RGI5_ARATH
ID RGI5_ARATH Reviewed; 1072 AA.
AC C0LGF5; Q9FX19;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase RGI5;
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Protein RECEPTOR OF RGF1 5 {ECO:0000303|PubMed:27229311};
DE AltName: Full=Protein RGF1 INSENSITIVE 5 {ECO:0000303|PubMed:27229312};
DE Flags: Precursor;
GN Name=RGI5 {ECO:0000303|PubMed:27229312};
GN Synonyms=RGFR5 {ECO:0000303|PubMed:27229311};
GN OrderedLocusNames=At1g34110 {ECO:0000312|Araport:AT1G34110};
GN ORFNames=F12G12.7 {ECO:0000312|EMBL:AAG12526.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-1072.
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INTERACTION WITH RGF1, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=27229311; DOI=10.1038/cr.2016.62;
RA Song W., Liu L., Wang J., Wu Z., Zhang H., Tang J., Lin G., Wang Y.,
RA Wen X., Li W., Han Z., Guo H., Chai J.;
RT "Signature motif-guided identification of receptors for peptide hormones
RT essential for root meristem growth.";
RL Cell Res. 26:674-685(2016).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=27229312; DOI=10.1038/cr.2016.63;
RA Ou Y., Lu X., Zi Q., Xun Q., Zhang J., Wu Y., Shi H., Wei Z., Zhao B.,
RA Zhang X., He K., Gou X., Li C., Li J.;
RT "RGF1 INSENSITIVE 1 to 5, a group of LRR receptor-like kinases, are
RT essential for the perception of root meristem growth factor 1 in
RT Arabidopsis thaliana.";
RL Cell Res. 26:686-698(2016).
CC -!- FUNCTION: Together with RGI1, RGI2, RGI3 and RGI4, acts as receptor of
CC RGF1, a peptide hormone that maintains the postembryonic root stem cell
CC niche by regulating the expression levels and patterns of the
CC transcription factor PLETHORA (PLT) (PubMed:27229312, PubMed:27229311).
CC Links RGF1 signal with its downstream components (PubMed:27229311).
CC {ECO:0000269|PubMed:27229311, ECO:0000269|PubMed:27229312}.
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:0000255|PROSITE-ProRule:PRU00159};
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:0000255|PROSITE-ProRule:PRU00159};
CC -!- SUBUNIT: Binds to RGF1; this interaction triggers the formation of
CC heterodimers with SERK1. {ECO:0000269|PubMed:27229311}.
CC -!- INTERACTION:
CC C0LGF5; Q9LJY0: PRK4; NbExp=2; IntAct=EBI-16964286, EBI-16914444;
CC C0LGF5; Q9LVI6: RLK902; NbExp=2; IntAct=EBI-16964286, EBI-1626936;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and hypocotyls.
CC {ECO:0000269|PubMed:27229311}.
CC -!- DEVELOPMENTAL STAGE: Present in the whole roots.
CC {ECO:0000269|PubMed:27229311}.
CC -!- PTM: Phosphorylated and ubiquitinated upon interaction with RGF1, thus
CC leading to activation a subsequent degradation.
CC {ECO:0000250|UniProtKB:Q9LHP4}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O22476}.
CC -!- DISRUPTION PHENOTYPE: Smaller root meristem size and fewer root
CC meristematic cortex cells, associated with shorter roots and a slighty
CC reduced sensitivity to RGF1 (PubMed:27229311). Quintuple mutants rgi1
CC rgi2 rgi3 rgi4 rgi5 display a consistent short primary root phenotype
CC with a small size of meristem associated with a total insensitivity to
CC RGF1 and undetectable levels of PLT1 and PLT2 (PubMed:27229312).
CC {ECO:0000269|PubMed:27229311, ECO:0000269|PubMed:27229312}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG12526.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC015446; AAG12526.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31671.1; -; Genomic_DNA.
DR EMBL; FJ708644; ACN59240.1; -; mRNA.
DR PIR; B86465; B86465.
DR RefSeq; NP_174673.3; NM_103134.4.
DR AlphaFoldDB; C0LGF5; -.
DR SMR; C0LGF5; -.
DR BioGRID; 25542; 27.
DR IntAct; C0LGF5; 29.
DR STRING; 3702.AT1G34110.1; -.
DR PaxDb; C0LGF5; -.
DR PRIDE; C0LGF5; -.
DR ProteomicsDB; 242430; -.
DR EnsemblPlants; AT1G34110.1; AT1G34110.1; AT1G34110.
DR GeneID; 840310; -.
