PXL1_ARATH
ID PXL1_ARATH Reviewed; 1029 AA.
AC Q9FRS6;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Leucine-rich repeat receptor-like protein kinase PXL1;
DE EC=2.7.11.1;
DE AltName: Full=Protein PHLOEM INTERCALATED WITH XYLEM-LIKE 1;
DE Flags: Precursor;
GN Name=PXL1; OrderedLocusNames=At1g08590; ORFNames=F22O13.7;
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 MRNA].
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 [2]
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 [3]
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17570668; DOI=10.1016/j.cub.2007.05.049;
RA Fisher K., Turner S.;
RT "PXY, a receptor-like kinase essential for maintaining polarity during
RT plant vascular-tissue development.";
RL Curr. Biol. 17:1061-1066(2007).
RN [5]
RP REVIEW.
RX PubMed=20016993; DOI=10.1007/s00709-009-0095-y;
RA Wang G., Fiers M.;
RT "CLE peptide signaling during plant development.";
RL Protoplasma 240:33-43(2010).
RN [6]
RP FUNCTION, INTERACTION WITH HIRD11, AND SUBCELLULAR LOCATION.
RX PubMed=25602612; DOI=10.1016/j.jplph.2015.01.001;
RA Jung C.G., Hwang S.G., Park Y.C., Park H.M., Kim D.S., Park D.H.,
RA Jang C.S.;
RT "Molecular characterization of the cold- and heat-induced Arabidopsis PXL1
RT gene and its potential role in transduction pathways under temperature
RT fluctuations.";
RL J. Plant Physiol. 176:138-146(2015).
CC -!- FUNCTION: Involved in the regulation of procambium maintenance and
CC polarity during vascular-tissue development (PubMed:17570668).
CC Phosphorylates HIRD11 and LHCA1 in vitro (PubMed:25602612).
CC {ECO:0000269|PubMed:17570668}.
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 -!- SUBUNIT: Interacts with HIRD11. {ECO:0000269|PubMed:25602612}.
CC -!- INTERACTION:
CC Q9FRS6; Q9SH71: At1g64210; NbExp=2; IntAct=EBI-16946268, EBI-20651385;
CC Q9FRS6; Q9LJF3: BRL3; NbExp=3; IntAct=EBI-16946268, EBI-20651413;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25602612};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Reduced procambial cells number, and adjacent or
CC interspersed xylem and phloem formation. {ECO:0000269|PubMed:17570668}.
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; FJ708630; ACN59226.1; -; mRNA.
DR EMBL; AC003981; AAF99755.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28312.1; -; Genomic_DNA.
DR PIR; T00712; T00712.
DR RefSeq; NP_172335.1; NM_100732.3.
DR AlphaFoldDB; Q9FRS6; -.
DR SMR; Q9FRS6; -.
DR BioGRID; 22622; 65.
DR IntAct; Q9FRS6; 44.
DR STRING; 3702.AT1G08590.1; -.
DR PaxDb; Q9FRS6; -.
DR PRIDE; Q9FRS6; -.
DR ProteomicsDB; 226135; -.
DR EnsemblPlants; AT1G08590.1; AT1G08590.1; AT1G08590.
DR GeneID; 837381; -.
DR Gramene; AT1G08590.1; AT1G08590.1; AT1G08590.
DR KEGG; ath:AT1G08590; -.
DR Araport; AT1G08590; -.
DR TAIR; locus:2025545; AT1G08590.
DR eggNOG; ENOG502QPWI; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9FRS6; -.
DR OMA; FPYGLGM; -.
DR OrthoDB; 89025at2759; -.
DR PhylomeDB; Q9FRS6; -.
DR PRO; PR:Q9FRS6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FRS6; baseline and differential.
