CLV1A_SOYBN
ID CLV1A_SOYBN Reviewed; 981 AA.
AC A0A0R0HPY5; Q9M6A8;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Leucine-rich repeat receptor-like kinase protein CLV1a {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=CLAVATA1-like protein 1A {ECO:0000303|PubMed:10760600};
DE Short=GmCLV1A {ECO:0000303|PubMed:10760600};
DE Flags: Precursor;
GN Name=CLV1A {ECO:0000303|PubMed:10760600};
GN ORFNames=GLYMA_11G114100 {ECO:0000312|EMBL:KRH29397.1};
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 [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 plant
CC growth. {ECO:0000250|UniProtKB:Q9M6A7}.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF197946; AAF59905.1; -; mRNA.
DR EMBL; CM000844; KRH29397.1; -; Genomic_DNA.
DR PIR; T50851; T50851.
DR RefSeq; NP_001238576.1; NM_001251647.1.
DR AlphaFoldDB; A0A0R0HPY5; -.
DR SMR; A0A0R0HPY5; -.
DR STRING; 3847.GLYMA11G12186.1; -.
DR EnsemblPlants; KRH29397; KRH29397; GLYMA_11G114100.
DR GeneID; 732661; -.
DR Gramene; KRH29397; KRH29397; GLYMA_11G114100.
DR KEGG; gmx:732661; -.
DR OMA; MMCVEND; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000008827; Chromosome 11.
DR ExpressionAtlas; A0A0R0HPY5; 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; 8.
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; 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..981
FT /note="Leucine-rich repeat receptor-like kinase protein
FT CLV1a"
FT /evidence="ECO:0000255"
FT /id="PRO_5014521660"
FT TRANSMEM 639..659
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..313
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 314..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 388..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 554..578
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 580..602
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT DOMAIN 690..973
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 815
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 696..704
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 718
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 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"
FT CONFLICT 971
FT /note="S -> F (in Ref. 1; AAF59905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 981 AA; 108507 MW; 59520B08FD258C29 CRC64;
MRSCVCYTLL LFVFFIWLHV ATCSSFSDMD ALLKLKESMK GDRAKDDALH DWKFSTSLSA
HCFFSGVSCD QELRVVAINV SFVPLFGHVP PEIGELDKLE NLTISQNNLT GELPKELAAL
TSLKHLNISH NVFSGYFPGK IILPMTELEV LDVYDNNFTG SLPEEFVKLE KLKYLKLDGN
YFSGSIPESY SEFKSLEFLS LSTNSLSGNI PKSLSKLKTL RILKLGYNNA YEGGIPPEFG
TMESLKYLDL SSCNLSGEIP PSLANMRNLD TLFLQMNNLT GTIPSELSDM VSLMSLDLSF
NGLTGEIPTR FSQLKNLTLM NFFHNNLRGS VPSFVGELPN LETLQLWENN FSSELPQNLG
QNGKFKFFDV TKNHFSGLIP RDLCKSGRLQ TFLITDNFFH GPIPNEIANC KSLTKIRASN
NYLNGAVPSG IFKLPSVTII ELANNRFNGE LPPEISGDSL GILTLSNNLF TGKIPPALKN
LRALQTLSLD TNEFLGEIPG EVFDLPMLTV VNISGNNLTG PIPTTFTRCV SLAAVDLSRN
MLDGEIPKGM KNLTDLSIFN VSINQISGSV PDEIRFMLSL TTLDLSYNNF IGKVPTGGQF
LVFSDKSFAG NPNLCSSHSC PNSSLKKRRG PWSLKSTRVI VMVIALATAA ILVAGTEYMR
RRRKLKLAMT WKLTGFQRLN LKAEEVVECL KEENIIGKGG AGIVYRGSMR NGSDVAIKRL
VGAGSGRNDY GFKAEIETVG KIRHRNIMRL LGYVSNKETN LLLYEYMPNG SLGEWLHGAK
GGHLKWEMRY KIAVEAAKGL CYLHHDCSPL IIHRDVKSNN ILLDAHFEAH VADFGLAKFL
YDLGSSQSMS SIAGSYGYIA PEYAYTLKVD EKSDVYSFGV VLLELIIGRK PVGEFGDGVD
IVGWVNKTRL ELSQPSDAAV VLAVVDPRLS GYPLISVIYM FNIAMMCVKE VGPTRPTMRE
VVHMLSNPPH STTHTHNLIN L
