(data stored in ACNUC13479 zone)

SWISSPROT: 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   07-JUN-2017, entry version 143.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT   receptor-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.,
RA   Jones B., Sandberg G., Zheng B.;
RT   "The Arabidopsis LRR-RLK, PXC1, is a regulator of secondary wall
RT   formation 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
CC       may play a role in vascular tissues development.
CC       {ECO:0000250|UniProtKB:Q9SJQ1}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
CC       type I membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in the vascular strands of
CC       cotyledons, the shoot apex, hypocotyls, roots, leaves, stems and
CC       flowers. {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
CC       protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC       URL="http://plantsp.genomics.purdue.edu/family/class.html";
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   UniGene; At.4740; -.
DR   ProteinModelPortal; Q9LZV7; -.
DR   SMR; Q9LZV7; -.
DR   IntAct; Q9LZV7; 6.
DR   STRING; 3702.AT5G01890.1; -.
DR   PaxDb; Q9LZV7; -.
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; ENOG410IG0X; Eukaryota.
DR   eggNOG; COG4886; LUCA.
DR   HOGENOM; HOG000116551; -.
DR   OMA; WNSEDYD; -.
DR   OrthoDB; EOG093601HM; -.
DR   PhylomeDB; Q9LZV7; -.
DR   PRO; PR:Q9LZV7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Genevisible; Q9LZV7; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   Gene3D; 3.80.10.10; -; 3.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR032675; L_dom-like.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
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; PF13855; LRR_8; 2.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SUPFAM; SSF52058; SSF52058; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q9LZV7.
DR   SWISS-2DPAGE; Q9LZV7.
KW   ATP-binding; Cell membrane; Complete proteome; Glycoprotein;
KW   Leucine-rich repeat; Membrane; Nucleotide-binding; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    967       Leucine-rich repeat receptor-like protein
FT                                kinase PXC2. {ECO:0000255}.
FT                                /FTId=PRO_0000432872.
FT   TOPO_DOM     21    609       Extracellular. {ECO:0000305}.
FT   TRANSMEM    610    630       Helical. {ECO:0000255}.
FT   TOPO_DOM    631    967       Cytoplasmic. {ECO:0000305}.
FT   REPEAT       91    114       LRR 1. {ECO:0000255}.
FT   REPEAT      115    139       LRR 2. {ECO:0000255}.
FT   REPEAT      141    164       LRR 3. {ECO:0000255}.
FT   REPEAT      165    189       LRR 4. {ECO:0000255}.
FT   REPEAT      191    212       LRR 5. {ECO:0000255}.
FT   REPEAT      214    236       LRR 6. {ECO:0000255}.
FT   REPEAT      237    260       LRR 7. {ECO:0000255}.
FT   REPEAT      262    284       LRR 8. {ECO:0000255}.
FT   REPEAT      285    307       LRR 9. {ECO:0000255}.
FT   REPEAT      308    332       LRR 10. {ECO:0000255}.
FT   REPEAT      334    356       LRR 11. {ECO:0000255}.
FT   REPEAT      384    408       LRR 12. {ECO:0000255}.
FT   REPEAT      410    432       LRR 13. {ECO:0000255}.
FT   REPEAT      433    456       LRR 14. {ECO:0000255}.
FT   REPEAT      457    480       LRR 15. {ECO:0000255}.
FT   REPEAT      482    503       LRR 16. {ECO:0000255}.
FT   REPEAT      504    528       LRR 17. {ECO:0000255}.
FT   REPEAT      530    552       LRR 18. {ECO:0000255}.
FT   DOMAIN      687    959       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     693    701       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   COMPBIAS    643    648       Poly-Ala. {ECO:0000255}.
FT   BINDING     715    715       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   CARBOHYD    103    103       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    127    127       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    171    171       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    219    219       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    296    296       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    315    315       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    331    331       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    374    374       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    415    415       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    446    446       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    479    479       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    487    487       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    516    516       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    535    535       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    540    540       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    571    571       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    587    587       N-linked (GlcNAc...) asparagine.
FT                                {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
//

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