SKN1_CAEEL
ID SKN1_CAEEL Reviewed; 623 AA.
AC P34707; Q8MPW2; Q8MPW3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Protein skinhead-1;
GN Name=skn-1; ORFNames=T19E7.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-623 (ISOFORM A), FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=1547503; DOI=10.1016/0092-8674(92)90078-q;
RA Bowerman B., Eaton B.A., Priess J.R.;
RT "skn-1, a maternally expressed gene required to specify the fate of ventral
RT blastomeres in the early C. elegans embryo.";
RL Cell 68:1061-1075(1992).
RN [3]
RP SUBUNIT, SUBCELLULAR LOCATION, AND DNA-BINDING.
RX PubMed=7939715; DOI=10.1126/science.7939715;
RA Blackwell T.K., Bowerman B., Priess J.R., Weintraub H.;
RT "Formation of a monomeric DNA binding domain by Skn-1 bZIP and homeodomain
RT elements.";
RL Science 266:621-628(1994).
RN [4]
RP FUNCTION.
RX PubMed=11463373; DOI=10.1016/s1097-2765(01)00195-2;
RA Maduro M.F., Meneghini M.D., Bowerman B., Broitman-Maduro G., Rothman J.H.;
RT "Restriction of mesendoderm to a single blastomere by the combined action
RT of SKN-1 and a GSK-3beta homolog is mediated by MED-1 and -2 in C.
RT elegans.";
RL Mol. Cell 7:475-485(2001).
RN [5]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-164 AND SER-430, AND
RP MUTAGENESIS OF SER-164 AND SER-430.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20624915; DOI=10.1074/jbc.m110.146274;
RA Okuyama T., Inoue H., Ookuma S., Satoh T., Kano K., Honjoh S., Hisamoto N.,
RA Matsumoto K., Nishida E.;
RT "The ERK-MAPK pathway regulates longevity through SKN-1 and insulin-like
RT signaling in Caenorhabditis elegans.";
RL J. Biol. Chem. 285:30274-30281(2010).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [8] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 240-ARG--ILE-623.
RX PubMed=22568582; DOI=10.1111/j.1474-9726.2012.00831.x;
RA Rizki G., Picard C.L., Pereyra C., Lee S.S.;
RT "Host cell factor 1 inhibits SKN-1 to modulate oxidative stress responses
RT in Caenorhabditis elegans.";
RL Aging Cell 11:717-721(2012).
RN [9]
RP FUNCTION, INTERACTION WITH PGAM-5 AND MXL-3, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLU-237 AND SER-245.
RX PubMed=23040073; DOI=10.1016/j.cmet.2012.09.007;
RA Paek J., Lo J.Y., Narasimhan S.D., Nguyen T.N., Glover-Cutter K.,
RA Robida-Stubbs S., Suzuki T., Yamamoto M., Blackwell T.K., Curran S.P.;
RT "Mitochondrial SKN-1/Nrf mediates a conserved starvation response.";
RL Cell Metab. 16:526-537(2012).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23106139; DOI=10.1111/jnc.12072;
RA VanDuyn N., Settivari R., LeVora J., Zhou S., Unrine J., Nass R.;
RT "The metal transporter SMF-3/DMT-1 mediates aluminum-induced dopamine
RT neuron degeneration.";
RL J. Neurochem. 124:147-157(2013).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23721876; DOI=10.1016/j.neuro.2013.05.014;
RA Settivari R., VanDuyn N., LeVora J., Nass R.;
RT "The Nrf2/SKN-1-dependent glutathione S-transferase pi homologue GST-1
RT inhibits dopamine neuron degeneration in a Caenorhabditis elegans model of
RT manganism.";
RL NeuroToxicology 38:51-60(2013).
RN [12]
RP FUNCTION.
RX PubMed=24385935; DOI=10.1371/journal.pgen.1004063;
RA Ghose P., Park E.C., Tabakin A., Salazar-Vasquez N., Rongo C.;
RT "Anoxia-reoxygenation regulates mitochondrial dynamics through the hypoxia
RT response pathway, SKN-1/Nrf, and stomatin-like protein STL-1/SLP-2.";
RL PLoS Genet. 9:E1004063-E1004063(2013).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25688864; DOI=10.1371/journal.pone.0117444;
RA Mendes T.K., Novakovic S., Raymant G., Bertram S.E., Esmaillie R.,
RA Nadarajan S., Breugelmans B., Hofmann A., Gasser R.B., Colaiacovo M.P.,
RA Boag P.R.;
RT "Investigating the role of RIO protein kinases in Caenorhabditis elegans.";
RL PLoS ONE 10:E0117444-E0117444(2015).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27528192; DOI=10.7554/elife.17721;
RA Lehrbach N.J., Ruvkun G.;
RT "Proteasome dysfunction triggers activation of SKN-1A/Nrf1 by the aspartic
RT protease DDI-1.";
RL Elife 5:0-0(2016).
RN [15]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-164 AND
RP SER-430, AND MUTAGENESIS OF SER-164 AND SER-430.
RX PubMed=26920757; DOI=10.1534/genetics.115.185272;
RA McCallum K.C., Liu B., Fierro-Gonzalez J.C., Swoboda P., Arur S.,
RA Miranda-Vizuete A., Garsin D.A.;
RT "TRX-1 Regulates SKN-1 Nuclear Localization Cell Non-autonomously in
RT Caenorhabditis elegans.";
RL Genetics 203:387-402(2016).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION (ISOFORMS B AND C), AND MUTAGENESIS OF
RP 553-GLN--ILE-623.
