NIK3_ARATH
ID NIK3_ARATH Reviewed; 632 AA.
AC Q93ZS4; O22717;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein NSP-INTERACTING KINASE 3;
DE EC=2.7.11.1;
DE AltName: Full=LRR receptor-like serine/threonine-protein kinase NIK3;
DE Flags: Precursor;
GN Name=NIK3; OrderedLocusNames=At1g60800; ORFNames=F8A5.31;
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;
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 FUNCTION, INTERACTION WITH CABBAGE LEAF CURL VIRUS NSP, SUBCELLULAR
RP LOCATION, ACTIVITY REGULATION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Involved in defense response to geminivirus infection.
CC {ECO:0000269|PubMed:15489295}.
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 Q93ZS4; Q9M9S4: At1g14390; NbExp=2; IntAct=EBI-17121474, EBI-16954682;
CC Q93ZS4; Q9FZB8-2: At1g51810; NbExp=2; IntAct=EBI-17121474, EBI-20653376;
CC Q93ZS4; Q9SH71: At1g64210; NbExp=2; IntAct=EBI-17121474, EBI-20651385;
CC Q93ZS4; Q9M9C5: At1g68400; NbExp=3; IntAct=EBI-17121474, EBI-1238661;
CC Q93ZS4; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-17121474, EBI-20651541;
CC Q93ZS4; C0LGL4: At2g28960; NbExp=2; IntAct=EBI-17121474, EBI-16946048;
CC Q93ZS4; Q9M8T0: At3g02880; NbExp=2; IntAct=EBI-17121474, EBI-1238677;
CC Q93ZS4; C0LGQ7: At4g20450; NbExp=2; IntAct=EBI-17121474, EBI-17121875;
CC Q93ZS4; Q9FL63: At5g24100; NbExp=3; IntAct=EBI-17121474, EBI-20657062;
CC Q93ZS4; C0LGV0: At5g48740; NbExp=2; IntAct=EBI-17121474, EBI-17091250;
CC Q93ZS4; A0A178UFM8: AXX17_At5g50380; NbExp=3; IntAct=EBI-17121474, EBI-20653342;
CC Q93ZS4; C0LGQ5: GSO1; NbExp=2; IntAct=EBI-17121474, EBI-16905069;
CC Q93ZS4; C0LGP3: LRR-RLK; NbExp=3; IntAct=EBI-17121474, EBI-20657203;
CC Q93ZS4; C0LGU7: MDIS1; NbExp=2; IntAct=EBI-17121474, EBI-16196163;
CC Q93ZS4; Q9LJY0: PRK4; NbExp=2; IntAct=EBI-17121474, EBI-16914444;
CC Q93ZS4; Q3E991: PRK6; NbExp=2; IntAct=EBI-17121474, EBI-20657264;
CC Q93ZS4; Q9LVI6: RLK902; NbExp=2; IntAct=EBI-17121474, EBI-1626936;
CC Q93ZS4; Q9XIC7: SERK2; NbExp=4; IntAct=EBI-17121474, EBI-6299033;
CC Q93ZS4; Q9M2R4: T10K17.40; NbExp=3; IntAct=EBI-17121474, EBI-20657109;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15489295};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:15489295}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves and flowers.
CC {ECO:0000269|PubMed:15489295}.
CC -!- PTM: Autophosphorylated.
CC -!- DISRUPTION PHENOTYPE: Enhanced susceptibility to geminivirus infection.
CC {ECO:0000269|PubMed:15489295}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB71968.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002292; AAB71968.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33734.1; -; Genomic_DNA.
DR EMBL; AY056294; AAL07143.1; -; mRNA.
DR EMBL; AY150495; AAN12912.1; -; mRNA.
DR EMBL; FJ708666; ACN59261.1; -; mRNA.
DR PIR; E96633; E96633.
DR RefSeq; NP_176279.1; NM_104763.3.
DR AlphaFoldDB; Q93ZS4; -.
DR SMR; Q93ZS4; -.
DR BioGRID; 27598; 59.
DR IntAct; Q93ZS4; 78.
DR STRING; 3702.AT1G60800.1; -.
DR PaxDb; Q93ZS4; -.
DR PRIDE; Q93ZS4; -.
DR ProteomicsDB; 249442; -.
DR EnsemblPlants; AT1G60800.1; AT1G60800.1; AT1G60800.
DR GeneID; 842374; -.
DR Gramene; AT1G60800.1; AT1G60800.1; AT1G60800.
DR KEGG; ath:AT1G60800; -.
DR Araport; AT1G60800; -.
DR TAIR; locus:2036636; AT1G60800.
DR eggNOG; ENOG502QVM7; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; Q93ZS4; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q93ZS4; -.
DR PRO; PR:Q93ZS4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93ZS4; baseline and differential.
DR Genevisible; Q93ZS4; 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:0015026; F:coreceptor activity; IGI:TAIR.
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:0048653; P:anther development; IGI:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0007639; P:homeostasis of number of meristem cells; IGI:TAIR.
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 ATP-binding; Cell membrane; Glycoprotein; Host-virus interaction; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Plant defense; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..632
FT /note="Protein NSP-INTERACTING KINASE 3"
FT /id="PRO_0000409727"
FT TOPO_DOM 26..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..632
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 97..121
FT /note="LRR 1"
FT REPEAT 122..145
FT /note="LRR 2"
FT REPEAT 147..168
FT /note="LRR 3"
FT REPEAT 169..193
FT /note="LRR 4"
FT DOMAIN 301..584
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 415..495
FT /note="Interaction with geminivirus NSP protein"
FT /evidence="ECO:0000250"
FT ACT_SITE 428
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 307..315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 461
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 462
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 467
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 475
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 478
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 557
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 632 AA; 70171 MW; 7DC54B2707188B8C CRC64;
MEGVRFVVWR LGFLVFVWFF DISSATLSPT GVNYEVTALV AVKNELNDPY KVLENWDVNS
VDPCSWRMVS CTDGYVSSLD LPSQSLSGTL SPRIGNLTYL QSVVLQNNAI TGPIPETIGR
LEKLQSLDLS NNSFTGEIPA SLGELKNLNY LRLNNNSLIG TCPESLSKIE GLTLVDISYN
NLSGSLPKVS ARTFKVIGNA LICGPKAVSN CSAVPEPLTL PQDGPDESGT RTNGHHVALA
FAASFSAAFF VFFTSGMFLW WRYRRNKQIF FDVNEQYDPE VSLGHLKRYT FKELRSATNH
FNSKNILGRG GYGIVYKGHL NDGTLVAVKR LKDCNIAGGE VQFQTEVETI SLALHRNLLR
LRGFCSSNQE RILVYPYMPN GSVASRLKDN IRGEPALDWS RRKKIAVGTA RGLVYLHEQC
DPKIIHRDVK AANILLDEDF EAVVGDFGLA KLLDHRDSHV TTAVRGTVGH IAPEYLSTGQ
SSEKTDVFGF GILLLELITG QKALDFGRSA HQKGVMLDWV KKLHQEGKLK QLIDKDLNDK
FDRVELEEIV QVALLCTQFN PSHRPKMSEV MKMLEGDGLA ERWEATQNGT GEHQPPPLPP
GMVSSSPRVR YYSDYIQESS LVVEAIELSG PR
