NIK2_ARATH
ID NIK2_ARATH Reviewed; 635 AA.
AC Q8RY65; Q9LSU7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein NSP-INTERACTING KINASE 2;
DE EC=2.7.11.1;
DE AltName: Full=LRR receptor-like serine/threonine-protein kinase NIK2;
DE Flags: Precursor;
GN Name=NIK2; OrderedLocusNames=At3g25560; ORFNames=MWL2.18;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 INTERACTION WITH CABBAGE LEAF CURL VIRUS NSP, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=15489295; DOI=10.1101/gad.1245904;
RA Fontes E.P., Santos A.A., Luz D.F., Waclawovsky A.J., Chory J.;
RT "The geminivirus nuclear shuttle protein is a virulence factor that
RT suppresses transmembrane receptor kinase activity.";
RL Genes Dev. 18:2545-2556(2004).
RN [6]
RP FUNCTION.
RX PubMed=18789471; DOI=10.1016/j.virol.2008.08.005;
RA Rocha C.S., Santos A.A., Machado J.P., Fontes E.P.;
RT "The ribosomal protein L10/QM-like protein is a component of the NIK-
RT mediated antiviral signaling.";
RL Virology 380:165-169(2008).
CC -!- FUNCTION: Involved in defense response to geminivirus infection (By
CC similarity). Phosphorylates RPL10A in vitro. {ECO:0000250,
CC ECO:0000269|PubMed:18789471}.
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 -!- 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;
CC -!- ACTIVITY REGULATION: Inhibited by the viral nuclear shuttle protein
CC (NSP) that binds to the region required for oligomerization.
CC {ECO:0000269|PubMed:15489295}.
CC -!- SUBUNIT: Oligomer. Interacts with geminivirus nuclear shuttle protein
CC (NSP). {ECO:0000269|PubMed:15489295}.
CC -!- INTERACTION:
CC Q8RY65; Q94F62: BAK1; NbExp=2; IntAct=EBI-20664696, EBI-617138;
CC Q8RY65; Q6XAT2: ERL2; NbExp=4; IntAct=EBI-20664696, EBI-16895926;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15489295};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:15489295}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8RY65-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in flowers and roots.
CC {ECO:0000269|PubMed:15489295}.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01326.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB025639; BAB01326.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77026.1; -; Genomic_DNA.
DR EMBL; AY075617; AAL91629.1; -; mRNA.
DR EMBL; BT002619; AAO11535.1; -; mRNA.
DR EMBL; FJ708728; ACN59323.1; -; mRNA.
DR RefSeq; NP_189183.2; NM_113453.3. [Q8RY65-1]
DR AlphaFoldDB; Q8RY65; -.
DR SMR; Q8RY65; -.
DR BioGRID; 7474; 17.
DR IntAct; Q8RY65; 18.
DR STRING; 3702.AT3G25560.3; -.
DR iPTMnet; Q8RY65; -.
DR PaxDb; Q8RY65; -.
DR PRIDE; Q8RY65; -.
DR ProteomicsDB; 251138; -. [Q8RY65-1]
DR EnsemblPlants; AT3G25560.1; AT3G25560.1; AT3G25560. [Q8RY65-1]
DR GeneID; 822143; -.
DR Gramene; AT3G25560.1; AT3G25560.1; AT3G25560. [Q8RY65-1]
DR KEGG; ath:AT3G25560; -.
DR Araport; AT3G25560; -.
DR eggNOG; ENOG502QVM7; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; Q8RY65; -.
DR PhylomeDB; Q8RY65; -.
DR PRO; PR:Q8RY65; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RY65; baseline and differential.
DR Genevisible; Q8RY65; 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: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; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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; Glycoprotein;
KW Host-virus interaction; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Plant defense; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..635
FT /note="Protein NSP-INTERACTING KINASE 2"
FT /id="PRO_0000409726"
FT TOPO_DOM 33..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 104..128
FT /note="LRR 1"
FT REPEAT 129..153
FT /note="LRR 2"
FT REPEAT 155..176
FT /note="LRR 3"
FT REPEAT 177..200
FT /note="LRR 4"
FT DOMAIN 312..591
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 214..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..502
FT /note="Interaction with geminivirus NSP protein"
FT /evidence="ECO:0000250"
FT REGION 593..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 435
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 318..326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 309
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 468
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 469
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 474
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 482
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 485
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 564
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
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 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 635 AA; 70606 MW; 848032CABD9DFA45 CRC64;
MLQGRREAKK SYALFSSTFF FFFICFLSSS SAELTDKGVN FEVVALIGIK SSLTDPHGVL
MNWDDTAVDP CSWNMITCSD GFVIRLEAPS QNLSGTLSSS IGNLTNLQTV LLQNNYITGN
IPHEIGKLMK LKTLDLSTNN FTGQIPFTLS YSKNLQYLRV NNNSLTGTIP SSLANMTQLT
FLDLSYNNLS GPVPRSLAKT FNVMGNSQIC PTGTEKDCNG TQPKPMSITL NSSQNKSSDG
GTKNRKIAVV FGVSLTCVCL LIIGFGFLLW WRRRHNKQVL FFDINEQNKE EMCLGNLRRF
NFKELQSATS NFSSKNLVGK GGFGNVYKGC LHDGSIIAVK RLKDINNGGG EVQFQTELEM
ISLAVHRNLL RLYGFCTTSS ERLLVYPYMS NGSVASRLKA KPVLDWGTRK RIALGAGRGL
LYLHEQCDPK IIHRDVKAAN ILLDDYFEAV VGDFGLAKLL DHEESHVTTA VRGTVGHIAP
EYLSTGQSSE KTDVFGFGIL LLELITGLRA LEFGKAANQR GAILDWVKKL QQEKKLEQIV
DKDLKSNYDR IEVEEMVQVA LLCTQYLPIH RPKMSEVVRM LEGDGLVEKW EASSQRAETN
RSYSKPNEFS SSERYSDLTD DSSVLVQAME LSGPR
