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Serine/threonine-protein kinase dkf-1 (EC 2.7.11.13)

 DKF1_CAEEL              Reviewed;         722 AA.
Q9XUJ7;
22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
07-JUN-2017, entry version 136.
RecName: Full=Serine/threonine-protein kinase dkf-1 {ECO:0000303|PubMed:16613841};
EC=2.7.11.13;
Name=dkf-1; ORFNames=W09C5.5;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF
LYS-455 AND THR-588, AND PHOSPHORYLATION AT THR-588.
PubMed=16613841; DOI=10.1074/jbc.M511899200;
Feng H., Ren M., Wu S.-L., Hall D.H., Rubin C.S.;
"Characterization of a novel protein kinase D: Caenorhabditis elegans
DKF-1 is activated by translocation-phosphorylation and regulates
movement and growth in vivo.";
J. Biol. Chem. 281:17801-17814(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, DOMAIN,
PHOSPHORYLATION AT THR-588, UBIQUITINATION, AND MUTAGENESIS OF
PRO-109; PHE-197; LYS-298; TRP-396 AND THR-588.
PubMed=16613842; DOI=10.1074/jbc.M511898200;
Feng H., Ren M., Rubin C.S.;
"Conserved domains subserve novel mechanisms and functions in DKF-1, a
Caenorhabditis elegans protein kinase D.";
J. Biol. Chem. 281:17815-17826(2006).
[4] {ECO:0000305}
ENZYME ACTIVITY.
PubMed=17728253; DOI=10.1074/jbc.M701532200;
Feng H., Ren M., Chen L., Rubin C.S.;
"Properties, regulation, and in vivo functions of a novel protein
kinase D: Caenorhabditis elegans DKF-2 links diacylglycerol second
messenger to the regulation of stress responses and life span.";
J. Biol. Chem. 282:31273-31288(2007).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=27184844; DOI=10.1016/j.celrep.2016.04.052;
Najibi M., Labed S.A., Visvikis O., Irazoqui J.E.;
"An evolutionarily conserved PLC-PKD-TFEB pathway for host defense.";
Cell Rep. 15:1728-1742(2016).
-!- FUNCTION: Converts transient diacylglycerol (DAG) signals into
prolonged physiological effects, independently of PKC
(PubMed:16613841, PubMed:16613842). Role in the regulation of
growth and neuromuscular control of movement (PubMed:16613841,
PubMed:16613842). Involved in immune response to S.aureus
bacterium by activating transcription factor hlh-30 downstream of
phospholipase plc-1 (PubMed:27184844).
{ECO:0000269|PubMed:16613841, ECO:0000269|PubMed:16613842,
ECO:0000269|PubMed:27184844}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:16613841, ECO:0000269|PubMed:16613842,
ECO:0000269|PubMed:17728253}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:16613841,
ECO:0000269|PubMed:16613842, ECO:0000269|PubMed:17728253};
-!- ENZYME REGULATION: Activated by DAG and phorbol esters. Phorbol-
ester/DAG-type domain 1 binds phorbol ester with high affinity and
mediates accumulation at the cell periphery. Phorbol-ester/DAG-
type domain 2 binds phorbol ester with low affinity but may
mediates initial contact, resulting in a conformational change
allowing previously occluded domain 1 to anchor the kinase.
Phosphorylation on Thr-588 is then also required for activation
and may also result in a further conformational change.
{ECO:0000269|PubMed:16613841, ECO:0000269|PubMed:16613842}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16613841,
ECO:0000269|PubMed:16613842}. Membrane
{ECO:0000269|PubMed:16613841, ECO:0000269|PubMed:16613842}.
Note=Translocation to the cell membrane is required for kinase
activation. On activation, the protein may migrate back to the
cytoplasm. {ECO:0000269|PubMed:16613841,
ECO:0000269|PubMed:16613842}.
-!- TISSUE SPECIFICITY: Highly expressed in embryos and at lower
levels through the four larval stages in adults. Present in a
region bounded by the anterior and posterior bulbs of the pharynx
and an area of the tail containing the lumbar, dorsorectal and
pre-anal ganglia. Expressed in neurons.
{ECO:0000269|PubMed:16613841}.
-!- DOMAIN: The PH domain inhibits PKD catalytic activity in the
absence of DAG, either by direct steric occlusion or distortion of
the PKD catalytic cleft. {ECO:0000269|PubMed:16613842}.
-!- PTM: Prolonged phosphorylation at Thr-588 results in
ubiquitination and degradation. {ECO:0000269|PubMed:16613841,
ECO:0000269|PubMed:16613842}.
-!- DISRUPTION PHENOTYPE: Loss of movement due to severe or complete
loss of muscle contraction near the anus resulting in partial
paralysis of the tail region (PubMed:16613841). RNAi-mediated
knockdown results in a shortened lifespan, prevents transcription
factor hlh-30 nuclear translocation during S.aureus infection and
reduces survival following infection (PubMed:27184844).
{ECO:0000269|PubMed:16613841, ECO:0000269|PubMed:27184844}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. PKD subfamily. {ECO:0000255}.
