PBL4_ARATH
ID PBL4_ARATH Reviewed; 412 AA.
AC Q5PP29; Q9LFY9;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable serine/threonine-protein kinase PBL4 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=PBS1-like protein 4 {ECO:0000303|PubMed:20413097};
GN Name=PBL4 {ECO:0000303|PubMed:20413097};
GN OrderedLocusNames=At1g26970 {ECO:0000312|Araport:AT1G26970};
GN ORFNames=T7N9.2 {ECO:0000312|EMBL:AAF79849.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20413097; DOI=10.1016/j.chom.2010.03.007;
RA Zhang J., Li W., Xiang T., Liu Z., Laluk K., Ding X., Zou Y., Gao M.,
RA Zhang X., Chen S., Mengiste T., Zhang Y., Zhou J.M.;
RT "Receptor-like cytoplasmic kinases integrate signaling from multiple plant
RT immune receptors and are targeted by a Pseudomonas syringae effector.";
RL Cell Host Microbe 7:290-301(2010).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O48814};
CC Lipid-anchor {ECO:0000250|UniProtKB:O48814}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79849.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC000348; AAF79849.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30765.1; -; Genomic_DNA.
DR EMBL; BT020268; AAV84489.1; -; mRNA.
DR EMBL; BT020441; AAW30020.1; -; mRNA.
DR PIR; G86396; G86396.
DR RefSeq; NP_174019.2; NM_102461.3.
DR AlphaFoldDB; Q5PP29; -.
DR SMR; Q5PP29; -.
DR STRING; 3702.AT1G26970.1; -.
DR PaxDb; Q5PP29; -.
DR PRIDE; Q5PP29; -.
DR ProteomicsDB; 236794; -.
DR EnsemblPlants; AT1G26970.1; AT1G26970.1; AT1G26970.
DR GeneID; 839588; -.
DR Gramene; AT1G26970.1; AT1G26970.1; AT1G26970.
DR KEGG; ath:AT1G26970; -.
DR Araport; AT1G26970; -.
DR TAIR; locus:2205714; AT1G26970.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_1_1; -.
DR InParanoid; Q5PP29; -.
DR OMA; TSKTVMK; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q5PP29; -.
DR PRO; PR:Q5PP29; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q5PP29; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Kinase; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Palmitate; Phosphoprotein; Plant defense;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..412
FT /note="Probable serine/threonine-protein kinase PBL4"
FT /id="PRO_0000438605"
FT DOMAIN 83..369
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 14..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 89..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 167
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 250
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 255
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 263
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9FE20"
SQ SEQUENCE 412 AA; 45527 MW; C31D38EAD74890E8 CRC64;
MGNCFGFSAK VGNRESPYRG SSRISAKRSQ SSRLSSLTIQ SSSYNDDTSV ASLQTPRSEG
ELLASPTLKA FTFNELKTAT RNFRPDSVIG EGGFGYVYKG WIDERTLSPS KPGSGMVVAV
KKLKEEGFQG HRQWLAEVDC LGRLHHMNLV KLIGYCSKGD HIRLLVYEYM PKGSLENHLF
RRGAEPIPWR TRIKVAIGAA RGLAFLHEAQ VIYRDFKASN ILLDSEFNAK LSDFGLAKVG
PTGDRTHVST QVMGTQGYAA PEYVATGRIT AKSDVYSFGV VLLELLSGRL TVDKTKVGVE
RNLVDWAIPY LGDKRKVFRI MDTKLGGQYP HKGACLTANT ALQCLNQEPK LRPKMSDVLS
TLEELEMTLK SGSISNSVMK LTSSSSSFTA KQRVRTPVAD PVLSSRRCRR VR
