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Serine/threonine-protein kinase dkf-2 (EC 2.7.11.13) (D kinase family-2)

 DKF2_CAEEL              Reviewed;        1070 AA.
O45818; B1V8I6; G5EEQ6; H9G324; H9G325; O62166; O62167;
22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
20-MAY-2008, sequence version 4.
28-MAR-2018, entry version 162.
RecName: Full=Serine/threonine-protein kinase dkf-2 {ECO:0000303|PubMed:17728253};
EC=2.7.11.13;
AltName: Full=D kinase family-2 {ECO:0000303|PubMed:17728253};
Name=dkf-2; ORFNames=T25E12.4;
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
PRO-332; PRO-484; LYS-643; SER-925 AND SER-929, AND PHOSPHORYLATION AT
SER-925 AND SER-929.
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).
[2] {ECO:0000312|EMBL:CAB04830.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB04830.2};
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, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
AND MUTAGENESIS OF SER-925 AND SER-929.
PubMed=19371715; DOI=10.1016/j.immuni.2009.03.007;
Ren M., Feng H., Fu Y., Land M., Rubin C.S.;
"Protein kinase D is an essential regulator of C. elegans innate
immunity.";
Immunity 30:521-532(2009).
-!- FUNCTION: Converts transient diacylglycerol (DAG) signals into
prolonged physiological effects, downstream of PKC. Acts in the
intestine to regulate both innate immunity by promoting activation
of PMK-1 and also stress response and life span by acting as an
upstream, negative regulator of the daf-16 transcription factor.
{ECO:0000269|PubMed:17728253, ECO:0000269|PubMed:19371715}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:17728253, ECO:0000269|PubMed:19371715}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:17728253,
ECO:0000269|PubMed:19371715};
-!- ENZYME REGULATION: Activated by DAG and phorbol esters. Phorbol-
ester/DAG-type domain 1 binds phorbol ester with low affinity.
Phorbol-ester/DAG-type domain 2 binds phorbol ester with high
affinity and targets the kinase to the cell periphery, enabling
phosphorylation and activation by colocalized tpa-1. Both domains
1 and 2 appear to bind DAG with equal affinity so may contribute
equally to translocation and activation.
{ECO:0000269|PubMed:17728253, ECO:0000269|PubMed:19371715}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17728253}.
Membrane {ECO:0000269|PubMed:17728253}. Note=Translocation to the
cell membrane is required for kinase activation.
{ECO:0000269|PubMed:17728253}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=a {ECO:0000269|PubMed:9851916};
IsoId=O45818-1; Sequence=Displayed;
Note=No experimental confirmation available. {ECO:0000305};
Name=b {ECO:0000269|PubMed:9851916};
IsoId=O45818-2; Sequence=VSP_053150, VSP_053153, VSP_053154,
VSP_053155;
Note=No experimental confirmation available. {ECO:0000305};
Name=c {ECO:0000269|PubMed:9851916};
IsoId=O45818-3; Sequence=VSP_053151, VSP_053152;
Note=No experimental confirmation available. {ECO:0000305};
Name=d;
IsoId=O45818-4; Sequence=VSP_053247;
Note=No experimental confirmation available.;
Name=e;
IsoId=O45818-5; Sequence=VSP_053248;
Note=No experimental confirmation available.;
Name=f;
IsoId=O45818-6; Sequence=VSP_053249;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in the late embryo, all larval
stages, and adult in the intestine and in cells positioned near
the posterior bulb of the pharynx. {ECO:0000269|PubMed:17728253,
ECO:0000269|PubMed:19371715}.
-!- PTM: Phosphorylation on Ser-925 by tpa-1 is the dominant regulator
of catalysis, phosphorylation on Ser-929 by tpa-1 has a lesser
effect. Prolonged phosphorylation results in ubiquitination and
degradation. {ECO:0000269|PubMed:17728253}.
-!- DISRUPTION PHENOTYPE: Increase in adult life span. Increased
levels of daf-16 translocate into the nucleus in response to heat
stress. Hypersensitive to killing by bacteria.
