NEK4_ORYSJ
ID NEK4_ORYSJ Reviewed; 943 AA.
AC Q60DG4; B9FPU0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Serine/threonine-protein kinase Nek4 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=NimA-related protein kinase 4 {ECO:0000303|PubMed:17886359};
DE AltName: Full=OsNek4 {ECO:0000303|PubMed:17886359};
GN Name=NEK4 {ECO:0000303|PubMed:17886359};
GN OrderedLocusNames=Os05g0440800 {ECO:0000312|EMBL:BAS94240.1},
GN LOC_Os05g36960 {ECO:0000305};
GN ORFNames=B1110B01.5 {ECO:0000312|EMBL:AAU90090.1},
GN OsJ_18694 {ECO:0000312|EMBL:EEE63870.1};
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(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; AC147462; AAU90090.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17583.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS94240.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE63870.1; -; Genomic_DNA.
DR EMBL; AK073901; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015637651.1; XM_015782165.1.
DR RefSeq; XP_015637652.1; XM_015782166.1.
DR AlphaFoldDB; Q60DG4; -.
DR SMR; Q60DG4; -.
DR STRING; 4530.OS05T0440800-01; -.
DR PaxDb; Q60DG4; -.
DR PRIDE; Q60DG4; -.
DR EnsemblPlants; Os05t0440800-01; Os05t0440800-01; Os05g0440800.
DR GeneID; 4338922; -.
DR Gramene; Os05t0440800-01; Os05t0440800-01; Os05g0440800.
DR KEGG; osa:4338922; -.
DR eggNOG; KOG0589; Eukaryota.
DR HOGENOM; CLU_000288_128_0_1; -.
DR InParanoid; Q60DG4; -.
DR OMA; VSDEWPT; -.
DR OrthoDB; 219308at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q60DG4; OS.
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:0043622; P:cortical microtubule organization; IEA:EnsemblPlants.
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..943
FT /note="Serine/threonine-protein kinase Nek4"
FT /id="PRO_0000314048"
FT DOMAIN 8..262
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 272..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 14..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 90
FT /note="G -> D (in Ref. 6; AK073901)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="K -> N (in Ref. 6; AK073901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 943 AA; 103492 MW; 75D82FF2776FD15D CRC64;
MESRMDQYEI MEQVGRGAFG AAILVNHKIE RKKYVLKKIR LARQTERCRK SAHQEMALIA
RLQHPYIVEF KEAWVEKGCY VCIVTGYCEG GDMDELMKKL NGTYFPEEKL LKWFAQLVLA
VDYLHSNYVL HRDLKCSNIF LTKDQDIRLG DFGLAKTLKE DDLTSSVVGT PNYMCPELLT
DIPYGFKSDI WSLGCCMYEM AAHRPAFKAF DMAGLISKIN RSSIGPLPAC YSSSMKTLIK
SMLRKSPEHR PTASEILKNP YLQPYVNQCR PLSDAPTPIR MPEKPLSTSR SNQRCTSESQ
SSSISCSDID STQSSDRSTS GGAPSTDSKL NDIRSIQDAD RADSDEKCVT PEDLRGNKNI
SGAELKRQDS SKSVHQHHRG ESKQPKIIEK IMTTLREESR LRENNSPVSS SGVKLTSAVS
NKNQAEQSSE SSRPHSGVSY SSKFGDISSN GWTNTSDECV DPVQVPLQLK QLSPTVEHCP
KLKNSGSSTP EPAKQIAENG SSASGMSKTK SSPSSSRRPS PQRQTVAGIP IVPFTVSKRA
HIKAESEKTP PRPAHSPNNS LHNLPPLIPI STNLSEENIK LGNSQAMPAP LEFVTAASKE
DISFYSNSVV DCVEKAEPSE VFESNSPAYL TPPWTGPVLD AKGENGLIAI PCSEIHTGTL
QKSMASNDDS SLSSPLDTFY LSFEQEFVCK DDSQSSKHGH SAVTLLSGED KFTVQELLAS
TPVISPFVSS TSNTLPEDKS SYQSFKKQSD SHSGPPVDVP AQTIRLNSFL VSDEWPTSET
VQGEARDTAA SKLLNVVRED FDVRSSSCST STQPSGQTPV RSKLNVPETN LASNISIPSI
SEAVRLSTAM DVKPYTSEAS NGVKEEASPA KEALDVTSFR QRAEALEGLL ELSADLLENN
RLEELAIVLQ PFGKNKVSPR ETAIWLARSF KGMMNEEGGR LSM