SEK1_CAEEL
ID SEK1_CAEEL Reviewed; 336 AA.
AC G5EDF7;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Dual specificity mitogen-activated protein kinase kinase sek-1 {ECO:0000305|PubMed:11751572};
DE Short=MAP kinase kinase sek-1 {ECO:0000305};
DE EC=2.7.12.2 {ECO:0000269|PubMed:11751572};
GN Name=sek-1 {ECO:0000312|WormBase:R03G5.2};
GN ORFNames=R03G5.2 {ECO:0000312|WormBase:R03G5.2};
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:0000312|EMBL:BAB43977.2}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, INTERACTION WITH NSY-1, PHOSPHORYLATION AT SER-204 AND
RP THR-208, AND MUTAGENESIS OF LYS-79; SER-204 AND THR-208.
RX PubMed=11751572; DOI=10.1093/embo-reports/kvf001;
RA Tanaka-Hino M., Sagasti A., Hisamoto N., Kawasaki M., Nakano S.,
RA Ninomiya-Tsuji J., Bargmann C.I., Matsumoto K.;
RT "SEK-1 MAPKK mediates Ca2+ signaling to determine neuronal asymmetric
RT development in Caenorhabditis elegans.";
RL EMBO Rep. 3:56-62(2002).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF GLY-212.
RX PubMed=12142542; DOI=10.1126/science.1073759;
RA Kim D.H., Feinbaum R., Alloing G., Emerson F.E., Garsin D.A., Inoue H.,
RA Tanaka-Hino M., Hisamoto N., Matsumoto K., Tan M.-W., Ausubel F.M.;
RT "A conserved p38 MAP kinase pathway in Caenorhabditis elegans innate
RT immunity.";
RL Science 297:623-626(2002).
RN [3] {ECO:0000312|EMBL:BAC11708.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Matsumoto K., Kawasaki M., Hisamoto N., Tanaka M.;
RT "MAP kinase kinase.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [4] {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).
RN [5]
RP INTERACTION WITH UNC-16.
RX PubMed=11738026; DOI=10.1016/s0896-6273(01)00532-3;
RA Byrd D.T., Kawasaki M., Walcoff M., Hisamoto N., Matsumoto K., Jin Y.;
RT "UNC-16, a JNK-signaling scaffold protein, regulates vesicle transport in
RT C. elegans.";
RL Neuron 32:787-800(2001).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=15256590; DOI=10.1073/pnas.0404073101;
RA Huffman D.L., Abrami L., Sasik R., Corbeil J., van der Goot F.G.,
RA Aroian R.V.;
RT "Mitogen-activated protein kinase pathways defend against bacterial pore-
RT forming toxins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10995-11000(2004).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=16166371; DOI=10.1101/gad.1324805;
RA Inoue H., Hisamoto N., An J.H., Oliveira R.P., Nishida E., Blackwell T.K.,
RA Matsumoto K.;
RT "The C. elegans p38 MAPK pathway regulates nuclear localization of the
RT transcription factor SKN-1 in oxidative stress response.";
RL Genes Dev. 19:2278-2283(2005).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=15888317; DOI=10.1016/j.mad.2004.11.012;
RA Kondo M., Yanase S., Ishii T., Hartman P.S., Matsumoto K., Ishii N.;
RT "The p38 signal transduction pathway participates in the oxidative stress-
RT mediated translocation of DAF-16 to Caenorhabditis elegans nuclei.";
RL Mech. Ageing Dev. 126:642-647(2005).
RN [9] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16729024; DOI=10.1038/sj.cdd.4401976;
RA Salinas L.S., Maldonado E., Navarro R.E.;
RT "Stress-induced germ cell apoptosis by a p53 independent pathway in
RT Caenorhabditis elegans.";
RL Cell Death Differ. 13:2129-2139(2006).
RN [10] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLY-212.
RX PubMed=18394898; DOI=10.1016/j.cub.2008.02.079;
RA Pujol N., Cypowyj S., Ziegler K., Millet A., Astrain A., Goncharov A.,
RA Jin Y., Chisholm A.D., Ewbank J.J.;
RT "Distinct innate immune responses to infection and wounding in the C.
