DKF1_CAEEL
ID DKF1_CAEEL Reviewed; 722 AA.
AC Q9XUJ7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Serine/threonine-protein kinase dkf-1 {ECO:0000303|PubMed:16613841};
DE EC=2.7.11.13;
GN Name=dkf-1; ORFNames=W09C5.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-455
RP AND THR-588, AND PHOSPHORYLATION AT THR-588.
RX PubMed=16613841; DOI=10.1074/jbc.m511899200;
RA Feng H., Ren M., Wu S.-L., Hall D.H., Rubin C.S.;
RT "Characterization of a novel protein kinase D: Caenorhabditis elegans DKF-1
RT is activated by translocation-phosphorylation and regulates movement and
RT growth in vivo.";
RL J. Biol. Chem. 281:17801-17814(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [3] {ECO:0000305}
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, DOMAIN,
RP PHOSPHORYLATION AT THR-588, UBIQUITINATION, AND MUTAGENESIS OF PRO-109;
RP PHE-197; LYS-298; TRP-396 AND THR-588.
RX PubMed=16613842; DOI=10.1074/jbc.m511898200;
RA Feng H., Ren M., Rubin C.S.;
RT "Conserved domains subserve novel mechanisms and functions in DKF-1, a
RT Caenorhabditis elegans protein kinase D.";
RL J. Biol. Chem. 281:17815-17826(2006).
RN [4] {ECO:0000305}
RP ENZYME ACTIVITY.
RX PubMed=17728253; DOI=10.1074/jbc.m701532200;
RA Feng H., Ren M., Chen L., Rubin C.S.;
RT "Properties, regulation, and in vivo functions of a novel protein kinase D:
RT Caenorhabditis elegans DKF-2 links diacylglycerol second messenger to the
RT regulation of stress responses and life span.";
RL J. Biol. Chem. 282:31273-31288(2007).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27184844; DOI=10.1016/j.celrep.2016.04.052;
RA Najibi M., Labed S.A., Visvikis O., Irazoqui J.E.;
RT "An evolutionarily conserved PLC-PKD-TFEB pathway for host defense.";
RL Cell Rep. 15:1728-1742(2016).
CC -!- FUNCTION: Converts transient diacylglycerol (DAG) signals into
CC prolonged physiological effects, independently of PKC (PubMed:16613841,
CC PubMed:16613842). Role in the regulation of growth and neuromuscular
CC control of movement (PubMed:16613841, PubMed:16613842). Involved in
CC immune response to S.aureus bacterium by activating transcription
CC factor hlh-30 downstream of phospholipase plc-1 (PubMed:27184844).
CC {ECO:0000269|PubMed:16613841, ECO:0000269|PubMed:16613842,
CC ECO:0000269|PubMed:27184844}.
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=2.7.11.13;
CC Evidence={ECO:0000269|PubMed:16613841, ECO:0000269|PubMed:16613842,
CC ECO:0000269|PubMed:17728253};
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=2.7.11.13; Evidence={ECO:0000269|PubMed:16613841,
CC ECO:0000269|PubMed:16613842, ECO:0000269|PubMed:17728253};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16613841, ECO:0000269|PubMed:16613842,
CC ECO:0000269|PubMed:17728253};
CC -!- ACTIVITY REGULATION: Activated by DAG and phorbol esters. Phorbol-
CC ester/DAG-type domain 1 binds phorbol ester with high affinity and
CC mediates accumulation at the cell periphery. Phorbol-ester/DAG-type
CC domain 2 binds phorbol ester with low affinity but may mediate initial
CC contact, resulting in a conformational change allowing previously
CC occluded domain 1 to anchor the kinase. Phosphorylation on Thr-588 is
CC then also required for activation and may also result in a further
CC conformational change. {ECO:0000269|PubMed:16613841,
CC ECO:0000269|PubMed:16613842}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16613841,
CC ECO:0000269|PubMed:16613842}. Membrane {ECO:0000269|PubMed:16613841,
CC ECO:0000269|PubMed:16613842}. Note=Translocation to the cell membrane
CC is required for kinase activation. On activation, the protein may
CC migrate back to the cytoplasm. {ECO:0000269|PubMed:16613841,
CC ECO:0000269|PubMed:16613842}.
