ID F4JA17_ARATH Unreviewed; 636 AA.
AC F4JA17;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=NSP-interacting kinase 2 {ECO:0000313|EMBL:AEE77027.1};
GN Name=NIK2 {ECO:0000313|EMBL:AEE77027.1, ECO:0000313|TAIR:AT3G25560};
GN Synonyms=AtNIK2 {ECO:0000313|EMBL:AEE77027.1}, NSP-interacting kinase
GN 2 {ECO:0000313|EMBL:AEE77027.1};
GN OrderedLocusNames=At3g25560 {ECO:0000313|Araport:AT3G25560,
GN ECO:0000313|EMBL:AEE77027.1};
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 {ECO:0000313|EMBL:AEE77027.1, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:AEE77027.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130713; DOI=10.1038/35048706;
RG European Union Chromosome 3 Arabidopsis Sequencing Consortium;
RG Institute for Genomic Research;
RG Kazusa DNA Research Institute;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Blocker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M.,
RA Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N.,
RA Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L.,
RA Weissenbach J., Saurin W., Quetier F., Schafer M., Muller-Auer S.,
RA Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N.,
RA Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P.,
RA Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S.,
RA Simionati B., Conrad A., Hornischer K., Kauer G., Lohnert T.H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schon O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwalder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.W., Mayer K.F., Kaul S.,
RA Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; CP002686; AEE77027.1; -; Genomic_DNA.
DR RefSeq; NP_974360.1; NM_202631.2.
DR AlphaFoldDB; F4JA17; -.
DR SMR; F4JA17; -.
DR ProteomicsDB; 209702; -.
DR EnsemblPlants; AT3G25560.2; AT3G25560.2; AT3G25560.
DR GeneID; 822143; -.
DR Gramene; AT3G25560.2; AT3G25560.2; AT3G25560.
DR Araport; AT3G25560; -.
DR TAIR; AT3G25560; NIK2.
DR OMA; QNCFRTT; -.
DR PhylomeDB; F4JA17; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4JA17; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
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 PANTHER; PTHR47988:SF94; PROTEIN NSP-INTERACTING KINASE 2; 1.
DR PANTHER; PTHR47988; SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AEE77027.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F4JA17,
KW ECO:0007829|ProteomicsDB:F4JA17};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..636
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003316435"
FT TRANSMEM 248..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 313..568
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 215..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 636 AA; 70796 MW; 66E7ED62260619EF CRC64;
MLQGRREAKK SYALFSSTFF FFFICFLSSS SAELTDKGVN FEVVALIGIK SSLTDPHGVL
MNWDDTAVDP CSWNMITCSD GFVIRLEAPS QNLSGTLSSS IGNLTNLQTV LLQNNYITGN
IPHEIGKLMK LKTLDLSTNN FTGQIPFTLS YSKNLQYFRR VNNNSLTGTI PSSLANMTQL
TFLDLSYNNL SGPVPRSLAK TFNVMGNSQI CPTGTEKDCN GTQPKPMSIT LNSSQNKSSD
GGTKNRKIAV VFGVSLTCVC LLIIGFGFLL WWRRRHNKQV LFFDINEQNK EEMCLGNLRR
FNFKELQSAT SNFSSKNLVG KGGFGNVYKG CLHDGSIIAV KRLKDINNGG GEVQFQTELE
MISLAVHRNL LRLYGFCTTS SERLLVYPYM SNGSVASRLK AKPVLDWGTR KRIALGAGRG
LLYLHEQCDP KIIHRDVKAA NILLDDYFEA VVGDFGLAKL LDHEESHVTT AVRGTVGHIA
PEYLSTGQSS EKTDVFGFGI LLLELITGLR ALEFGKAANQ RGAILDWVKK LQQEKKLEQI
VDKDLKSNYD RIEVEEMVQV ALLCTQYLPI HRPKMSEVVR MLEGDGLVEK WEASSQRAET
NRSYSKPNEF SSSERYSDLT DDSSVLVQAM ELSGPR
//