RT elegans epidermis.";
RL Curr. Biol. 18:481-489(2008).
RN [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=19497412; DOI=10.1016/j.cbi.2009.03.012;
RA Wang S., Wu L., Wang Y., Luo X., Lu Y.;
RT "Copper-induced germline apoptosis in Caenorhabditis elegans: the
RT independent roles of DNA damage response signaling and the dependent roles
RT of MAPK cascades.";
RL Chem. Biol. Interact. 180:151-157(2009).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF GLY-212.
RX PubMed=20062796; DOI=10.1371/journal.ppat.1000717;
RA Butschi A., Titz A., Waelti M.A., Olieric V., Paschinger K., Noebauer K.,
RA Guo X., Seeberger P.H., Wilson I.B., Aebi M., Hengartner M.O., Kuenzler M.;
RT "Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity
RT towards nematotoxic fungal galectin CGL2.";
RL PLoS Pathog. 6:E1000717-E1000717(2010).
RN [13]
RP FUNCTION.
RX PubMed=21212236; DOI=10.1534/genetics.110.124883;
RA Hayakawa T., Kato K., Hayakawa R., Hisamoto N., Matsumoto K., Takeda K.,
RA Ichijo H.;
RT "Regulation of anoxic death in Caenorhabditis elegans by mammalian
RT apoptosis signal-regulating kinase (ASK) family proteins.";
RL Genetics 187:785-792(2011).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-212.
RX PubMed=22216003; DOI=10.1371/journal.ppat.1002453;
RA Hoeven R.V., McCallum K.C., Cruz M.R., Garsin D.A.;
RT "Ce-Duox1/BLI-3 generated reactive oxygen species trigger protective SKN-1
RT activity via p38 MAPK signaling during infection in C. elegans.";
RL PLoS Pathog. 7:E1002453-E1002453(2011).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22308034; DOI=10.1074/jbc.m111.314146;
RA Lee K., Shim J., Bae J., Kim Y.J., Lee J.;
RT "Stabilization of RNT-1 protein, runt-related transcription factor (RUNX)
RT protein homolog of Caenorhabditis elegans, by oxidative stress through
RT mitogen-activated protein kinase pathway.";
RL J. Biol. Chem. 287:10444-10452(2012).
RN [16]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-212.
RX PubMed=22363008; DOI=10.1126/science.1215156;
RA Blum E.S., Abraham M.C., Yoshimura S., Lu Y., Shaham S.;
RT "Control of nonapoptotic developmental cell death in Caenorhabditis elegans
RT by a polyglutamine-repeat protein.";
RL Science 335:970-973(2012).
CC -!- FUNCTION: Dual specificity protein kinase which acts as an essential
CC component of the p38 signal transduction pathway which is also composed
CC of upstream effector nsy-1 and downstream effector pmk-1
CC (PubMed:11751572). May phosphorylate pmk-1 (PubMed:12142542,
CC PubMed:16166371). Downstream of CaMKII unc-43 and adapter protein tir-
CC 1, plays a role in determining asymmetric cell fates in olfactory AWC
CC neurons during neuronal development. Activation results in the
CC repression of odorant receptor str-2 expression in one of the 2 AWC
CC neurons (PubMed:11751572, PubMed:12142542). Involved in resistance to
CC pathogenic Gram-positive and Gram-negative bacterial and fungal
CC infection (PubMed:12142542, PubMed:18394898, PubMed:22216003). Involved
CC in resistance to the nematotoxic C.cinerea galectin Cgl2
CC (PubMed:20062796). Probably by promoting pmk-1-mediated activation of
CC skn-1, involved in the up-regulation of gcs-1 and glutathione-S-
CC transferase gst-4 expression upon bacterial infection
CC (PubMed:22216003). Probably downstream of tir-1, required for the
CC expression of antimicrobial peptide nlp-29 in the epidermis in response
CC to fungal infection or physical injury (PubMed:18394898,
CC PubMed:22308034). Regulates susceptibility of B.thuringiensis pore-
CC forming toxin Cry5B and Cry21A (PubMed:15256590). Involved in the
CC response to oxidative stress (PubMed:15888317, PubMed:22308034). May
CC regulate transcription factor daf-16 localization during oxidative
CC stress (PubMed:15888317). By phosphorylating pmk-1, regulates skn-1
CC localization during oxidative stress (PubMed:16166371). By
CC phosphorylating and activating pmk-1, plays a role in the stabilization
CC of transcription factor rnt-1 in the intestine during oxidative stress
CC (PubMed:22308034). Up-regulates expression of gcs-1 in intestine upon
CC arsenite treatment (PubMed:16166371). Regulates germline proliferation
CC in response to osmotic stress, starvation and germline apoptosis
CC induced by heavy metals, such as Cu(2+) (PubMed:16729024,
CC PubMed:19497412). In association with mek-1, regulates germline cell
CC apoptosis in response to oxidative, osmotic and heat shock stresses
CC (PubMed:16729024). Plays a role downstream of tir-1/nsy-1 in regulating
CC susceptibility to anoxia (PubMed:21212236). In males, by regulating
CC pqn-41 expression, involved in non-apoptotic death of the linker cell
CC which guides gonad elongation during larval development
CC (PubMed:22363008). Involved in egg laying (PubMed:12142542).