-----------------------------------------------------------------------
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EMBL; Z82077; CAB04940.1; -; Genomic_DNA.
PIR; T26297; T26297.
RefSeq; NP_493390.1; NM_060989.5.
UniGene; Cel.16567; -.
ProteinModelPortal; Q9XUJ7; -.
SMR; Q9XUJ7; -.
BioGrid; 38628; 1.
STRING; 6239.W09C5.5; -.
iPTMnet; Q9XUJ7; -.
EPD; Q9XUJ7; -.
PaxDb; Q9XUJ7; -.
PeptideAtlas; Q9XUJ7; -.
EnsemblMetazoa; W09C5.5; W09C5.5; WBGene00012352.
GeneID; 173234; -.
KEGG; cel:CELE_W09C5.5; -.
UCSC; W09C5.5; c. elegans.
CTD; 173234; -.
WormBase; W09C5.5; CE20167; WBGene00012352; dkf-1.
eggNOG; KOG4236; Eukaryota.
eggNOG; ENOG410XQZ3; LUCA.
GeneTree; ENSGT00840000129794; -.
HOGENOM; HOG000015135; -.
InParanoid; Q9XUJ7; -.
KO; K06070; -.
OMA; FGYARFI; -.
OrthoDB; EOG091G02RG; -.
PhylomeDB; Q9XUJ7; -.
Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
SignaLink; Q9XUJ7; -.
PRO; PR:Q9XUJ7; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00012352; -.
GO; GO:0030424; C:axon; IDA:WormBase.
GO; GO:0005938; C:cell cortex; IDA:WormBase.
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0030425; C:dendrite; IDA:WormBase.
GO; GO:0016020; C:membrane; IDA:WormBase.
GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
GO; GO:0005886; C:plasma membrane; IDA:WormBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004697; F:protein kinase C activity; IEA:UniProtKB-EC.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
GO; GO:0002253; P:activation of immune response; IMP:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; IMP:UniProtKB.
GO; GO:0089700; P:protein kinase D signaling; IBA:GO_Central.
GO; GO:1902477; P:regulation of defense response to bacterium, incompatible interaction; IMP:UniProtKB.
CDD; cd00029; C1; 2.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR015727; Protein_Kinase_C_mu-related.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR22968; PTHR22968; 1.
Pfam; PF00130; C1_1; 2.
Pfam; PF00069; Pkinase; 1.
SMART; SM00109; C1; 2.
SMART; SM00233; PH; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 2.
PROSITE; PS50081; ZF_DAG_PE_2; 2.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium;
Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 722 Serine/threonine-protein kinase dkf-1.
/FTId=PRO_0000385352.
DOMAIN 279 407 PH. {ECO:0000255}.
DOMAIN 426 685 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 98 148 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 186 236 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 432 440 ATP. {ECO:0000250|UniProtKB:P28523,
ECO:0000255|PROSITE-ProRule:PRU00159}.
ACT_SITE 551 551 Proton acceptor.
{ECO:0000250|UniProtKB:P28523,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027}.
BINDING 455 455 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:16613841}.
MOD_RES 588 588 Phosphothreonine.
{ECO:0000269|PubMed:16613841,
ECO:0000269|PubMed:16613842}.
MUTAGEN 109 109 P->G: Loss of sensitivity to phorbol
ester or DAG stimulation of kinase
activity. Loss of sensitivity to phorbol
ester or DAG stimulation of kinase
activity; when associated with G-197.
{ECO:0000269|PubMed:16613842}.
MUTAGEN 197 197 F->G: Increase in sensitivity to phorbol
ester or DAG stimulation of kinase
activity. Loss of sensitivity to phorbol
ester or DAG stimulation of kinase
activity; when associated with G-109.
{ECO:0000269|PubMed:16613842}.
MUTAGEN 298 298 K->A: Increase in sensitivity to phorbol
ester-stimulation of kinase activity.
{ECO:0000269|PubMed:16613842}.
MUTAGEN 396 396 W->A: Increase in sensitivity to phorbol
ester-stimulation of kinase activity.
{ECO:0000269|PubMed:16613842}.
MUTAGEN 455 455 K->Q: Loss of kinase activity.
{ECO:0000269|PubMed:16613841}.
MUTAGEN 588 588 T->A: Loss of basal kinase activity and
phorbol ester-stimulated kinase activity.
Resistant to proteasome-mediated
degradation.
{ECO:0000269|PubMed:16613841,
ECO:0000269|PubMed:16613842}.
MUTAGEN 588 588 T->D: High basal kinase activity, loss of
phorbol ester-stimulated kinase activity.
{ECO:0000269|PubMed:16613841,
ECO:0000269|PubMed:16613842}.
MUTAGEN 588 588 T->E: High basal kinase activity, loss of
phorbol ester-stimulated kinase activity.
{ECO:0000269|PubMed:16613841,
ECO:0000269|PubMed:16613842}.
MUTAGEN 588 588 T->S: No effect on basal kinase activity,
phorbol ester-stimulated kinase activity,
or stability.
{ECO:0000269|PubMed:16613841,
ECO:0000269|PubMed:16613842}.
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


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