PXC3_ARATH
ID PXC3_ARATH Reviewed; 890 AA.
AC O22938; Q0WRK5;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Leucine-rich repeat receptor-like tyrosine-protein kinase PXC3 {ECO:0000305};
DE EC=2.7.10.1;
DE AltName: Full=Protein PXY/TDR-CORRELATED 3 {ECO:0000303|PubMed:23815750};
DE Flags: Precursor;
GN Name=PXC3 {ECO:0000303|PubMed:23815750}; OrderedLocusNames=At2g41820;
GN ORFNames=T11A7.8;
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 TISSUE SPECIFICITY.
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 that may
CC play a role in vascular tissues development.
CC {ECO:0000250|UniProtKB:Q9SJQ1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- WEB RESOURCE: Name=Arabidopsis protein tyrosine kinases;
CC URL="http://www.bio.unipd.it/molbinfo/PTKtable.html";
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DR EMBL; AC002339; AAC02766.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10036.1; -; Genomic_DNA.
DR EMBL; FJ708712; ACN59307.1; -; mRNA.
DR EMBL; AK228301; BAF00244.1; -; mRNA.
DR PIR; E84846; E84846.
DR RefSeq; NP_181713.1; NM_129746.3.
DR AlphaFoldDB; O22938; -.
DR SMR; O22938; -.
DR BioGRID; 4118; 92.
DR IntAct; O22938; 72.
DR STRING; 3702.AT2G41820.1; -.
DR PaxDb; O22938; -.
DR PRIDE; O22938; -.
DR ProteomicsDB; 224808; -.
DR EnsemblPlants; AT2G41820.1; AT2G41820.1; AT2G41820.
DR GeneID; 818781; -.
DR Gramene; AT2G41820.1; AT2G41820.1; AT2G41820.
DR KEGG; ath:AT2G41820; -.
DR Araport; AT2G41820; -.
DR TAIR; locus:2054421; AT2G41820.
DR eggNOG; ENOG502QR50; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; O22938; -.
DR OMA; KWVHTAP; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; O22938; -.
DR PRO; PR:O22938; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22938; baseline and differential.
DR Genevisible; O22938; 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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.80.10.10; -; 3.
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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome; Repeat; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..890
FT /note="Leucine-rich repeat receptor-like tyrosine-protein
FT kinase PXC3"
FT /id="PRO_0000403325"
FT TOPO_DOM 24..534
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 556..890
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 67..85
FT /note="LRR 1"
FT REPEAT 86..108
FT /note="LRR 2"
FT REPEAT 110..132
FT /note="LRR 3"
FT REPEAT 133..157
FT /note="LRR 4"
FT REPEAT 159..181
FT /note="LRR 5"
FT REPEAT 182..205
FT /note="LRR 6"
FT REPEAT 206..229
FT /note="LRR 7"
FT REPEAT 231..254
FT /note="LRR 8"
FT REPEAT 256..276
FT /note="LRR 9"
FT REPEAT 278..300
FT /note="LRR 10"
FT REPEAT 301..325
FT /note="LRR 11"
FT REPEAT 326..349
FT /note="LRR 12"
FT REPEAT 350..373
FT /note="LRR 13"
FT REPEAT 375..397
FT /note="LRR 14"
FT REPEAT 399..421
FT /note="LRR 15"
FT REPEAT 422..446
FT /note="LRR 16"
FT REPEAT 447..469
FT /note="LRR 17"
FT REPEAT 471..492
FT /note="LRR 18"
FT DOMAIN 608..886
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 735
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 614..622
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 636
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
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 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 240
FT /note="N -> S (in Ref. 4; BAF00244)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="E -> G (in Ref. 4; BAF00244)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 890 AA; 97245 MW; D43D2B4C848DA568 CRC64;
MTFWCMSILL IVGFLSKSEL CEAQLSDEAT LVAINRELGV PGWSSNGTDY CTWVGLKCGV
NNSFVEMLDL SGLQLRGNVT LISDLRSLKH LDLSGNNFNG RIPTSFGNLS ELEFLDLSLN
RFVGAIPVEF GKLRGLRAFN ISNNLLVGEI PDELKVLERL EEFQVSGNGL NGSIPHWVGN
LSSLRVFTAY ENDLVGEIPN GLGLVSELEL LNLHSNQLEG KIPKGIFEKG KLKVLVLTQN
RLTGELPEAV GICSGLSSIR IGNNELVGVI PRTIGNISGL TYFEADKNNL SGEIVAEFSK
CSNLTLLNLA ANGFAGTIPT ELGQLINLQE LILSGNSLFG EIPKSFLGSG NLNKLDLSNN
RLNGTIPKEL CSMPRLQYLL LDQNSIRGDI PHEIGNCVKL LQLQLGRNYL TGTIPPEIGR
MRNLQIALNL SFNHLHGSLP PELGKLDKLV SLDVSNNLLT GSIPPLLKGM MSLIEVNFSN
NLLNGPVPVF VPFQKSPNSS FLGNKELCGA PLSSSCGYSE DLDHLRYNHR VSYRIVLAVI
GSGVAVFVSV TVVVLLFMMR EKQEKAAAKN VDVEENVEDE QPAIIAGNVF LENLKQGIDL
DAVVKATMKE SNKLSTGTFS SVYKAVMPSG MIVSVKKLKS MDRAISHHQN KMIRELERLS
KLCHDHLVRP IGFVIYEDVA LLLHQHLPNG NLTQLIHEST KKPEYQPDWP MRLSIAVGAA
EGLAFLHQVA IIHLDVSSSN VLLDSGYKAV LGEIEISKLL DPSRGTASIS SVAGSFGYIP
PEYAYTMQVT APGNVYSYGV VLLEILTSRA PVEEEFGEGV DLVKWVHGAS ARGETPEQIL
DAKLSTVSFA WRREMLAALK VALLCTDITP AKRPKMKKVV EMLQEVKQIK
