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NEK4_ARATH
ID   NEK4_ARATH              Reviewed;         555 AA.
AC   Q8RXT4; Q9M1W2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Serine/threonine-protein kinase Nek4;
DE            EC=2.7.11.1;
DE   AltName: Full=NimA-related protein kinase 4;
DE            Short=AtNek4;
GN   Name=NEK4; OrderedLocusNames=At3g63280; ORFNames=F16M2.130;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder 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.X.,
RA   Kaul S., 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]
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   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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB86429.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL138648; CAB86429.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE80460.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE80461.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM64569.1; -; Genomic_DNA.
DR   EMBL; AY080682; AAL86305.1; -; mRNA.
DR   EMBL; AY117234; AAM51309.1; -; mRNA.
DR   PIR; T48117; T48117.
DR   RefSeq; NP_001118899.1; NM_001125427.1.
DR   RefSeq; NP_001326587.1; NM_001340197.1.
DR   RefSeq; NP_191887.2; NM_116193.5.
DR   AlphaFoldDB; Q8RXT4; -.
DR   SMR; Q8RXT4; -.
DR   BioGRID; 10817; 4.
DR   STRING; 3702.AT3G63280.1; -.
DR   PaxDb; Q8RXT4; -.
DR   PRIDE; Q8RXT4; -.
DR   ProteomicsDB; 238697; -.
DR   EnsemblPlants; AT3G63280.1; AT3G63280.1; AT3G63280.
DR   EnsemblPlants; AT3G63280.2; AT3G63280.2; AT3G63280.
DR   EnsemblPlants; AT3G63280.3; AT3G63280.3; AT3G63280.
DR   GeneID; 825503; -.
DR   Gramene; AT3G63280.1; AT3G63280.1; AT3G63280.
DR   Gramene; AT3G63280.2; AT3G63280.2; AT3G63280.
DR   Gramene; AT3G63280.3; AT3G63280.3; AT3G63280.
DR   KEGG; ath:AT3G63280; -.
DR   Araport; AT3G63280; -.
DR   TAIR; locus:2077274; AT3G63280.
DR   eggNOG; KOG0589; Eukaryota.
DR   HOGENOM; CLU_000288_128_3_1; -.
DR   InParanoid; Q8RXT4; -.
DR   PhylomeDB; Q8RXT4; -.
DR   PRO; PR:Q8RXT4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8RXT4; baseline and differential.
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..555
FT                   /note="Serine/threonine-protein kinase Nek4"
FT                   /id="PRO_0000314040"
FT   DOMAIN          4..258
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          288..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..477
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   555 AA;  62898 MW;  958EFAA4FD3E0065 CRC64;
     MERYEVLEQI GKGSFGSALL VRHKQERKKY VLKKIRLARQ SDRARRSAHQ EMELISTVRN
     PFVVEYKDSW VEKGCYVCIV IGYCQGGDMT DTIKRACGVH FPEEKLCQWL VQLLMALDYL
     HSNHILHRDV KCSNIFLTKE QDIRLGDFGL AKILTSDDLT SSVVGTPSYM CPELLADIPY
     GSKSDIWSLG CCMYEMAAHK PPFKASDVQT LITKIHKLIM DPIPAMYSGS FRGLIKSMLR
     KNPELRPSAN ELLNHPHLQP YISMVYMKLE SPRRSTFPLQ FSERDATLKE RRRSSFSNDR
     RLNPSVSDTE AGSVSSSGKA SPTPMFNGRK VSEVTVGVVR EEIVPQRQEE AKKQSGAART
     PRVAGTSAKA STQRTVFKHE LMKVSNPTER RRRVSLPLVV ENPYTYESDI TALCSLNSPD
     VSVNTPRFDK IAEFPEDIFQ NQNRETASRR EVARHSFSSP PCPPHGEDNS NGSITKDKCT
     VQKRSVSEVK QRRFDTSSYQ QRAEALEGLL EFSAKLLQQE RYDELGVLLK PFGAERVSSR
     ETAIWLTKSF KEASV
 
 
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