{ECO:0000269|PubMed:17728253, ECO:0000269|PubMed:19371715}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. PKD subfamily. {ECO:0000255}.
-----------------------------------------------------------------------
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EMBL; Z82052; CAB04830.2; -; Genomic_DNA.
EMBL; AL021507; CAB04830.2; JOINED; Genomic_DNA.
EMBL; AL021572; CAB04830.2; JOINED; Genomic_DNA.
EMBL; Z92967; CAB04830.2; JOINED; Genomic_DNA.
EMBL; Z92967; CAB07477.1; -; Genomic_DNA.
EMBL; Z92967; CAQ35035.1; -; Genomic_DNA.
EMBL; AL021507; CAQ35035.1; JOINED; Genomic_DNA.
EMBL; AL021572; CAQ35035.1; JOINED; Genomic_DNA.
EMBL; Z92967; CCD31057.1; -; Genomic_DNA.
EMBL; AL021507; CCD31057.1; JOINED; Genomic_DNA.
EMBL; AL021572; CCD31057.1; JOINED; Genomic_DNA.
EMBL; Z82052; CCG28246.1; -; Genomic_DNA.
EMBL; AL021507; CCG28246.1; JOINED; Genomic_DNA.
EMBL; AL021572; CCG28246.1; JOINED; Genomic_DNA.
EMBL; Z92967; CCG28246.1; JOINED; Genomic_DNA.
EMBL; Z82052; CCG28247.1; -; Genomic_DNA.
EMBL; AL021507; CCG28247.1; JOINED; Genomic_DNA.
EMBL; AL021572; CCG28247.1; JOINED; Genomic_DNA.
EMBL; Z92967; CCG28247.1; JOINED; Genomic_DNA.
RefSeq; NP_001123022.1; NM_001129550.1. [O45818-3]
RefSeq; NP_001256724.1; NM_001269795.1. [O45818-5]
RefSeq; NP_001256725.1; NM_001269796.1. [O45818-6]
RefSeq; NP_001256726.1; NM_001269797.1. [O45818-4]
RefSeq; NP_507239.2; NM_074838.5. [O45818-1]
RefSeq; NP_507240.1; NM_074839.3.
UniGene; Cel.17825; -.
ProteinModelPortal; O45818; -.
SMR; O45818; -.
STRING; 6239.T25E12.4a; -.
iPTMnet; O45818; -.
PaxDb; O45818; -.
PeptideAtlas; O45818; -.
EnsemblMetazoa; T25E12.4a; T25E12.4a; WBGene00012019. [O45818-1]
GeneID; 180121; -.
KEGG; cel:CELE_T25E12.4; -.
UCSC; T25E12.4a; c. elegans.
CTD; 180121; -.
WormBase; T25E12.4a; CE42484; WBGene00012019; dkf-2. [O45818-1]
WormBase; T25E12.4b; CE52401; WBGene00012019; dkf-2. [O45818-2]
WormBase; T25E12.4c; CE42507; WBGene00012019; dkf-2. [O45818-3]
WormBase; T25E12.4d; CE46242; WBGene00012019; dkf-2. [O45818-4]
WormBase; T25E12.4e; CE47100; WBGene00012019; dkf-2. [O45818-5]
WormBase; T25E12.4f; CE47405; WBGene00012019; dkf-2. [O45818-6]
eggNOG; KOG4236; Eukaryota.
eggNOG; ENOG410XQZ3; LUCA.
GeneTree; ENSGT00910000144054; -.
HOGENOM; HOG000015135; -.
InParanoid; O45818; -.
KO; K06070; -.
OMA; GEMQDPD; -.
OrthoDB; EOG091G02RG; -.
PhylomeDB; O45818; -.
Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
SignaLink; O45818; -.
PRO; PR:O45818; -.
Proteomes; UP000001940; Chromosome V.
Bgee; WBGene00012019; -.
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:WormBase.
GO; GO:0005829; C:cytosol; IDA:WormBase.
GO; GO:0016020; C:membrane; IDA:WormBase.
GO; GO:0005886; C:plasma membrane; IDA:WormBase.
GO; GO:1902554; C:serine/threonine protein kinase complex; IDA:WormBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IPI:WormBase.
GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
GO; GO:0004697; F:protein kinase C activity; IEA:UniProtKB-EC.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:WormBase.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:WormBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
GO; GO:0045087; P:innate immune response; IMP:WormBase.
GO; GO:0035556; P:intracellular signal transduction; IMP:WormBase.
GO; GO:0042308; P:negative regulation of protein import into nucleus; IMP:WormBase.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IGI:WormBase.
GO; GO:0089700; P:protein kinase D signaling; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
CDD; cd00029; C1; 2.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
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; PF00169; PH; 1.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 2.
SMART; SM00233; PH; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50003; PH_DOMAIN; 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;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Immunity; Innate immunity; Kinase; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 1070 Serine/threonine-protein kinase dkf-2.
/FTId=PRO_0000385354.
DOMAIN 624 726 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 770 1026 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 321 371 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 473 523 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 776 784 ATP. {ECO:0000250|UniProtKB:P28523,
ECO:0000255|PROSITE-ProRule:PRU00159}.
COMPBIAS 217 220 Poly-Ser. {ECO:0000255}.
ACT_SITE 893 893 Proton acceptor.
{ECO:0000250|UniProtKB:P28523,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027}.
BINDING 799 799 ATP. {ECO:0000250|UniProtKB:Q9XUJ7,
ECO:0000255|PROSITE-ProRule:PRU00159}.
MOD_RES 925 925 Phosphoserine.
{ECO:0000269|PubMed:17728253}.
MOD_RES 929 929 Phosphoserine.
{ECO:0000269|PubMed:17728253}.
VAR_SEQ 1 533 Missing (in isoform b).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_053150.
VAR_SEQ 1 222 Missing (in isoform d). {ECO:0000305}.
/FTId=VSP_053247.
VAR_SEQ 1 197 Missing (in isoform c).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_053151.
VAR_SEQ 198 310 DHSDDEVWTPYRPPPNREYSSSSEPMMGDLTFRLQSGIHKK
SIAVEGTEIALRDLRNEALQFIKEIYPEKGCSSLEDYILLY
KHDLRSINILQLITTSSDVTDGTLVEVVIGS -> MTDRHP
ESKTSTSSNSPSISSSTSSSLKMMKKQQRAKSCATPNSGRK
SPRLEVKAMTISSSPTAQRFVFQQQASFQVLEDFENLKVYE
EKEKQRKKEKAPDVGRRTYIVIGA (in isoform c).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_053152.
VAR_SEQ 470 471 Missing (in isoform e). {ECO:0000305}.
/FTId=VSP_053248.
VAR_SEQ 534 701 LGSQADDGASEDRDDDLSLRSGSGAHKKAQNTPSAPLQGSE
GSGSPGPVVSFAANALSNMPDDDVISSESANIPLMRVVMSK
KQTKRKNNKLLKEGWIVHYTDQQNMRKKHYWRLDTKGITMY
QDENTTRYYKEIPLNEILNVSMSPPDKTADYLFEIRTGVCV
YFIS -> MILNILRLPHADEPTTSQSVQDYPLVHFSPRRH
QKFRTIISVGDSDVIKDSSLTDEELYNIIHASPIARKSSTV
SSTDSGYLGSSGASSSCVRSREGSTVSSTITVERTRRGGST
ASSEPDSVADSEGAGSYSSFSSIASTASRMLGRAADCLVLM
TKRNGWSGDA (in isoform b).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_053153.
VAR_SEQ 541 541 G -> GTSLTGSMDNLRMCSVPFGSDQSTSG (in
isoform f). {ECO:0000305}.
/FTId=VSP_053249.
VAR_SEQ 750 755 ETGHLG -> KTRPPY (in isoform b).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_053154.
VAR_SEQ 756 1070 Missing (in isoform b).
{ECO:0000303|PubMed:9851916}.
/FTId=VSP_053155.
MUTAGEN 332 332 P->G: Loss of sensitivity to phorbol
ester or DAG stimulation of kinase
activity; when associated with G-484. No
effect on sensitivity to phorbol ester,
loss of DAG stimulation of kinase
activity. {ECO:0000269|PubMed:17728253}.
