CLV1B_SOYBN
ID CLV1B_SOYBN Reviewed; 987 AA.
AC Q9M6A7; Q8GSN9;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Leucine-rich repeat receptor-like kinase protein CLV1B {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=CLAVATA1-like protein 1B {ECO:0000303|PubMed:10760600};
DE Short=GmCLV1B {ECO:0000303|PubMed:10760600};
DE AltName: Full=Nodule autoregulation receptor protein kinase {ECO:0000303|PubMed:12411574};
DE Short=GmNARK {ECO:0000303|PubMed:12411574};
DE AltName: Full=Protein NITRATE-TOLERANT SUPERNODULATING 1 {ECO:0000303|PubMed:12442172};
DE Flags: Precursor;
GN Name=CLV1B {ECO:0000303|PubMed:10760600};
GN Synonyms=NARK {ECO:0000303|PubMed:12411574},
GN NTS1 {ECO:0000303|PubMed:12442172};
GN ORFNames=GLYMA_12G040000 {ECO:0000312|EMBL:KRH24413.1};
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10760600; DOI=10.1016/s0167-4781(00)00061-0;
RA Yamamoto E., Karakaya H.C., Knap H.T.;
RT "Molecular characterization of two soybean homologs of Arabidopsis thaliana
RT CLAVATA1 from the wild type and fasciation mutant.";
RL Biochim. Biophys. Acta 1491:333-340(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12411574; DOI=10.1126/science.1077937;
RA Searle I.R., Men A.E., Laniya T.S., Buzas D.M., Iturbe-Ormaetxe I.,
RA Carroll B.J., Gresshoff P.M.;
RT "Long-distance signaling in nodulation directed by a CLAVATA1-like receptor
RT kinase.";
RL Science 299:109-112(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
CC -!- FUNCTION: LRR receptor kinase involved in the regulation of root and
CC shoot growth, and root nodule organogenesis (PubMed:12411574). Involved
CC in long distance nodulation signaling events (PubMed:12411574).
CC Involved in the autoregulation of nodulation (AON), a long distance
CC systemic signaling from root to shoot and back again, which allows
CC legumes to limit the number of root nodules formed based on available
CC nitrogen and previous rhizobial colonization (PubMed:12411574). Acts
CC from shoot to root to control AON (PubMed:12411574).
CC {ECO:0000269|PubMed:12411574}.
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, vegetative shoot apex,
CC and reproductive floral apex. {ECO:0000269|PubMed:10760600}.
CC -!- DISRUPTION PHENOTYPE: Dramatic increase in root nodule number when
CC inoculated with symbiotic rhizobia. {ECO:0000269|PubMed:12411574}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41332.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF197947; AAF59906.1; -; mRNA.
DR EMBL; AB092811; BAC41332.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY166655; AAN74865.1; -; Genomic_DNA.
DR EMBL; AP009560; BAX25285.1; -; Genomic_DNA.
DR EMBL; CM000845; KRH24413.1; -; Genomic_DNA.
DR PIR; T50850; T50850.
DR RefSeq; NP_001238004.1; NM_001251075.1.
DR AlphaFoldDB; Q9M6A7; -.
DR SMR; Q9M6A7; -.
DR STRING; 3847.GLYMA12G04390.1; -.
DR PRIDE; Q9M6A7; -.
DR EnsemblPlants; KRH24413; KRH24413; GLYMA_12G040000.
DR GeneID; 732625; -.
DR Gramene; KRH24413; KRH24413; GLYMA_12G040000.
DR KEGG; gmx:732625; -.
DR eggNOG; ENOG502QQ4T; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9M6A7; -.
DR OMA; GQFMVFN; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000008827; Chromosome 12.
DR ExpressionAtlas; Q9M6A7; baseline and differential.
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: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: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; PF13516; LRR_6; 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; 10.
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; Cell membrane; Differentiation; Glycoprotein;
KW Growth regulation; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..987
FT /note="Leucine-rich repeat receptor-like kinase protein
FT CLV1B"
FT /evidence="ECO:0000255"
FT /id="PRO_5014589467"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 96..120
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 122..144
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 145..169
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 170..192
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 193..217
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 219..241
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 242..266
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 267..290
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 292..314
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 315..337
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 338..362
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 364..386
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 387..410
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 411..434
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 435..458
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 460..481
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 482..505
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 507..529
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 530..553
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 555..577
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 578..602
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT DOMAIN 696..985
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 821
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 702..710
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 724
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 987 AA; 108908 MW; 97BCC247DF59F8B7 CRC64;
MRSCVCYTLL LFIFFIWLRV ATCSSFTDME SLLKLKDSMK GDKAKDDALH DWKFFPSLSA
HCFFSGVKCD RELRVVAINV SFVPLFGHLP PEIGQLDKLE NLTVSQNNLT GVLPKELAAL
TSLKHLNISH NVFSGHFPGQ IILPMTKLEV LDVYDNNFTG PLPVELVKLE KLKYLKLDGN
YFSGSIPESY SEFKSLEFLS LSTNSLSGKI PKSLSKLKTL RYLKLGYNNA YEGGIPPEFG
SMKSLRYLDL SSCNLSGEIP PSLANLTNLD TLFLQINNLT GTIPSELSAM VSLMSLDLSI
NDLTGEIPMS FSQLRNLTLM NFFQNNLRGS VPSFVGELPN LETLQLWDNN FSFVLPPNLG
QNGKLKFFDV IKNHFTGLIP RDLCKSGRLQ TIMITDNFFR GPIPNEIGNC KSLTKIRASN
NYLNGVVPSG IFKLPSVTII ELANNRFNGE LPPEISGESL GILTLSNNLF SGKIPPALKN
LRALQTLSLD ANEFVGEIPG EVFDLPMLTV VNISGNNLTG PIPTTLTRCV SLTAVDLSRN
MLEGKIPKGI KNLTDLSIFN VSINQISGPV PEEIRFMLSL TTLDLSNNNF IGKVPTGGQF
AVFSEKSFAG NPNLCTSHSC PNSSLYPDDA LKKRRGPWSL KSTRVIVIVI ALGTAALLVA
VTVYMMRRRK MNLAKTWKLT AFQRLNFKAE DVVECLKEEN IIGKGGAGIV YRGSMPNGTD
VAIKRLVGAG SGRNDYGFKA EIETLGKIRH RNIMRLLGYV SNKETNLLLY EYMPNGSLGE
WLHGAKGGHL KWEMRYKIAV EAAKGLCYLH HDCSPLIIHR DVKSNNILLD GDLEAHVADF
GLAKFLYDPG ASQSMSSIAG SYGYIAPEYA YTLKVDEKSD VYSFGVVLLE LIIGRKPVGE
FGDGVDIVGW VNKTRLELAQ PSDAALVLAV VDPRLSGYPL TSVIYMFNIA MMCVKEMGPA
RPTMREVVHM LSEPPHSATH THNLINL
