DAPK_CAEEL
ID DAPK_CAEEL Reviewed; 1425 AA.
AC O44997; Q3ZLV1;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Death-associated protein kinase dapk-1;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P53355};
GN Name=dapk-1 {ECO:0000312|WormBase:K12C11.4}; Synonyms=mor-3, tag-119;
GN ORFNames=K12C11.4;
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].
RA Chen J.-Y., Chen R.-H., Wu Y.-C.;
RT "Molecular characterization of DAP kinase in Caenorhabditis elegans.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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, AND DISRUPTION PHENOTYPE.
RX PubMed=17785524; DOI=10.1101/gad.1573107;
RA Kang C., You Y.J., Avery L.;
RT "Dual roles of autophagy in the survival of Caenorhabditis elegans during
RT starvation.";
RL Genes Dev. 21:2161-2171(2007).
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19164535; DOI=10.1073/pnas.0809339106;
RA Tong A., Lynn G., Ngo V., Wong D., Moseley S.L., Ewbank J.J., Goncharov A.,
RA Wu Y.C., Pujol N., Chisholm A.D.;
RT "Negative regulation of Caenorhabditis elegans epidermal damage responses
RT by death-associated protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1457-1461(2009).
RN [5]
RP FUNCTION, INTERACTION WITH PTRN-1, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF LYS-57 AND SER-179.
RX PubMed=27661253; DOI=10.7554/elife.15833;
RA Chuang M., Hsiao T.I., Tong A., Xu S., Chisholm A.D.;
RT "DAPK interacts with Patronin and the microtubule cytoskeleton in epidermal
RT development and wound repair.";
RL Elife 5:E15833-E15833(2016).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF SER-179.
RX PubMed=28087624; DOI=10.1242/dev.146001;
RA Chen F., Chisholm A.D., Jin Y.;
RT "Tissue-specific regulation of alternative polyadenylation represses
RT expression of a neuronal ankyrin isoform in C. elegans epidermal
RT development.";
RL Development 144:698-707(2017).
CC -!- FUNCTION: Negative regulator of epidermal barrier repair and innate
CC immune responses to wounding (PubMed:19164535, PubMed:27661253). The
CC role in epidermal tissue integrity and wound healing is established
CC through the inhibition of epidermal microtubule stability, possibly via
CC the negative regulation of the microtubule minus-end binding protein
CC ptrn-1 (PubMed:27661253). In epidermis, prevents expression of specific
CC unc-44 isoforms probably by promoting nuclear localization of pinn-1,
CC which in turn may affect sydn-1-ssup-72-mediated regulation of
CC alternative polyadenylation of unc-44 mRNA (PubMed:28087624). Appears
CC to act downstream of or in parallel to muscarinic signaling in the
CC regulation of autophagy (PubMed:17785524).
CC {ECO:0000269|PubMed:17785524, ECO:0000269|PubMed:19164535,
CC ECO:0000269|PubMed:27661253, ECO:0000269|PubMed:28087624}.
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:P53355};
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:P53355};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P53355};
CC -!- SUBUNIT: Interacts with ptrn-1. {ECO:0000269|PubMed:27661253}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:27661253}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:27661253}. Note=Exhibits
CC movement along microtubules. {ECO:0000269|PubMed:27661253}.
CC -!- TISSUE SPECIFICITY: Expressed in epidermis, muscles and neurons.
CC {ECO:0000269|PubMed:19164535}.
CC -!- DEVELOPMENTAL STAGE: Present from late embryogenesis onwards.
CC {ECO:0000269|PubMed:19164535}.
CC -!- DISRUPTION PHENOTYPE: Beginning in the L3 stage, animals display
CC striking and progressive defects in morphology of the epidermis and
CC cuticle in several body regions, particularly in the nose, tail, vulva,
CC and the dorsal midline in the region of the posterior pharyngeal bulb
CC (PubMed:19164535, PubMed:27661253). The cuticle in these regions
CC becomes up to 5-10 times thicker than the wild-type, at the expense of
CC underlying epidermis (PubMed:19164535, PubMed:27661253). Up-regulates
CC innate immune responses to damage (PubMed:19164535). Decreases
CC starvation-induced autophagy (PubMed:17785524). Disorganization and
CC hyper-stabilization of epidermal microtubules and reduced microtubule
CC growth rates (PubMed:27661253). Treatment with a microtubule
CC stabilizing drug, paclitaxel, results in enhanced epidermal morphology
CC defects (PubMed:27661253). In a ptrn-1 mutant background, suppression
CC of the epidermal morphology defects (PubMed:27661253).
CC {ECO:0000269|PubMed:17785524, ECO:0000269|PubMed:19164535,
CC ECO:0000269|PubMed:27661253}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. DAP kinase subfamily. {ECO:0000255}.
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DR EMBL; AY733040; AAW57534.1; -; mRNA.
DR EMBL; BX284601; CCD72943.1; -; Genomic_DNA.
DR PIR; T32930; T32930.
DR RefSeq; NP_490840.2; NM_058439.4.
DR AlphaFoldDB; O44997; -.
DR SMR; O44997; -.
DR BioGRID; 52023; 1.
DR STRING; 6239.K12C11.4; -.
DR EPD; O44997; -.
DR PaxDb; O44997; -.
DR PeptideAtlas; O44997; -.
DR EnsemblMetazoa; K12C11.4a.1; K12C11.4a.1; WBGene00003400.
DR GeneID; 187322; -.
DR KEGG; cel:CELE_K12C11.4; -.
DR UCSC; K12C11.4; c. elegans.
DR CTD; 187322; -.
DR WormBase; K12C11.4; CE40262; WBGene00003400; dapk-1.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_002849_2_0_1; -.
DR InParanoid; O44997; -.
