NEKL3_CAEEL
ID NEKL3_CAEEL Reviewed; 302 AA.
AC G5EFM9;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Serine/threonine-protein kinase nekl-3 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9HC98};
DE AltName: Full=Molting protein MLT-1 {ECO:0000312|EMBL:ABG36763.1};
DE AltName: Full=Never in mitosis A kinase-like 3 {ECO:0000305|PubMed:25523392};
DE Short=NimA kinase-like 3 {ECO:0000305};
GN Name=nekl-3 {ECO:0000312|WormBase:F19H6.1};
GN Synonyms=mlt-1 {ECO:0000312|WormBase:F19H6.1};
GN ORFNames=F19H6.1 {ECO:0000312|WormBase:F19H6.1};
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:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP PRO-194.
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).
RN [2] {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).
CC -!- FUNCTION: Probable serine/threonine-protein kinase required for the
CC completion of molting. {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-2.
CC {ECO:0000269|PubMed:25523392}.
CC -!- TISSUE SPECIFICITY: Expressed in hypodermal cells including in hyp7
CC syncytium but not in seam cells. May be expressed in vulva, uterus and
CC some neurons. {ECO:0000269|PubMed:25523392}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the hypodermis at the beginning of
CC embryonic morphogenesis and throughout larval and adult stages.
CC {ECO:0000269|PubMed:25523392}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a failure to
CC shed the cuticle in the middle part of the body at the end of the first
CC molt. {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; DQ645955; ABG36763.1; -; mRNA.
DR EMBL; Z68115; CAA92169.2; -; Genomic_DNA.
DR EMBL; Z50873; CAA92169.2; JOINED; Genomic_DNA.
DR PIR; T21075; T21075.
DR RefSeq; NP_510080.2; NM_077679.5.
DR AlphaFoldDB; G5EFM9; -.
DR SMR; G5EFM9; -.
DR STRING; 6239.F19H6.1.2; -.
DR EPD; G5EFM9; -.
DR PaxDb; G5EFM9; -.
DR PeptideAtlas; G5EFM9; -.
DR EnsemblMetazoa; F19H6.1.1; F19H6.1.1; WBGene00008956.
DR EnsemblMetazoa; F19H6.1.2; F19H6.1.2; WBGene00008956.
DR GeneID; 181398; -.
DR KEGG; cel:CELE_F19H6.1; -.
DR CTD; 181398; -.
DR WormBase; F19H6.1; CE31484; WBGene00008956; nekl-3.
DR eggNOG; KOG0591; Eukaryota.
DR GeneTree; ENSGT00940000156725; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; G5EFM9; -.
DR OMA; MHAHTAT; -.
DR OrthoDB; 1290401at2759; -.
DR PhylomeDB; G5EFM9; -.
DR PRO; PR:G5EFM9; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00008956; Expressed in larva and 4 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0008406; P:gonad development; IGI:UniProtKB.
DR GO; GO:0042303; P:molting cycle; IMP:UniProtKB.
DR GO; GO:0035264; P:multicellular organism growth; IGI:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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; Cytoplasm; Developmental protein; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..302
FT /note="Serine/threonine-protein kinase nekl-3"
FT /id="PRO_0000433009"
FT DOMAIN 23..288
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 194
FT /note="P->L: Failure to shed the cuticle in the middle part
FT of the body at the end of the first molt."
FT /evidence="ECO:0000269|PubMed:25523392"
SQ SEQUENCE 302 AA; 34578 MW; C72304AEA9F90BAC CRC64;
MDKISNIYNF DDPPPDKLSL ELFIIEKKIG KGQFSEVFRA QCTWVDLHVA LKKIQVFEMV
DQKARQDCLK EIDLLKQLNH VNVIRYYASF IDNNQLNIVL ELAEAGDMSR MIKHFKKGGR
LIPEKTIWKY FVQLARALAH MHSKRIMHRD IKPANVFITG NGIVKLGDLG LGRFFSSKTT
AAHSLVGTPY YMSPERIQES GYNFKSDLWS TGCLLYEMAA LQSPFYGDKM NLYSLCKKIE
NCEYPPLPAD IYSTQLRDLV SRCILPEASK RPETSEVLQV AEHMNNYFSP SGDQSTTPST
QF