MUTAGEN 484 484 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-332.
{ECO:0000269|PubMed:17728253}.
MUTAGEN 643 643 K->A: Small increase in basal kinase
activity, no effect on sensitivity to
phorbol ester stimulation of kinase
activity. {ECO:0000269|PubMed:17728253}.
MUTAGEN 925 925 S->A: Loss of sensitivity to phorbol
ester stimulation of kinase activity.
{ECO:0000269|PubMed:17728253,
ECO:0000269|PubMed:19371715}.
MUTAGEN 925 925 S->D: High basal kinase activity, loss of
phorbol ester-stimulated kinase activity
and ability to phosphorylate pmk-1; when
associated with D-929.
{ECO:0000269|PubMed:17728253,
ECO:0000269|PubMed:19371715}.
MUTAGEN 929 929 S->A: Moderate loss of sensitivity to
phorbol ester stimulation of kinase
activity. {ECO:0000269|PubMed:17728253,
ECO:0000269|PubMed:19371715}.
MUTAGEN 929 929 S->D: High basal kinase activity, loss of
phorbol ester-stimulated kinase activity
and ability to phosphorylate pmk-1; when
associated with D-925.
{ECO:0000269|PubMed:17728253,
ECO:0000269|PubMed:19371715}.
SEQUENCE 1070 AA; 120583 MW; 6A4891629C021973 CRC64;
MDANDYPRLY YTSMPSSSTS MVTTTRFSTS FSPSIPCHRQ ENFRRHSTSA LAKRNGSESE
KSAEIRENPD EIEVSRVSGR DSSLAFYTTA HETSSMLSRD SRDETLTPNE HIHQASSRRV
SANDSVFEDG YVDFVDEPRE HGSRRKSFEK FTDRNGEEKE GRVFELSTPQ PTREAAPGAH
QFQLPTLLVT STPTTVFDHS DDEVWTPYRP PPNREYSSSS EPMMGDLTFR LQSGIHKKSI
AVEGTEIALR DLRNEALQFI KEIYPEKGCS SLEDYILLYK HDLRSINILQ LITTSSDVTD
GTLVEVVIGS CPQNERIVVH PHTLFVHSYK VPTFCDFCGE LLFGLVKQGL KCFGCGLNYH
KRCASKIPNN CNGSKQRRPS AIPLSPSNSN ILNLNERRHS RRESCLEALD AARPSSTLGG
AATPNIFITS DDCGDAVGGN YLQMPRKDRS CSWSGRPLWM EIAEATRVKL QVPHTFQVHS
YKLPTVCQHC KKLLKGLIRQ GMQCRDCKYN CHKKCSEHVA KDCSGNTKAS QFFLGSQADD
GASEDRDDDL SLRSGSGAHK KAQNTPSAPL QGSEGSGSPG PVVSFAANAL SNMPDDDVIS
SESANIPLMR VVMSKKQTKR KNNKLLKEGW IVHYTDQQNM RKKHYWRLDT KGITMYQDEN
TTRYYKEIPL NEILNVSMSP PDKTADYLFE IRTGVCVYFI SGSPSDEKGS SLDAQSWTTA
IQSALMPVTP QSSVVGGKRI DKLKVPTEGE TGHLGAKIQT EHEFSQLYQI FAEEVLGSGQ
FGTVYGGIHR RNGQHVAVKL IDKLKFPPNK EDLLRAEVQI LEKVDHPGVV HFMQMLETTD
RIFVVMEKLK GDMLEMILSS EKGRLSERTT QFLVAQILEA LRYLHHLNIV HCDLKPENIL
LNSNSDFPQV KLCDFGFARI IGEKSFRRSV VGTPAYLAPE VLRNKGFNRS LDMWSVGVIV
YVSLSGTFPF NEDEDINDQI QNAEFMYPPT PWKEISENAI EFINGLLQVK MSKRYTVTKA
QSQIWMQNYT LWSDLRVLEK AVGQRFVTHE SDDVRWQAYE KEHNVTPVYV


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