CC {ECO:0000269|PubMed:11751572, ECO:0000269|PubMed:12142542,
CC ECO:0000269|PubMed:15256590, ECO:0000269|PubMed:15888317,
CC ECO:0000269|PubMed:16166371, ECO:0000269|PubMed:16729024,
CC ECO:0000269|PubMed:18394898, ECO:0000269|PubMed:19497412,
CC ECO:0000269|PubMed:20062796, ECO:0000269|PubMed:21212236,
CC ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:22308034,
CC ECO:0000269|PubMed:22363008}.
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=2.7.12.2;
CC Evidence={ECO:0000269|PubMed:11751572};
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=2.7.12.2; Evidence={ECO:0000269|PubMed:11751572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC Evidence={ECO:0000269|PubMed:11751572};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11751572};
CC -!- ACTIVITY REGULATION: Activated by nsy-1-mediated phosphorylation.
CC {ECO:0000269|PubMed:11751572}.
CC -!- SUBUNIT: Interacts with nsy-1 (PubMed:11751572). Interacts with unc-16
CC (PubMed:11738026). {ECO:0000269|PubMed:11738026,
CC ECO:0000269|PubMed:11751572}.
CC -!- TISSUE SPECIFICITY: Expressed in linker cell in males.
CC {ECO:0000269|PubMed:22363008}.
CC -!- INDUCTION: By B.thuringiensis pore-forming toxin Cry5B.
CC {ECO:0000269|PubMed:15256590}.
CC -!- DISRUPTION PHENOTYPE: Upon infection by P.aeruginosa and E.faecalis,
CC RNAi-mediated knockdown results in a reduced up-regulation of gst-4 and
CC gcs-1 expression (PubMed:22216003). Causes a severe reduction in rnt-1
CC accumulation in the intestine during oxidative stress mediated by
CC paraquat (PubMed:22308034). RNAi-mediated knockdown in a ced-1 mutant
CC background causes a moderate reduction in germline cell apoptosis
CC during oogenesis in response to oxidative and heat shock stresses. The
CC phenotype is more severe and also affects the response to osmotic
CC stress in a mek-1 and ced-1 mutant background (PubMed:16729024).
CC {ECO:0000269|PubMed:16729024, ECO:0000269|PubMed:22216003,
CC ECO:0000269|PubMed:22308034}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; AB060731; BAB43977.2; -; mRNA.
DR EMBL; AB024087; BAC11708.1; -; mRNA.
DR EMBL; BX284606; CCD68028.1; -; Genomic_DNA.
DR PIR; T16665; T16665.
DR RefSeq; NP_509322.2; NM_076921.4.
DR AlphaFoldDB; G5EDF7; -.
DR SMR; G5EDF7; -.
DR IntAct; G5EDF7; 4.
DR STRING; 6239.R03G5.2.2; -.
DR iPTMnet; G5EDF7; -.
DR EPD; G5EDF7; -.
DR PaxDb; G5EDF7; -.
DR PeptideAtlas; G5EDF7; -.
DR EnsemblMetazoa; R03G5.2.1; R03G5.2.1; WBGene00004758.
DR GeneID; 181043; -.
