PXC1_ARATH
ID PXC1_ARATH Reviewed; 672 AA.
AC Q9SJQ1; Q0WSR7;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Leucine-rich repeat receptor-like protein kinase PXC1 {ECO:0000305};
DE AltName: Full=Protein PXY/TDR-CORRELATED 1 {ECO:0000303|PubMed:23815750};
DE Flags: Precursor;
GN Name=PXC1 {ECO:0000303|PubMed:23815750};
GN OrderedLocusNames=At2g36570 {ECO:0000312|Araport:AT2G36570};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-111, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23815750; DOI=10.1186/1471-2229-13-94;
RA Wang J., Kucukoglu M., Zhang L., Chen P., Decker D., Nilsson O., Jones B.,
RA Sandberg G., Zheng B.;
RT "The Arabidopsis LRR-RLK, PXC1, is a regulator of secondary wall formation
RT correlated with the TDIF-PXY/TDR-WOX4 signaling pathway.";
RL BMC Plant Biol. 13:94-94(2013).
CC -!- FUNCTION: Leucine-rich repeat receptor-like protein kinase involved in
CC secondary cell wall formation in xylem fibers. May play a role in a
CC regulatory network which also incorporates the TDR/PXY signaling
CC pathway and regulates the maturation of interfascicular fiber cells.
CC May promote the initiation of secondary cell wall deposition during the
CC procedure of cell expansion. {ECO:0000269|PubMed:23815750}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular strands of cotyledons,
CC the shoot apex, hypocotyls, roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:23815750}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but under short day conditions inflorescence stems of
CC mutant plants show dramatic reduction of secondary cell wall formation
CC in xylem fibers, leading to the inability of the stems to support an
CC upright growth. {ECO:0000269|PubMed:23815750}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AC006919; AAD24639.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09269.1; -; Genomic_DNA.
DR EMBL; FJ708710; ACN59305.1; -; mRNA.
DR EMBL; AK227854; BAE99831.1; -; mRNA.
DR PIR; B84782; B84782.
DR RefSeq; NP_181196.1; NM_129213.3.
DR AlphaFoldDB; Q9SJQ1; -.
DR SMR; Q9SJQ1; -.
DR IntAct; Q9SJQ1; 4.
DR STRING; 3702.AT2G36570.1; -.
DR iPTMnet; Q9SJQ1; -.
DR PaxDb; Q9SJQ1; -.
DR PRIDE; Q9SJQ1; -.
DR ProteomicsDB; 226024; -.
DR EnsemblPlants; AT2G36570.1; AT2G36570.1; AT2G36570.
DR GeneID; 818230; -.
DR Gramene; AT2G36570.1; AT2G36570.1; AT2G36570.
DR KEGG; ath:AT2G36570; -.
DR Araport; AT2G36570; -.
DR TAIR; locus:2044913; AT2G36570.
DR eggNOG; ENOG502QPUR; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR OMA; HGHRMSG; -.
DR OrthoDB; 474027at2759; -.
DR PhylomeDB; Q9SJQ1; -.
DR PRO; PR:Q9SJQ1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJQ1; baseline and differential.
DR Genevisible; Q9SJQ1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Isopeptide bond;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..672
FT /note="Leucine-rich repeat receptor-like protein kinase
FT PXC1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432871"
FT TOPO_DOM 22..269
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..672
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 87..110
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 112..134
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 135..158
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 160..181
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 182..205
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT DOMAIN 357..645
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 233..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 363..371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 44
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 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CROSSLNK 111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT CONFLICT 208
FT /note="D -> N (in Ref. 4; BAE99831)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="L -> F (in Ref. 4; BAE99831)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 672 AA; 73539 MW; D6EB0A9A4E9A9CBE CRC64;
MAAKPLLLPL LLLLHLSITL AQNDTNALTL FRLQTDTHGN LAGNWTGSDA CTSSWQGVSC
SPSSHRVTEL SLPSLSLRGP LTSLSSLDQL RLLDLHDNRL NGTVSPLTNC KNLRLVYLAG
NDLSGEIPKE ISFLKRMIRL DLSDNNIRGV IPREILGFTR VLTIRIQNNE LTGRIPDFSQ
MKSLLELNVS FNELHGNVSD GVVKKFGDLS FSGNEGLCGS DPLPVCTITN DPESSNTDQI
VPSNPTSIPH SPVSVREPEI HSHRGIKPGI IAAVIGGCVA VIVLVSFGFA FCCGRLDRNG
ERSKSGSVET GFVGGGEGKR RSSYGEGGES DATSATDRSR LVFFERRKQF ELDDLLKASA
EMLGKGSLGT VYKAVLDDGS TTVAVKRLKD ANPCPRKEFE QYMEIIGRLK HQNVVKLRAY
YYAKEEKLLV YEYLPNGSLH SLLHGNRGPG RIPLDWTTRI SLMLGAARGL AKIHDEYSIS
KIPHGNIKSS NVLLDRNGVA LIADFGLSLL LNPVHAIARL GGYRAPEQSE IKRLSQKADV
YSFGVLLLEV LTGKAPSIFP SPSRPRSAAS VAVEEEEEAV VDLPKWVRSV VKEEWTAEVF
DPELLRYKNI EEEMVAMLHI GLACVVPQPE KRPTMAEVVK MVEEIRVEQS PVGEDFDESR
NSMSPSLATT DG
