NEK3_ORYSJ
ID NEK3_ORYSJ Reviewed; 585 AA.
AC Q6ZEZ5; B7ECN6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Serine/threonine-protein kinase Nek3 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=NimA-related protein kinase 3 {ECO:0000303|PubMed:17886359};
DE AltName: Full=OsNek3 {ECO:0000303|PubMed:17886359};
GN Name=NEK3 {ECO:0000303|PubMed:17886359};
GN OrderedLocusNames=Os07g0176600 {ECO:0000312|EMBL:BAT00290.1},
GN LOC_Os07g08000 {ECO:0000305};
GN ORFNames=OsJ_23299 {ECO:0000312|EMBL:EEE66668.1},
GN P0534H07.24 {ECO:0000312|EMBL:BAC83436.1};
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=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 [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, INTERACTION WITH PLIM2B, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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 (Probable).
CC May function downstream of DCW11 in retrograde signaling from the
CC mitochondria to the nucleus. Seems to be involved in the mechanism of
CC cytoplasmic male sterility (CMS) occurrence (PubMed:19224952).
CC {ECO:0000269|PubMed:19224952, 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 -!- SUBUNIT: Interacts with PLIM2B. {ECO:0000269|PubMed:19224952}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen grains.
CC {ECO:0000269|PubMed:19224952}.
CC -!- DEVELOPMENTAL STAGE: Expressed in anthers from the bi-cellular to the
CC tri-cellular pollen stage. {ECO:0000269|PubMed:19224952}.
CC -!- MISCELLANEOUS: Expression in anthers at the tri-cellular pollen stage
CC is down-regulated in cytoplasmic male sterility (CMS) rice lines.
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; AP004307; BAC83436.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF20936.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT00290.1; -; Genomic_DNA.
DR EMBL; CM000144; EEE66668.1; -; Genomic_DNA.
DR EMBL; AK066812; BAG90133.1; -; mRNA.
DR EMBL; AK067073; BAG90253.1; -; mRNA.
DR RefSeq; XP_015645555.1; XM_015790069.1.
DR AlphaFoldDB; Q6ZEZ5; -.
DR SMR; Q6ZEZ5; -.
DR BioGRID; 811579; 1.
DR STRING; 4530.OS07T0176600-01; -.
DR PaxDb; Q6ZEZ5; -.
DR PRIDE; Q6ZEZ5; -.
DR EnsemblPlants; Os07t0176600-01; Os07t0176600-01; Os07g0176600.
DR GeneID; 4342542; -.
DR Gramene; Os07t0176600-01; Os07t0176600-01; Os07g0176600.
DR KEGG; osa:4342542; -.
DR eggNOG; KOG0589; Eukaryota.
DR HOGENOM; CLU_000288_128_3_1; -.
DR InParanoid; Q6ZEZ5; -.
DR OMA; AHKEQPP; -.
DR OrthoDB; 317437at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q6ZEZ5; 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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..585
FT /note="Serine/threonine-protein kinase Nek3"
FT /id="PRO_0000314047"
FT DOMAIN 4..258
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 354..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..413
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 585 AA; 65803 MW; FB191642EABE72EF CRC64;
MEQYEVLEQI GKGSFGSALL VRHKVEKKRY VLKKIRLARQ TDRCRRSAHQ EMELIAKVRN
PYIVEYKDSW VEKGCYVCIV IGYCEGGDMS EAIKKANSNY FSEERLCMWL VQLLMALDYL
HVNHILHRDV KCSNIFLTKD QNIRLGDFGL AKVLTSDDLT SSVVGTPSYM CPELLADIPY
GSKSDIWSLG CCLYEMTALK PAFKAFDMQT LINKISKSVL APLPTIYSGA FRGLIKSMLR
KSPDHRPSAA ELLKHPHLQP FVLELQLKSS PARNLFPDTN KASCSDDENN WKAKYSKSHS
FKVDRIVKVD KVAANNGHPS STGTAKDYQE LLKQPMDELL GQLTEKVVDE VIHGNHSRVT
KSPAPTPRRA SSTPRIRLEP SKTFHARAAE TPPSKCSLER ASQPTRRAST PVNMLQTPEK
RQGADILTRL KSPDVSVNSP RIDRIAEFPI PSFDDEQLHP TTKLKLYPPS ITDQSITKDK
CTFQVLRSDS SKNHTGDSSD PSILGTDSNP LITSSSDWMK QRRFDTTSYR QRAEALEGLL
EFSAQLLQQE RFEELGILLK PFGPGKASPR ETAIWLSKSF KGTGL