DR KEGG; cel:CELE_R03G5.2; -.
DR CTD; 181043; -.
DR WormBase; R03G5.2; CE31210; WBGene00004758; sek-1.
DR eggNOG; KOG0984; Eukaryota.
DR GeneTree; ENSGT00940000168458; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; G5EDF7; -.
DR OMA; HAYKIGK; -.
DR OrthoDB; 688282at2759; -.
DR PhylomeDB; G5EDF7; -.
DR Reactome; R-CEL-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-CEL-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-CEL-6811555; PI5P Regulates TP53 Acetylation.
DR SignaLink; G5EDF7; -.
DR PRO; PR:G5EDF7; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004758; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:WormBase.
DR GO; GO:0106310; F:protein serine kinase activity; IGI:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0035545; P:determination of left/right asymmetry in nervous system; IMP:WormBase.
DR GO; GO:0045087; P:innate immune response; IMP:WormBase.
DR GO; GO:0000165; P:MAPK cascade; IGI:WormBase.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:ParkinsonsUK-UCL.
DR GO; GO:0038066; P:p38MAPK cascade; IMP:WormBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IGI:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1901046; P:positive regulation of oviposition; IMP:WormBase.
DR GO; GO:1902097; P:positive regulation of transcription from RNA polymerase II promoter involved in defense response to Gram-negative bacterium; IMP:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR GO; GO:0093002; P:response to nematicide; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:WormBase.
DR GO; GO:0000303; P:response to superoxide; IMP:WormBase.
DR GO; GO:0009636; P:response to toxic substance; IMP:UniProtKB.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IMP:WormBase.
DR GO; GO:0034607; P:turning behavior involved in mating; IMP:WormBase.
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; Kinase; Magnesium; Metal-binding; Neurogenesis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Stress response; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..336
FT /note="Dual specificity mitogen-activated protein kinase
FT kinase sek-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433601"
FT DOMAIN 50..311
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 56..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11751572"
FT MOD_RES 208
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11751572"
FT MUTAGEN 79
FT /note="K->R: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:11751572"
FT MUTAGEN 204
FT /note="S->D: Phosphomimetic mutant which likely results in
FT constitutive activation. Loss of str-2 expression in either
FT of the AWC neurons; when associated with D-208."
FT /evidence="ECO:0000269|PubMed:11751572"
FT MUTAGEN 208
FT /note="T->D: Phosphomimetic mutant which likely results in
FT constitutive activation. Loss of str-2 expression in either
FT of the AWC neurons; when associated with D-204."
FT /evidence="ECO:0000269|PubMed:11751572"
FT MUTAGEN 212
FT /note="G->R: In ag1; loss of pmk-1 phosphorylation. Upon
FT pathogenic bacterial infection, decrease in survival rate
FT and severe loss of gst-4 and gsc-1 expression. Loss of nlp-
FT 29 expression in response to fungal infection. Moderate
FT decrease in survival rate upon C.cinerea galectin Cgl2
FT exposure. Promotes linker cell survival in 53 percent of
FT animals. Egg-laying defect. Normal development and
FT lifespan."
FT /evidence="ECO:0000269|PubMed:12142542,
FT ECO:0000269|PubMed:18394898, ECO:0000269|PubMed:20062796,
FT ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:22363008"
SQ SEQUENCE 336 AA; 38700 MW; 5E5E4EF1CC374FA0 CRC64;
MERKGRERKL PGMKIVMPTP VETPTMNLED RCLIKLTNES EEIEIAATDL VVLEELGKGG
YGIVEKMQHR QSGIIMAVKR IKSSINDQSQ KQMLNELDAC RRSDCCPQMV RFYGAMFREG
DVWICMEVMD TSLDKFYRHA YKIGKHIPEP FIGKMALSVI EGLNFMKEQL NLIHRDVKPS
NILLNRHGQV KICDFGISGH LTNSMAKTVQ AGCKPYMPPE RIDGETKSAY DVRADVWSLG
ITIIEIAVGT HPYANWKTPF EQLKQVVKEP PPKLPMESGF SVDCQYFVKR CLEKDYNERP
KYPELLAMPF MEQARNEKQF SMARFINEIL DTVWRR