DR Genevisible; Q9FRS6; AT.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR GO; GO:0010067; P:procambium histogenesis; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 9.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Developmental protein; Differentiation;
KW Glycoprotein; Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW Phosphoprotein; 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..1029
FT /note="Leucine-rich repeat receptor-like protein kinase
FT PXL1"
FT /id="PRO_0000401292"
FT TOPO_DOM 24..644
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 666..1029
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 81..100
FT /note="LRR 1"
FT REPEAT 101..124
FT /note="LRR 2"
FT REPEAT 126..148
FT /note="LRR 3"
FT REPEAT 149..172
FT /note="LRR 4"
FT REPEAT 174..195
FT /note="LRR 5"
FT REPEAT 196..222
FT /note="LRR 6"
FT REPEAT 224..243
FT /note="LRR 7"
FT REPEAT 244..268
FT /note="LRR 8"
FT REPEAT 269..292
FT /note="LRR 9"
FT REPEAT 293..316
FT /note="LRR 10"
FT REPEAT 317..339
FT /note="LRR 11"
FT REPEAT 341..364
FT /note="LRR 12"
FT REPEAT 365..388
FT /note="LRR 13"
FT REPEAT 389..412
FT /note="LRR 14"
FT REPEAT 414..436
FT /note="LRR 15"
FT REPEAT 437..461
FT /note="LRR 16"
FT REPEAT 463..483
FT /note="LRR 17"
FT REPEAT 485..507
FT /note="LRR 18"
FT REPEAT 508..531
FT /note="LRR 19"
FT REPEAT 532..555
FT /note="LRR 20"
FT REPEAT 556..579
FT /note="LRR 21"
FT REPEAT 581..604
FT /note="LRR 22"
FT DOMAIN 714..1007
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 854
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 720..728
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 744
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 706
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 801
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 841
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 895
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 902
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 903
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1029 AA; 113820 MW; FC41C89E0B558728 CRC64;
MAIPRLFFLF YYIGFALFPF VSSETFQNSE QEILLAFKSD LFDPSNNLQD WKRPENATTF
SELVHCHWTG VHCDANGYVA KLLLSNMNLS GNVSDQIQSF PSLQALDLSN NAFESSLPKS
LSNLTSLKVI DVSVNSFFGT FPYGLGMATG LTHVNASSNN FSGFLPEDLG NATTLEVLDF
RGGYFEGSVP SSFKNLKNLK FLGLSGNNFG GKVPKVIGEL SSLETIILGY NGFMGEIPEE
FGKLTRLQYL DLAVGNLTGQ IPSSLGQLKQ LTTVYLYQNR LTGKLPRELG GMTSLVFLDL
SDNQITGEIP MEVGELKNLQ LLNLMRNQLT GIIPSKIAEL PNLEVLELWQ NSLMGSLPVH
LGKNSPLKWL DVSSNKLSGD IPSGLCYSRN LTKLILFNNS FSGQIPEEIF SCPTLVRVRI
QKNHISGSIP AGSGDLPMLQ HLELAKNNLT GKIPDDIALS TSLSFIDISF NHLSSLSSSI
FSSPNLQTFI ASHNNFAGKI PNQIQDRPSL SVLDLSFNHF SGGIPERIAS FEKLVSLNLK
SNQLVGEIPK ALAGMHMLAV LDLSNNSLTG NIPADLGASP TLEMLNVSFN KLDGPIPSNM
LFAAIDPKDL VGNNGLCGGV LPPCSKSLAL SAKGRNPGRI HVNHAVFGFI VGTSVIVAMG
MMFLAGRWIY TRWDLYSNFA REYIFCKKPR EEWPWRLVAF QRLCFTAGDI LSHIKESNII
GMGAIGIVYK AEVMRRPLLT VAVKKLWRSP SPQNDIEDHH QEEDEEDDIL REVNLLGGLR
HRNIVKILGY VHNEREVMMV YEYMPNGNLG TALHSKDEKF LLRDWLSRYN VAVGVVQGLN
YLHNDCYPPI IHRDIKSNNI LLDSNLEARI ADFGLAKMML HKNETVSMVA GSYGYIAPEY
GYTLKIDEKS DIYSLGVVLL ELVTGKMPID PSFEDSIDVV EWIRRKVKKN ESLEEVIDAS
IAGDCKHVIE EMLLALRIAL LCTAKLPKDR PSIRDVITML AEAKPRRKSV CQVAGDLPIF
RNSPVVGLI
