NEK7_RAT
ID NEK7_RAT Reviewed; 302 AA.
AC D3ZBE5;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Serine/threonine-protein kinase Nek7;
DE EC=2.7.11.1;
DE AltName: Full=Never in mitosis A-related kinase 7;
DE Short=NimA-related protein kinase 7;
GN Name=Nek7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11516946; DOI=10.1016/s0960-9822(01)00369-4;
RA Belham C., Comb M.J., Avruch J.;
RT "Identification of the NIMA family kinases NEK6/7 as regulators of the p70
RT ribosomal S6 kinase.";
RL Curr. Biol. 11:1155-1167(2001).
CC -!- FUNCTION: Protein kinase which plays an important role in mitotic cell
CC cycle progression. Required for microtubule nucleation activity of the
CC centrosome, robust mitotic spindle formation and cytokinesis (By
CC similarity). Phosphorylates RPS6KB1 (PubMed:11516946). Phosphorylates
CC EML4 at 'Ser-146', promoting its dissociation from microtubules during
CC mitosis which is required for efficient chromosome congression (By
CC similarity). Essential protein for NLRP3 inflammasome assembly and
CC activation that acts downstream stimuli such as K(+) efflux.
CC Dispensable for the induction of core inflammasome components, but
CC necessary for subsequent formation of the NLRP3:PYCARD complex, and
CC activation of CASP1. Serves as a cellular switch that enforces mutual
CC exclusivity of the inflammasome response and cell division. Exerts its
CC effects on the NLRP3 inflammasome independently of its kinase activity
CC (By similarity). {ECO:0000250|UniProtKB:Q8TDX7,
CC ECO:0000250|UniProtKB:Q9ES74, ECO:0000269|PubMed:11516946}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Binding to NEK9 stimulates its activity by
CC releasing the autoinhibitory function of Tyr-97.
CC {ECO:0000250|UniProtKB:Q8TDX7}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with NEK9 (By similarity).
CC Interacts with ANKS3; this interaction alters the subcellular
CC distribution of NEK7 by preventing its nuclear translocation (By
CC similarity). Interacts (via N-terminus) with NLRP3 (via LRR repeat
CC domain); the interaction is required for the formation of the complex
CC NLRP3:PYCARD, oligomerization of PYCARD and activation of CASP1 (By
CC similarity). {ECO:0000250|UniProtKB:Q8TDX7,
CC ECO:0000250|UniProtKB:Q9ES74}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TDX7}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8TDX7}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q8TDX7}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q8TDX7}.
CC Note=Present at centrosome throughout the cell cycle. Also detected at
CC spindle midzone of the anaphase cells and eventually concentrates at
CC the midbody (By similarity). Interaction with ANKS3 prevents its
CC translocation to the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:Q8TDX7}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver.
CC {ECO:0000269|PubMed:11516946}.
CC -!- DOMAIN: Displays an autoinhibited conformation: Tyr-97 side chain
CC points into the active site, interacts with the activation loop, and
CC blocks the alphaC helix. The autoinhibitory conformation is released
CC upon binding with NEK9. {ECO:0000250|UniProtKB:Q8TDX7}.
CC -!- DOMAIN: The NTE (N-terminal extension) motif is a structural component
CC of the catalytic domain and thus contributes to activity.
CC {ECO:0000250|UniProtKB:Q8TDX7}.
CC -!- PTM: Phosphorylation at Ser-195 required for its activation.
CC {ECO:0000250|UniProtKB:Q8TDX7}.
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; CH473958; EDM09639.1; -; Genomic_DNA.
DR RefSeq; NP_001101816.1; NM_001108346.2.
DR RefSeq; XP_006249988.1; XM_006249926.3.
DR AlphaFoldDB; D3ZBE5; -.
DR SMR; D3ZBE5; -.
DR BioGRID; 262254; 1.
DR IntAct; D3ZBE5; 4.
DR STRING; 10116.ENSRNOP00000000817; -.
DR iPTMnet; D3ZBE5; -.
DR PhosphoSitePlus; D3ZBE5; -.
DR jPOST; D3ZBE5; -.
DR PaxDb; D3ZBE5; -.
DR PeptideAtlas; D3ZBE5; -.
DR PRIDE; D3ZBE5; -.
DR Ensembl; ENSRNOT00000000817; ENSRNOP00000000817; ENSRNOG00000000657.
DR GeneID; 360850; -.
DR KEGG; rno:360850; -.
DR UCSC; RGD:1311160; rat.
DR CTD; 140609; -.
DR RGD; 1311160; Nek7.
DR eggNOG; KOG0591; Eukaryota.
DR GeneTree; ENSGT00940000156725; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; D3ZBE5; -.
DR OrthoDB; 1290401at2759; -.
DR PhylomeDB; D3ZBE5; -.
DR TreeFam; TF105135; -.
DR PRO; PR:D3ZBE5; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Proteomes; UP000234681; Chromosome 13.
DR Bgee; ENSRNOG00000000657; Expressed in quadriceps femoris and 18 other tissues.
DR ExpressionAtlas; D3ZBE5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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; IDA:UniProtKB.
DR GO; GO:0035865; P:cellular response to potassium ion; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; ISS:UniProtKB.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:RGD.
DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:RGD.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00109; TYRKINASE.
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 Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..302
FT /note="Serine/threonine-protein kinase Nek7"
FT /id="PRO_0000412823"
FT DOMAIN 34..299
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 20..33
FT /note="NTE motif"
FT /evidence="ECO:0000250"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 40..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 97
FT /note="Autoinhibitory"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX7"
FT MOD_RES 195
FT /note="Phosphoserine; by NEK9"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX7"
SQ SEQUENCE 302 AA; 34529 MW; 1773BB6E19DFBEDA CRC64;
MDEQPQGMQG PPVPQFQPQK ALRPDMGYNT LANFRIEKKI GRGQFSEVYR ASCLLDGVPV
ALKKVQIFDL MDAKARADCI KEIDLLKQLN HPNVIKYYAS FIEDNELNIV LELADAGDLS
RMIKHFKKQK RLIPERTVWK YFVQLCSALD HMHSRRVMHR DIKPANVFIT ATGVVKLGDL
GLGRFFSSKT TAAHSLVGTP YYMSPERIHE NGYNFKSDIW SLGCLLYEMA ALQSPFYGDK
MNLYSLCKKI EQCDYPPLPS DHYSEELRQL VNICINPDPE KRPDIAYVYD VAKRMHACTA
SS