DR Gramene; AT1G34110.1; AT1G34110.1; AT1G34110.
DR KEGG; ath:AT1G34110; -.
DR Araport; AT1G34110; -.
DR TAIR; locus:2009071; AT1G34110.
DR eggNOG; ENOG502QSRW; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; C0LGF5; -.
DR OrthoDB; 116688at2759; -.
DR PhylomeDB; C0LGF5; -.
DR PRO; PR:C0LGF5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0LGF5; baseline and differential.
DR Genevisible; C0LGF5; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0001653; F:peptide receptor activity; IMP: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:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0010074; P:maintenance of meristem identity; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010082; P:regulation of root meristem growth; IGI:TAIR.
DR Gene3D; 3.80.10.10; -; 6.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 10.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 16.
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; Disulfide bond; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1072
FT /note="LRR receptor-like serine/threonine-protein kinase
FT RGI5"
FT /id="PRO_0000387526"
FT TOPO_DOM 22..706
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 728..1072
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 66..89
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 90..113
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 114..138
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 140..162
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 164..185
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 187..211
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 212..234
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 235..259
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 260..283
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 285..307
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 308..331
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 332..355
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 356..379
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 381..402
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 403..427
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 429..451
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 452..475
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 477..499
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 500..523
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 524..546
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 548..571
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 572..595
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 597..619
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 620..642
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 643..667
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT DOMAIN 772..1067
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 171..172
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 193..196
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 216..221
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 244
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 266..268
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 314..317
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 336..338
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 384..388
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 410..413
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 432..436
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 456..458
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT ACT_SITE 900
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 778..786
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 800
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 800
FT /note="Essential for autophosphorylation activity"
FT /evidence="ECO:0000250|UniProtKB:Q9LHP4"
FT MOD_RES 764
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 851
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 887
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 944
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 951
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 952
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 97
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 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 650
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 56..63
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
SQ SEQUENCE 1072 AA; 116725 MW; 3A5348584E41C766 CRC64;
MERERSNFFF LFLFCSWVSM AQPTLSLSSD GQALLSLKRP SPSLFSSWDP QDQTPCSWYG
ITCSADNRVI SVSIPDTFLN LSSIPDLSSL SSLQFLNLSS TNLSGPIPPS FGKLTHLRLL
DLSSNSLSGP IPSELGRLST LQFLILNANK LSGSIPSQIS NLFALQVLCL QDNLLNGSIP
SSFGSLVSLQ QFRLGGNTNL GGPIPAQLGF LKNLTTLGFA ASGLSGSIPS TFGNLVNLQT
LALYDTEISG TIPPQLGLCS ELRNLYLHMN KLTGSIPKEL GKLQKITSLL LWGNSLSGVI
PPEISNCSSL VVFDVSANDL TGDIPGDLGK LVWLEQLQLS DNMFTGQIPW ELSNCSSLIA
LQLDKNKLSG SIPSQIGNLK SLQSFFLWEN SISGTIPSSF GNCTDLVALD LSRNKLTGRI
PEELFSLKRL SKLLLLGNSL SGGLPKSVAK CQSLVRLRVG ENQLSGQIPK EIGELQNLVF
LDLYMNHFSG GLPYEISNIT VLELLDVHNN YITGDIPAQL GNLVNLEQLD LSRNSFTGNI
PLSFGNLSYL NKLILNNNLL TGQIPKSIKN LQKLTLLDLS YNSLSGEIPQ ELGQVTSLTI
NLDLSYNTFT GNIPETFSDL TQLQSLDLSS NSLHGDIKVL GSLTSLASLN ISCNNFSGPI
PSTPFFKTIS TTSYLQNTNL CHSLDGITCS SHTGQNNGVK SPKIVALTAV ILASITIAIL
AAWLLILRNN HLYKTSQNSS SSPSTAEDFS YPWTFIPFQK LGITVNNIVT SLTDENVIGK
GCSGIVYKAE IPNGDIVAVK KLWKTKDNNE EGESTIDSFA AEIQILGNIR HRNIVKLLGY
CSNKSVKLLL YNYFPNGNLQ QLLQGNRNLD WETRYKIAIG AAQGLAYLHH DCVPAILHRD
VKCNNILLDS KYEAILADFG LAKLMMNSPN YHNAMSRVAG SYGYIAPEYG YTMNITEKSD
VYSYGVVLLE ILSGRSAVEP QIGDGLHIVE WVKKKMGTFE PALSVLDVKL QGLPDQIVQE
MLQTLGIAMF CVNPSPVERP TMKEVVTLLM EVKCSPEEWG KTSQPLIKPS SS
