PIX13_ARATH
ID PIX13_ARATH Reviewed; 414 AA.
AC Q9SII6; F4IMG9; Q6QJ33; Q6QJ34; Q8LEZ7; Q93W33;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Probable serine/threonine-protein kinase PIX13 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
GN Name=PIX13 {ECO:0000303|PubMed:23951354};
GN Synonyms=KIN3 {ECO:0000303|PubMed:21219905};
GN OrderedLocusNames=At2g17220 {ECO:0000312|Araport:AT2G17220};
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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-201 AND 178-407 (ISOFORM 1).
RA Kurth J., Leister D.;
RT "Protein kinases in chloroplasts.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2.
RX PubMed=21219905; DOI=10.1016/j.febslet.2011.01.001;
RA Stael S., Bayer R.G., Mehlmer N., Teige M.;
RT "Protein N-acylation overrides differing targeting signals.";
RL FEBS Lett. 585:517-522(2011).
RN [8]
RP INTERACTION WITH XANTHOMONAS CAMPESTRIS XOPAC/AVRAC.
RX PubMed=23951354; DOI=10.1371/journal.pone.0073469;
RA Guy E., Lautier M., Chabannes M., Roux B., Lauber E., Arlat M., Noel L.D.;
RT "xopAC-triggered immunity against Xanthomonas depends on Arabidopsis
RT receptor-like cytoplasmic kinase genes PBL2 and RIPK.";
RL PLoS ONE 8:E73469-E73469(2013).
CC -!- FUNCTION: May be involved in plant defense signaling.
CC {ECO:0000250|UniProtKB:O48814}.
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 Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with the Xanthomonas campestris effector
CC XopAC/AvrAC. {ECO:0000269|PubMed:23951354}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21219905};
CC Lipid-anchor {ECO:0000305|PubMed:21219905}. Nucleus
CC {ECO:0000269|PubMed:21219905}. Note=Predominantly localized at the
CC plasma membrane. {ECO:0000269|PubMed:21219905}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SII6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SII6-2; Sequence=VSP_058689;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. experimental confirmation available. {ECO:0000305}.
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; AC007127; AAD25140.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC06599.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06600.1; -; Genomic_DNA.
DR EMBL; AF370585; AAK43904.1; -; mRNA.
DR EMBL; AY049263; AAK83605.1; -; mRNA.
DR EMBL; AY149966; AAN31120.1; -; mRNA.
DR EMBL; BX819921; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY085132; AAM61685.1; -; mRNA.
DR EMBL; AY536849; AAS65787.1; -; mRNA.
DR EMBL; AY536850; AAS65788.1; -; mRNA.
DR PIR; E84549; E84549.
DR RefSeq; NP_565408.1; NM_127276.3. [Q9SII6-1]
DR RefSeq; NP_973478.1; NM_201749.1. [Q9SII6-2]
DR AlphaFoldDB; Q9SII6; -.
DR SMR; Q9SII6; -.
DR STRING; 3702.AT2G17220.1; -.
DR iPTMnet; Q9SII6; -.
DR PaxDb; Q9SII6; -.
DR PRIDE; Q9SII6; -.
DR ProteomicsDB; 236762; -. [Q9SII6-1]
DR EnsemblPlants; AT2G17220.1; AT2G17220.1; AT2G17220. [Q9SII6-1]
DR EnsemblPlants; AT2G17220.2; AT2G17220.2; AT2G17220. [Q9SII6-2]
DR GeneID; 816227; -.
DR Gramene; AT2G17220.1; AT2G17220.1; AT2G17220. [Q9SII6-1]
DR Gramene; AT2G17220.2; AT2G17220.2; AT2G17220. [Q9SII6-2]
DR KEGG; ath:AT2G17220; -.
DR Araport; AT2G17220; -.
DR TAIR; locus:2059642; AT2G17220.
DR eggNOG; KOG1187; Eukaryota.
DR InParanoid; Q9SII6; -.
DR OMA; KPLHHRS; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9SII6; -.
DR PRO; PR:Q9SII6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SII6; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Kinase; Lipoprotein;
KW Membrane; Myristate; Nucleotide-binding; Nucleus; Palmitate; Plant defense;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:21219905"
FT CHAIN 2..414
FT /note="Probable serine/threonine-protein kinase PIX13"
FT /id="PRO_0000438604"
FT DOMAIN 87..370
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 220
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 93..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:21219905"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT VAR_SEQ 26
FT /note="Missing (in isoform 2)"
FT /id="VSP_058689"
FT MUTAGEN 2
FT /note="G->A: Drastic reduction of plasma membrane
FT localization and strong increase of nuclear localization."
FT /evidence="ECO:0000269|PubMed:21219905"
FT CONFLICT 49
FT /note="N -> K (in Ref. 5; AAM61685)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="R -> K (in Ref. 5; AAM61685)"
FT /evidence="ECO:0000305"
FT CONFLICT 408..409
FT /note="QN -> HT (in Ref. 5; AAM61685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 45552 MW; 5C916C0E3304B1A4 CRC64;
MGLCWGSPSD SPPTTTPSST GNISSVGTFK SSNNTTTTGT SRGSNISSNS GFSVASGEDA
YPDGQILPIP NLRIFSLAEL RASTRNFRSE NVLGEGGFGK VFKGWLEDKT PGKQSNGTVI
AVKKLNAESF QGFEEWQCEV NFLGRVSHPN LVKLLGYCLE GEELLLVYEY MQKGSLENHL
FRKGSAVQPL SWEIRLKIAI GAAKGLAFLH ASEKQVIYRD FKASNILLDG SYNAKISDFG
LAKLGPSASQ SHITTRVMGT HGYAAPEYVA TGHLYVKSDV YGFGVVLAEI LTGLHALDPT
RPTGQHNLTE WIKPHLSERR KLRSIMDPRL EGKYPFKSAF RVAQLALKCL GPEPKNRPSM
KEVVESLELI EAANEKPLER RTTRASPSIR QQQGHYRPQQ LSSFRPRQNV SRAH
