NEKL2_CAEEL
ID NEKL2_CAEEL Reviewed; 357 AA.
AC O01775;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Serine/threonine-protein kinase nekl-2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9HC98};
DE AltName: Full=Never in mitosis A kinase-like 2 {ECO:0000305|PubMed:25523392};
DE Short=NimA-kinase-like 2 {ECO:0000305};
GN Name=nekl-2 {ECO:0000312|WormBase:ZC581.1};
GN ORFNames=ZC581.1 {ECO:0000312|WormBase:ZC581.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25523392; DOI=10.1016/j.ydbio.2014.12.008;
RA Yochem J., Lazetic V., Bell L., Chen L., Fay D.;
RT "C. elegans NIMA-related kinases NEKL-2 and NEKL-3 are required for the
RT completion of molting.";
RL Dev. Biol. 398:255-266(2015).
CC -!- FUNCTION: Probable serine/threonine-protein kinase required for the
CC completion of molting. May play a role in endocytosis in the hypodermis
CC syncytium. {ECO:0000269|PubMed:25523392}.
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:0000250|UniProtKB:Q9HC98};
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:0000250|UniProtKB:Q9HC98};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9HC98};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25523392}. Note=In
CC hyp7 syncytium, localizes in puncta and small tubules near the plasma
CC membrane apical region. Does not co-localize with nekl-3.
CC {ECO:0000269|PubMed:25523392}.
CC -!- TISSUE SPECIFICITY: Expressed in hypodermal cells including in hyp7
CC syncytium but not in seam cells. {ECO:0000269|PubMed:25523392}.
CC -!- DISRUPTION PHENOTYPE: Failure to shed the cuticle at the end of the
CC first molt resulting in an arrest at the L1 to L2 transition stage.
CC RNAi-mediated knockdown results in a less severe phenotype
CC characterized by a failure to shed the cuticle only in the middle part
CC of the body at the end of the first molt. In hyp7 syncytium, RNAi-
CC mediated knockdown results in the apical membrane accumulation of lrp-1
CC and mislocalization of several components of the endocytic machinery.
CC {ECO:0000269|PubMed:25523392}.
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; FO080589; CCD64899.1; -; Genomic_DNA.
DR PIR; T29771; T29771.
DR RefSeq; NP_491914.1; NM_059513.4.
DR AlphaFoldDB; O01775; -.
DR SMR; O01775; -.
DR DIP; DIP-24804N; -.
DR IntAct; O01775; 1.
DR STRING; 6239.ZC581.1; -.
DR EPD; O01775; -.
DR PaxDb; O01775; -.
DR PeptideAtlas; O01775; -.
DR EnsemblMetazoa; ZC581.1.1; ZC581.1.1; WBGene00022631.
DR GeneID; 191199; -.
DR KEGG; cel:CELE_ZC581.1; -.
DR UCSC; ZC581.1; c. elegans.
DR CTD; 191199; -.
DR WormBase; ZC581.1; CE15235; WBGene00022631; nekl-2.
DR eggNOG; KOG0589; Eukaryota.
DR GeneTree; ENSGT00940000170273; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; O01775; -.
DR OMA; NNKDIWA; -.
DR OrthoDB; 1290401at2759; -.
DR PhylomeDB; O01775; -.
DR PRO; PR:O01775; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022631; Expressed in material anatomical entity and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; 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; IEA:UniProtKB-KW.
DR GO; GO:0042303; P:molting cycle; IMP:UniProtKB.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:UniProtKB.
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; Cytoplasm; Developmental protein; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..357
FT /note="Serine/threonine-protein kinase nekl-2"
FT /id="PRO_0000433008"
FT DOMAIN 4..267
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 281..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 357 AA; 40504 MW; D13844D0C145ACD8 CRC64;
MDNYEKVRVV GRGAFGVCWL CRGKNDASHQ KVIIKLINTH GMTEKEENSI QSEVNLLKKV
QHPLIIGYID SFIMDNQLGI VMQYAEGGTL ERLINDQRAI KDSNMREYFP EKTVLDYFTQ
ILIALNHMHQ KNIVHRDLKP QNILMNRRKT VLKLSDFGIS KELGTKSAAS TVIGTPNYLS
PEICESRPYN QKSDMWSLGC VLYELLQLER AFDGENLPAI VMKITRSKQN PLGDHVSNDV
KMLVENLLKT HTDKRPDVSQ LLSDPLVLPY LISIHCDLGR IEPPPTDKRK PSASLSSRLR
TYPTQSTLRP YSLSSNAPTT HLTQLTPMPS HIDSGFFSSG RTSNQRTQSR SQVHSKY
