Psat2g134080.1; Psat2g134080.1.cds; Psat2g134080.
DR EnsemblPlants; Psat2g134120.1; Psat2g134120.1.cds; Psat2g134120.
DR Gramene; Psat2g134080.1; Psat2g134080.1.cds; Psat2g134080.
DR Gramene; Psat2g134120.1; Psat2g134120.1.cds; Psat2g134120.
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:0009877; P:nodulation; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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..924
FT /note="Nodulation receptor kinase"
FT /id="PRO_0000024365"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 406..428
FT /note="LRR 1"
FT REPEAT 430..452
FT /note="LRR 2"
FT REPEAT 453..475
FT /note="LRR 3"
FT REPEAT 477..498
FT /note="LRR 4"
FT DOMAIN 595..872
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT COILED 361..382
FT /evidence="ECO:0000255"
FT ACT_SITE 721
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 601..609
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 623
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 604
FT /note="G->E: In P4; loss of nodulation and mycorrhizal
FT infection."
FT /evidence="ECO:0000269|PubMed:12087406"
FT MUTAGEN 739
FT /note="D->N: In P55/F4-141; loss of nodulation and
FT mycorrhizal infection."
FT /evidence="ECO:0000269|PubMed:12087406"
SQ SEQUENCE 924 AA; 103732 MW; 1732BBBECEB70C6B CRC64;
MMELRVICII RLVVACVLCL CIFIRSASSA TEGFESIACC ADSNYTDPKT NLNYTTDYRW
YSDKSNCRQI PEILLSHRSN INFRLFDIDE GKRCYNLPTI KDQVYLIRGT FPFDSVNTSF
YVSIGATELG EVTSSRLEDL EIEGVFRAPK DNIDFCLLKE DVNPFISQLE LRPLPEEYLH
DFSTNVLKLI SRNNLCGIED DIRFPVDQND RIWKATSTPS YALPLSFNVS NVELNGKVTP
PLQVLQTALT HPERLEFVHV GLETDDYEYS VLLYFLELND TLKAGQRVFD IYLNSEIKKE
GFDVLEGGSK YSYTVLNISA NGSLNITLVK ASGSKFGPLL NAYEILQARP WIDETDQTDL
EVIQKMRKEL LLQNQDNEAL ESWSGDPCML FPWKGVACDG SNGSSVITKL DLSSSNLKGT
IPSSVTEMTK LQILNLSHNH FDGYIPSFPP SSLLISVDLS YNDLTGQLPE SIISLPHLNS
LYFGCNQHMR DDDEAKLNSS LINTDYGRCN AKKPKFGQVF MIGAITSGSI LITLAVVILF
FCRYRHKSIT LEGFGGKTYP MATNIIFSLP SKDDFFIKSV SVKPFTLEYI ELATEKYKTL
IGEGGFGSVY RGTLDDGQEV AVKVRSATST QGTREFDNEL NLLSAIQHEN LVPLLGYCNE
YDQQILVYPF MSNGSLLDRL YGEPAKRKIL DWPTRLSIAL GAARGLAYLH TFPGRSVIHR
DVKSSNILLD HSMCAKVADF GFSKYAPQEG DSYVSLEVRG TAGYLDPEYY KTQQLSEKSD
VFSFGVVLLE IVSGREPLNI KRPRVEWSLV EWAKPYIRAS KVDEIVDPGI KGGYHAEALW
RVVEVALQCL EPYSTYRPCM VDIVRELEDA LIIENNASEY MKSIDSLGGS NRYSIVMDKR
ALPSTTSTAE STITTQNVSH PQPR
