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NEK2_ORYSJ
ID   NEK2_ORYSJ              Reviewed;         591 AA.
AC   Q2QMH1; B7EKP8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Serine/threonine-protein kinase Nek2 {ECO:0000305};
DE            EC=2.7.11.1 {ECO:0000305};
DE   AltName: Full=NimA-related protein kinase 2 {ECO:0000303|PubMed:17886359};
DE   AltName: Full=OsNek2 {ECO:0000303|PubMed:17886359};
GN   Name=NEK2 {ECO:0000303|PubMed:17886359};
GN   OrderedLocusNames=Os12g0604700 {ECO:0000312|EMBL:BAT17975.1},
GN   LOC_Os12g41180 {ECO:0000312|EMBL:ABA99823.1};
GN   ORFNames=OsJ_035350 {ECO:0000312|EMBL:EAZ21141.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
RP   FUNCTION, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17886359; DOI=10.1111/j.1365-313x.2007.03161.x;
RA   Vigneault F., Lachance D., Cloutier M., Pelletier G., Levasseur C.,
RA   Seguin A.;
RT   "Members of the plant NIMA-related kinases are involved in organ
RT   development and vascularization in poplar, Arabidopsis and rice.";
RL   Plant J. 51:575-588(2007).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=19224952; DOI=10.1093/pcp/pcp026;
RA   Fujii S., Yamada M., Toriyama K.;
RT   "Cytoplasmic male sterility-related protein kinase, OsNek3, is regulated
RT   downstream of mitochondrial protein phosphatase 2C, DCW11.";
RL   Plant Cell Physiol. 50:828-837(2009).
CC   -!- FUNCTION: May be involved in plant development processes.
CC       {ECO:0000305|PubMed:17886359}.
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   -!- TISSUE SPECIFICITY: Expressed in anthers, pistils and leaves.
CC       {ECO:0000269|PubMed:19224952}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000305}.
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DR   EMBL; DP000011; ABA99823.1; -; Genomic_DNA.
DR   EMBL; AP008218; BAF30238.1; -; Genomic_DNA.
DR   EMBL; AP014968; BAT17975.1; -; Genomic_DNA.
DR   EMBL; CM000149; EAZ21141.1; -; Genomic_DNA.
DR   EMBL; AK072382; BAG92945.1; -; mRNA.
DR   RefSeq; XP_015618225.1; XM_015762739.1.
DR   AlphaFoldDB; Q2QMH1; -.
DR   SMR; Q2QMH1; -.
DR   STRING; 4530.OS12T0604700-01; -.
DR   PaxDb; Q2QMH1; -.
DR   PRIDE; Q2QMH1; -.
DR   EnsemblPlants; Os12t0604700-01; Os12t0604700-01; Os12g0604700.
DR   GeneID; 4352734; -.
DR   Gramene; Os12t0604700-01; Os12t0604700-01; Os12g0604700.
DR   KEGG; osa:4352734; -.
DR   eggNOG; KOG0589; Eukaryota.
DR   HOGENOM; CLU_000288_128_3_1; -.
DR   InParanoid; Q2QMH1; -.
DR   OMA; RNMSPIY; -.
DR   OrthoDB; 317437at2759; -.
DR   Proteomes; UP000000763; Chromosome 12.
DR   Proteomes; UP000007752; Chromosome 12.
DR   Proteomes; UP000059680; Chromosome 12.
DR   ExpressionAtlas; Q2QMH1; baseline and differential.
DR   Genevisible; Q2QMH1; OS.
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; IBA:GO_Central.
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; IPR008271; Ser/Thr_kinase_AS.
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   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..591
FT                   /note="Serine/threonine-protein kinase Nek2"
FT                   /id="PRO_0000314045"
FT   DOMAIN          4..258
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          309..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        129
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   591 AA;  66029 MW;  F5BD392A94896C82 CRC64;
     MDQYEVLEQI GKGAFGSALL VRHKLEKKKY VLKKIRLARQ TDRTRRSAHQ EMQLIATVRN
     PFIVEYKDSW VEKGCYVCIV IGYCEGGDMA EAIKRANGTY FSEEKLCKWL VQLLMALDYL
     HANHILHRDV KCSNIFIARD QSIRLGDFGL AKILTSDDLA SSVVGTPSYM CPELLADIPY
     GTKSDIWSLG CCIYEMTALR PAFKAFDMQA LINKITKSIV SPLPTKYSGA FRGLIKSMLR
     KSPEHRPSAA QLLKHPQLQP YVLQVQLKSS PTRNILPIHQ SLTDKVKKMT FPSDVVDSAR
     RRMARRNSLG NERTVTFSKP SPERNSVSST RSIKEYTTTQ SVKGLSVDSS EAGDEVTSKA
     IITKTSSILR TPKSLPAKTY TARNQLEPPK TSYNRTYRSE LPSKTTPNKI ARPARRASLP
     LSTYETPTKR SISILEQLDS PDVSVNAPRI DRIAEFPLAS SEDPLLPIHN KLSPGHGSCS
     TPPFINRSIT KDKCTIQVLR TDGDNGSDSS GRNATAASSR GSNDSRQQRF DTSSFQQRAE
     ALEGLLEFSA QLLQQERYEE LGILLKPFGP EKASPRETAI WLTKSFKETA S
 
 
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