DR OMA; RSMHDFQ; -.
DR OrthoDB; 67579at2759; -.
DR PhylomeDB; O44997; -.
DR PRO; PR:O44997; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003400; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; O44997; baseline and differential.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP 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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13857; Ank_5; 2.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 7.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51424; ROC; 1.
PE 1: Evidence at protein level;
KW ANK repeat; ATP-binding; Cytoplasm; Cytoskeleton; Developmental protein;
KW GTP-binding; Immunity; Innate immunity; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1425
FT /note="Death-associated protein kinase dapk-1"
FT /id="PRO_0000400089"
FT DOMAIN 28..289
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 392..421
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 425..454
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 458..487
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 491..520
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 524..553
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 557..586
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 590..619
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT REPEAT 623..652
FT /note="ANK 8"
FT /evidence="ECO:0000255"
FT DOMAIN 695..950
FT /note="Roc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT REPEAT 810..841
FT /note="ANK 9"
FT /evidence="ECO:0000255"
FT REPEAT 934..963
FT /note="ANK 10"
FT /evidence="ECO:0000255"
FT DOMAIN 1308..1389
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 34..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P53355,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P53355,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 57
FT /note="K->A: Normal localization and movement along
FT microtubules and no exhibition of epidermal morphology
FT defects."
FT /evidence="ECO:0000269|PubMed:27661253"
FT MUTAGEN 179
FT /note="S->L: In ju4; Causes severe epidermal morphology
FT defects, including progressive accumulation of the cuticle
FT and degeneration of the underlying epidermis, accelerated
FT wound closure, and disorganization and hyper-stabilization
FT of epidermal microtubules. Reduces microtubule growth
FT rates. Increased ptrn-1 filaments in the anterior lateral
FT epidermis. In L4 larvae and in adults, disrupts expression
FT of specific unc-44 mRNAs in L4 seam cells and in head and
FT tail epidermal cells. Reduces nuclear localization of pinn-
FT 1 in epidermal cells. Increases expression of antimicrobial
FT peptides. Epidermal defects are suppressed in an unc-44 or
FT ptrn-1 mutant background."
FT /evidence="ECO:0000269|PubMed:27661253,
FT ECO:0000269|PubMed:28087624"
SQ SEQUENCE 1425 AA; 158968 MW; 1118403F098DAFC5 CRC64;
MSDDVNSSAT STSSSTVHFD DTPFEDVYEI ETELGSGQFA VVRRVRDRKT GEKYAAKFIK
KRRYATSRRG VTRQNIEREV RVLQKIRGNS NVVELHAVYE TASDVIIVLE LVSGGELFDH
VCAKECLDEV EAAAFIKQIL LAVRHLHSLH IVHLDIKPEN VMLKQRGDSQ IKIIDFGLSR
EIEPGAVVKD MVGTPEFVAP EVVNYEALSP ATDMWAVGVV TYILLSGGSP FLGDNRDETF
SNITRVRYHF SDRYFKNTSK HAKDFIYRLF VRDVDQRATV EECLQHPWIR GPEGNAIDIR
KASCITISHI QSFKTRQRWK RCVELVMVLL KASKSSRRIG DGRFDEEDMV ASCTLICAEE
GNLRALHKLS ALHKLLPNAT RKSLKSSFSE PNGATAMHCA AKYGHAEVFN YFHMKGGNIC
ARDDNGDTPL HVACRFAQHT VAGYVANEKI DVDSINKTGE TALHCAVESA DTRVVRLLLQ
LRPRLDLPNA SGDTVLHLAA DSINPRIVPL LVCLAPPLHL RNIREETPLH VAAARGHVDC
VQALLDANSP IDAVEQDGKT ALIIALENGN VDIASILITN GCDINHADHH GDTALHIASK
HGLLQAVQTL CHCAVTVDSV NANKKTALHL AAHYGHVDII RVLLLARADV TLRGDDGLTA
ELVAVAAERL EAHSLLKMVK SQEIREEYIS QLYPLDTSLR RIKLKLLGHS QSGKTRLVQT
LHSSRGISSF LESVTRRISD HYSPSSSMKD DGIHSTNGSF VSESNNNSSF DLAAAAGSKY
APPHSQYTRG IDVQTVNING CGEFSVWEFG GYEPMHTCYD HFVGNADCIH LILYRTSDPT
EVQYKQILYW MNFLKGRVTP FEPIGHCGFS SRRSKVIIVG THATSSLFPQ MNQEGEYVSS
DIEAMLNTVR LRFETHFDMD HRLILLDATN PSCIGMKTLK MELAKCRTNI LAKLLKPLAI
LDTVVNHLNL VRKKHANFPV ITWPDFIQLV RNEINPLTGD AHCRQIVQQL QLIGELVYLR
NDLCDADYVV LNAEWFGTHI LGQLLSAEFL SKASPNGSYH TSSLAKIFPE IPEQSDLMTI
LEVLQLCAPD ARTGAHEFPV FIQTEAPDSI WRPYSLKEKE RDTVYGGVRI LPMRGMERSL
HSTFPRIQVA LRRSINDYQP AKDTQLHQWS ECSKLVSQDR EAVIRMVGDA VEIRARGPSE
SATSMFYFME DLINLVEHAA AEVGPGISLE RHFISPKHLK EHREHPALFP PESMMEMQQR
ESLSVKGTQD EEELFTDVVC FGSRDVARHL TLGIDVGVAD LQMASRCELA CLLDPPHAMG
RDWSILAVKL QLTDQVPDVD STGQSLSRTD QLLNEWAIHH PEQASVGNLC RILVELGRCD
ARDALYRTVP LYVFAPLEDQ FLLETNDSGV VSSCHSSSEH NPINI