CC -!- TISSUE SPECIFICITY: Highly expressed in embryos and at lower levels
CC through the four larval stages in adults. Present in a region bounded
CC by the anterior and posterior bulbs of the pharynx and an area of the
CC tail containing the lumbar, dorsorectal and pre-anal ganglia. Expressed
CC in neurons. {ECO:0000269|PubMed:16613841}.
CC -!- DOMAIN: The PH domain inhibits PKD catalytic activity in the absence of
CC DAG, either by direct steric occlusion or distortion of the PKD
CC catalytic cleft. {ECO:0000269|PubMed:16613842}.
CC -!- PTM: Prolonged phosphorylation at Thr-588 results in ubiquitination and
CC degradation. {ECO:0000269|PubMed:16613841,
CC ECO:0000269|PubMed:16613842}.
CC -!- DISRUPTION PHENOTYPE: Loss of movement due to severe or complete loss
CC of muscle contraction near the anus resulting in partial paralysis of
CC the tail region (PubMed:16613841). RNAi-mediated knockdown results in a
CC shortened lifespan, prevents transcription factor hlh-30 nuclear
CC translocation during S.aureus infection and reduces survival following
CC infection (PubMed:27184844). {ECO:0000269|PubMed:16613841,
CC ECO:0000269|PubMed:27184844}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PKD subfamily. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z82077; CAB04940.1; -; Genomic_DNA.
DR PIR; T26297; T26297.
DR RefSeq; NP_493390.1; NM_060989.5.
DR PDB; 6RA0; X-ray; 2.26 A; A=1-151.
DR PDBsum; 6RA0; -.
DR AlphaFoldDB; Q9XUJ7; -.
DR SMR; Q9XUJ7; -.
DR BioGRID; 38628; 1.
DR STRING; 6239.W09C5.5; -.
DR iPTMnet; Q9XUJ7; -.
DR EPD; Q9XUJ7; -.
DR PaxDb; Q9XUJ7; -.
DR PeptideAtlas; Q9XUJ7; -.
DR PRIDE; Q9XUJ7; -.
DR EnsemblMetazoa; W09C5.5.1; W09C5.5.1; WBGene00012352.
DR GeneID; 173234; -.
DR KEGG; cel:CELE_W09C5.5; -.
DR UCSC; W09C5.5; c. elegans.
DR CTD; 173234; -.
DR WormBase; W09C5.5; CE20167; WBGene00012352; dkf-1.
DR eggNOG; KOG4236; Eukaryota.
DR GeneTree; ENSGT00950000183024; -.
DR HOGENOM; CLU_009772_0_0_1; -.
DR InParanoid; Q9XUJ7; -.
DR OMA; YARFIPE; -.
DR OrthoDB; 367841at2759; -.
DR PhylomeDB; Q9XUJ7; -.
DR Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:Q9XUJ7; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00012352; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0016020; C:membrane; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
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:WormBase.
DR GO; GO:0002253; P:activation of immune response; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB.
DR GO; GO:0089700; P:protein kinase D signaling; IBA:GO_Central.
DR CDD; cd00029; C1; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015727; Protein_Kinase_C_mu-related.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22968; PTHR22968; 2.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..722
FT /note="Serine/threonine-protein kinase dkf-1"
FT /id="PRO_0000385352"
FT DOMAIN 279..407
FT /note="PH"
FT /evidence="ECO:0000255"
FT DOMAIN 426..685
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 98..148
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 186..236
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ACT_SITE 551
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 432..440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:16613841"
FT MOD_RES 588
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16613841,
FT ECO:0000269|PubMed:16613842"
FT MUTAGEN 109
FT /note="P->G: Loss of sensitivity to phorbol ester or DAG
FT stimulation of kinase activity. Loss of sensitivity to
FT phorbol ester or DAG stimulation of kinase activity; when
FT associated with G-197."
