PXC2_ARATH
ID PXC2_ARATH Reviewed; 967 AA.
AC Q9LZV7;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Leucine-rich repeat receptor-like protein kinase PXC2 {ECO:0000305};
DE AltName: Full=Protein PXY/TDR-CORRELATED 2 {ECO:0000303|PubMed:23815750};
DE Flags: Precursor;
GN Name=PXC2 {ECO:0000303|PubMed:23815750};
GN OrderedLocusNames=At5g01890 {ECO:0000312|Araport:AT5G01890};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [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 -!- INTERACTION:
CC Q9LZV7; C0LGD6: At1g05700; NbExp=2; IntAct=EBI-1238200, EBI-16963709;
CC Q9LZV7; C0LGD8: At1g07550; NbExp=2; IntAct=EBI-1238200, EBI-16907406;
CC Q9LZV7; Q9FZB8-2: At1g51810; NbExp=2; IntAct=EBI-1238200, EBI-20653376;
CC Q9LZV7; C0LGG3: At1g51820; NbExp=3; IntAct=EBI-1238200, EBI-17066817;
CC Q9LZV7; C0LGI2: At1g67720; NbExp=2; IntAct=EBI-1238200, EBI-17070892;
CC Q9LZV7; Q9M9C5: At1g68400; NbExp=3; IntAct=EBI-1238200, EBI-1238661;
CC Q9LZV7; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-1238200, EBI-20651541;
CC Q9LZV7; C0LGL4: At2g28960; NbExp=2; IntAct=EBI-1238200, EBI-16946048;
CC Q9LZV7; C0LGQ7: At4g20450; NbExp=2; IntAct=EBI-1238200, EBI-17121875;
CC Q9LZV7; C0LGQ5: GSO1; NbExp=2; IntAct=EBI-1238200, EBI-16905069;
CC Q9LZV7; C0LGP3: LRR-RLK; NbExp=2; IntAct=EBI-1238200, EBI-20657203;
CC Q9LZV7; Q9XIC7: SERK2; NbExp=2; IntAct=EBI-1238200, EBI-6299033;
CC Q9LZV7; O64483: SIRK; NbExp=2; IntAct=EBI-1238200, EBI-16905038;
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AL162351; CAB82759.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90406.1; -; Genomic_DNA.
DR EMBL; AF424563; AAL11557.1; -; mRNA.
DR EMBL; BT004520; AAO42766.1; -; mRNA.
DR EMBL; FJ708767; ACN59360.1; -; mRNA.
DR PIR; T48210; T48210.
DR RefSeq; NP_195809.1; NM_120267.3.
DR AlphaFoldDB; Q9LZV7; -.
DR SMR; Q9LZV7; -.
DR IntAct; Q9LZV7; 43.
DR STRING; 3702.AT5G01890.1; -.
DR PaxDb; Q9LZV7; -.
DR PRIDE; Q9LZV7; -.
DR ProteomicsDB; 224807; -.
DR EnsemblPlants; AT5G01890.1; AT5G01890.1; AT5G01890.
DR GeneID; 831677; -.
DR Gramene; AT5G01890.1; AT5G01890.1; AT5G01890.
DR KEGG; ath:AT5G01890; -.
DR Araport; AT5G01890; -.
DR TAIR; locus:2181042; AT5G01890.
DR eggNOG; ENOG502QT06; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9LZV7; -.
DR OMA; QNLYDMR; -.
DR OrthoDB; 151146at2759; -.
DR PhylomeDB; Q9LZV7; -.
DR PRO; PR:Q9LZV7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZV7; baseline and differential.
DR Genevisible; Q9LZV7; 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:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..967
FT /note="Leucine-rich repeat receptor-like protein kinase
FT PXC2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432872"
FT TOPO_DOM 21..609
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 631..967
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 91..114
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 115..139
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 141..164
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 165..189
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 191..212
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 214..236
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 237..260
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 262..284
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 285..307
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 308..332
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 334..356
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 384..408
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 410..432
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 433..456
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 457..480
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 482..503
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 504..528
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 530..552
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT DOMAIN 687..959
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 693..701
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 715
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 103
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 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 967 AA; 104179 MW; A4AD198542EA019F CRC64;
MFNGAVSLLF LFLAVVSARA DPTFNDDVLG LIVFKAGLDD PLSKLSSWNS EDYDPCNWVG
CTCDPATNRV SELRLDAFSL SGHIGRGLLR LQFLHTLVLS NNNLTGTLNP EFPHLGSLQV
VDFSGNNLSG RIPDGFFEQC GSLRSVSLAN NKLTGSIPVS LSYCSTLTHL NLSSNQLSGR
LPRDIWFLKS LKSLDFSHNF LQGDIPDGLG GLYDLRHINL SRNWFSGDVP SDIGRCSSLK
SLDLSENYFS GNLPDSMKSL GSCSSIRLRG NSLIGEIPDW IGDIATLEIL DLSANNFTGT
VPFSLGNLEF LKDLNLSANM LAGELPQTLS NCSNLISIDV SKNSFTGDVL KWMFTGNSES
SSLSRFSLHK RSGNDTIMPI VGFLQGLRVL DLSSNGFTGE LPSNIWILTS LLQLNMSTNS
LFGSIPTGIG GLKVAEILDL SSNLLNGTLP SEIGGAVSLK QLHLHRNRLS GQIPAKISNC
SALNTINLSE NELSGAIPGS IGSLSNLEYI DLSRNNLSGS LPKEIEKLSH LLTFNISHNN
ITGELPAGGF FNTIPLSAVT GNPSLCGSVV NRSCLSVHPK PIVLNPNSSN PTNGPALTGQ
IRKSVLSISA LIAIGAAAVI AIGVVAVTLL NVHARSSVSR HDAAAALALS VGETFSCSPS
KDQEFGKLVM FSGEVDVFDT TGADALLNKD SELGRGGFGV VYKTSLQDGR PVAVKKLTVS
GLIKSQEEFE REMRKLGKLR HKNVVEIKGY YWTQSLQLLI HEFVSGGSLY RHLHGDESVC
LTWRQRFSII LGIARGLAFL HSSNITHYNM KATNVLIDAA GEAKVSDFGL ARLLASALDR
CVLSGKVQSA LGYTAPEFAC RTVKITDRCD VYGFGILVLE VVTGKRPVEY AEDDVVVLCE
TVREGLEEGR VEECVDPRLR GNFPAEEAIP VIKLGLVCGS QVPSNRPEME EVVKILELIQ
CPSHDLE
