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NEK3_ARATH
ID   NEK3_ARATH              Reviewed;         568 AA.
AC   Q8RX66;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Serine/threonine-protein kinase Nek3;
DE            EC=2.7.11.1;
DE   AltName: Full=NimA-related protein kinase 3;
DE            Short=AtNek3;
GN   Name=NEK3; OrderedLocusNames=At5g28290; ORFNames=T8M17.60;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   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).
CC   -!- FUNCTION: May be involved in plant development processes.
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000305}.
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DR   EMBL; AF296835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED93785.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM68653.1; -; Genomic_DNA.
DR   EMBL; AY090360; AAL91264.1; -; mRNA.
DR   EMBL; BT015415; AAU05538.1; -; mRNA.
DR   RefSeq; NP_001330383.1; NM_001344066.1.
DR   RefSeq; NP_198181.1; NM_122712.3.
DR   AlphaFoldDB; Q8RX66; -.
DR   SMR; Q8RX66; -.
DR   BioGRID; 18185; 3.
DR   IntAct; Q8RX66; 3.
DR   STRING; 3702.AT5G28290.1; -.
DR   iPTMnet; Q8RX66; -.
DR   PaxDb; Q8RX66; -.
DR   PRIDE; Q8RX66; -.
DR   ProteomicsDB; 238355; -.
DR   EnsemblPlants; AT5G28290.1; AT5G28290.1; AT5G28290.
DR   EnsemblPlants; AT5G28290.2; AT5G28290.2; AT5G28290.
DR   GeneID; 832912; -.
DR   Gramene; AT5G28290.1; AT5G28290.1; AT5G28290.
DR   Gramene; AT5G28290.2; AT5G28290.2; AT5G28290.
DR   KEGG; ath:AT5G28290; -.
DR   Araport; AT5G28290; -.
DR   TAIR; locus:2185314; AT5G28290.
DR   eggNOG; KOG0589; Eukaryota.
DR   HOGENOM; CLU_000288_128_3_1; -.
DR   InParanoid; Q8RX66; -.
DR   OMA; ATPKRWM; -.
DR   OrthoDB; 317437at2759; -.
DR   PhylomeDB; Q8RX66; -.
DR   PRO; PR:Q8RX66; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8RX66; baseline and differential.
DR   Genevisible; Q8RX66; AT.
DR   GO; GO:0055028; C:cortical microtubule; 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; IBA:GO_Central.
DR   GO; GO:0007017; P:microtubule-based process; 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..568
FT                   /note="Serine/threonine-protein kinase Nek3"
FT                   /id="PRO_0000314039"
FT   DOMAIN          4..258
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          277..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..501
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   568 AA;  63754 MW;  D2CB32FE9F25A72C CRC64;
     MEHYEVLEQI GKGSFGSALL VRHKHEKKLY VLKKIRLARQ TGRTRRSAHQ EMELISKIRN
     PFIVEYKDSW VEKGCYVCIV IGYCKGGDMA EAIKKANGVE FSEEKLCKWL VQLLMALEYL
     HASHILHRDV KCSNIFLTKD QDIRLGDFGL AKILTSDDLA SSVVGTPSYM CPELLADIPY
     GSKSDIWSLG CCMYEMTALK PAFKAFDMQG LINRINRSIV APLPAQYSTA FRSLVKSMLR
     KNPELRPSAS DLLRQPLLQP YVQKVLLKLS FREHDTLPSE SERRSSYPQQ RKRTSGKSVS
     FGPSRFGVDQ EDSVSSVKPV HTYLHRHRPV DLSANDTSRV VVRRPAVSSV VSNSSKYVPV
     RSNQPKSGGL LKPAVVTRRA SLPISQKPAK GTKDSLYHPN IGILHQLNSP DVSVNSPRID
     RIKFPLASYE EMPFIPVVRK KKGSSRGSYS PPPEPPLDCS ITKDKFTLEP ERETKSDLSD
     QNATAGASSR ASSGASRRQR FDPSSYRQRA EALEGLLEFS ARLLIDERYD ELNVLLKPFG
     PGKVSPRETA IWLSKSFKES SPSNLEED
 
 
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