FT /evidence="ECO:0000269|PubMed:16613842"
FT MUTAGEN 197
FT /note="F->G: Increase in sensitivity to phorbol ester or
FT DAG stimulation of kinase activity. Loss of sensitivity to
FT phorbol ester or DAG stimulation of kinase activity; when
FT associated with G-109."
FT /evidence="ECO:0000269|PubMed:16613842"
FT MUTAGEN 298
FT /note="K->A: Increase in sensitivity to phorbol ester-
FT stimulation of kinase activity."
FT /evidence="ECO:0000269|PubMed:16613842"
FT MUTAGEN 396
FT /note="W->A: Increase in sensitivity to phorbol ester-
FT stimulation of kinase activity."
FT /evidence="ECO:0000269|PubMed:16613842"
FT MUTAGEN 455
FT /note="K->Q: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:16613841"
FT MUTAGEN 588
FT /note="T->A: Loss of basal kinase activity and phorbol
FT ester-stimulated kinase activity. Resistant to proteasome-
FT mediated degradation."
FT /evidence="ECO:0000269|PubMed:16613841,
FT ECO:0000269|PubMed:16613842"
FT MUTAGEN 588
FT /note="T->D: High basal kinase activity, loss of phorbol
FT ester-stimulated kinase activity."
FT /evidence="ECO:0000269|PubMed:16613841,
FT ECO:0000269|PubMed:16613842"
FT MUTAGEN 588
FT /note="T->E: High basal kinase activity, loss of phorbol
FT ester-stimulated kinase activity."
FT /evidence="ECO:0000269|PubMed:16613841,
FT ECO:0000269|PubMed:16613842"
FT MUTAGEN 588
FT /note="T->S: No effect on basal kinase activity, phorbol
FT ester-stimulated kinase activity, or stability."
FT /evidence="ECO:0000269|PubMed:16613841,
FT ECO:0000269|PubMed:16613842"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:6RA0"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:6RA0"
FT HELIX 33..49
FT /evidence="ECO:0007829|PDB:6RA0"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:6RA0"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:6RA0"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6RA0"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:6RA0"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:6RA0"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:6RA0"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:6RA0"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:6RA0"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:6RA0"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:6RA0"
SQ SEQUENCE 722 AA; 80962 MW; 13B00CC189AFC73E CRC64;
MDGSQGSTDY GDHVVLRYGG TREMVPLIRH EQMLDMLMER ARQIVQGFGN LDTRNMYLFR
HEYNSPTLLY PITSASQITS GSILEIILVD RTEAAVIPHV VEPESYMRPT FCDFCGEMLT
GLMRQGVKCK NCNGNFHKRC SNAARNNCGA PGAPGAQPSR PPILPPIPTT PTGFPVAALS
TPTGLPHTLI EHSYRQFTVC KVCDHLLVGL VKQGLKCRDC GVNVHRKCAM ELASNCVLSE
NAISRVNFTD PEGPGSSSSD NIPLFRLPGQ VGTRATEKKK LEGWMMHFIL SDPERRLKHY
WMMQSNAIHL YNEYSEGIGV NPNRVYRIIP LAEITSVVQN NGKSVLAKHP PHCFEIRTTT
NTVFCVGEDY HAFSGGPPKK IPRSMSVRPS SNTTMWFQFI KESLQPPSRN EDNAEQALEF
ANLYQVLSDK TLGSGQFGTV YSAIQRHSGK EVAVKVISKE RFSKKGSGAE SMRAEVAILQ
QTCHPGIVCL EFMCETKDKI FVVMEKMNGD MLEMILSQEL GRLNSRATKF LLVQILCALK
YLHDQGIAHC DLKPENVLLS DMGSNFPQTK ICDFGYARFI PESQFRKTVV GTPAYLPPEV
LQRKGYNKSL DMWSVGVIIY VTLSGTFPFN EGEEISEQIQ NASFMFPTEP WSEVEPLAVD
LIQKLLKVEI EARMSIEQCL DHGWLKGEQL YRDLRDLEVR LNTPRYLTSP QDDILYGTLV
NP