RX PubMed=34407394; DOI=10.1016/j.celrep.2021.109529;
RA Wu C., Karakuzu O., Garsin D.A.;
RT "Tribbles pseudokinase NIPI-3 regulates intestinal immunity in
RT Caenorhabditis elegans by controlling SKN-1/Nrf activity.";
RL Cell Rep. 36:109529-109529(2021).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 540-623.
RX PubMed=9628487; DOI=10.1038/nsb0698-484;
RA Rupert P.B., Daughdrill G.W., Bowerman B., Matthews B.W.;
RT "A new DNA-binding motif in the Skn-1 binding domain-DNA complex.";
RL Nat. Struct. Biol. 5:484-491(1998).
CC -!- FUNCTION: Transcription factor required to specify the fate of ventral
CC blastomeres in the early embryo, and postembryonically for the
CC development of the intestine (PubMed:1547503). Directly regulates
CC expression of zygotically expressed med-1 and med-2 to direct
CC mesendoderm development (PubMed:1547503, PubMed:11463373). Required for
CC stl-1 mRNA up-regulation in response to oxidative stress and anoxia
CC (PubMed:24385935). Involved in regulating innate immunity, acting
CC downstream of the pmk-1 p38/MAPK pathway and probably also downstream
CC of nipi-3 (PubMed:34407394). Required for the up-regulation of gcs-1
CC and several glutathione-S-transferase mRNAs in response to oxidative
CC stress generated during pathogenic bacterial infection
CC (PubMed:22216003). Modulates oxidative stress responses in concert with
CC transcriptional coregulator hcf-1 (PubMed:22568582). Regulates the
CC transcription of genes associated with metabolism in response to
CC changes in nutrient availability (PubMed:23040073). In neurons,
CC involved in mitochondrial fusion and behavioral recovery during
CC reoxygenation (PubMed:24385935). Required for riok-1 mRNA expression in
CC the intestine (PubMed:25688864). Downstream of the let-60/Ras, mek-2
CC and pmk-1 pathway, positively regulates lifespan probably by preventing
CC transcription of insulin-like peptides such as ins-39
CC (PubMed:20624915). Prevents degeneration of dopaminergic CEP neurons in
CC response to high Al(3+) or Mn(2+) levels, probably by promoting the
CC expression of glutathione-S-transferase gst-1 (PubMed:23106139,
CC PubMed:23721876). {ECO:0000269|PubMed:11463373,
CC ECO:0000269|PubMed:1547503, ECO:0000269|PubMed:20624915,
CC ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:22568582,
CC ECO:0000269|PubMed:23040073, ECO:0000269|PubMed:23106139,
CC ECO:0000269|PubMed:23721876, ECO:0000269|PubMed:24385935,
CC ECO:0000269|PubMed:25688864}.
CC -!- FUNCTION: [Isoform a]: Directed by the ER-associated degradation
CC pathway (ERAD), mediates proteasomal homeostasis by regulating the
CC expression of proteasomal subunits such as rpt-3 to confer resistance
CC to proteasomal dysfunction. {ECO:0000269|PubMed:27528192}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7939715}.
CC -!- SUBUNIT: [Isoform a]: Interacts with pgma-5 (PubMed:23040073).
CC Interacts with transcription factor mxl-3 (via N-terminus)
CC (PubMed:23040073). {ECO:0000269|PubMed:23040073}.
CC -!- SUBUNIT: [Isoform c]: Interacts with pgma-5 (PubMed:23040073).
CC Interacts with transcription factor mxl-3 (via N-terminus)
CC (PubMed:23040073). {ECO:0000269|PubMed:23040073}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16166371,
CC ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:26920757,
CC ECO:0000269|PubMed:7939715}. Cytoplasm {ECO:0000269|PubMed:16166371,
CC ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:26920757}. Note=In
CC absence of stress, localizes in the cytoplasm of intestinal cells
CC (PubMed:16166371, PubMed:22216003, PubMed:26920757). Upon paraquat or
CC arsenite treatments or upon bacterial infection, localizes in the
CC nucleus (PubMed:16166371, PubMed:22216003, PubMed:26920757). Nuclear
CC localization is regulated by pmk-1-mediated phosphorylation
CC (PubMed:16166371, PubMed:26920757). Nuclear localization is regulated
CC by transcriptional coregulator hcf-1. {ECO:0000269|PubMed:16166371,
CC ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:22568582,
CC ECO:0000269|PubMed:26920757}.
CC -!- SUBCELLULAR LOCATION: [Isoform a]: Nucleus
CC {ECO:0000269|PubMed:27528192}. Mitochondrion
CC {ECO:0000269|PubMed:23040073}. Note=Localizes to the nucleus in
CC response to proteasomal dysfunction. {ECO:0000269|PubMed:27528192}.
CC -!- SUBCELLULAR LOCATION: [Isoform b]: Nucleus
CC {ECO:0000269|PubMed:34407394}. Note=Localizes to the nucleus in
CC response to pathogenic bacteria such as P.aeruginosa or E.faecalis, in
CC a nipi-3-dependent manner. {ECO:0000269|PubMed:34407394}.
CC -!- SUBCELLULAR LOCATION: [Isoform c]: Nucleus
CC {ECO:0000269|PubMed:34407394}. Note=Localizes to the nucleus in
CC response to pathogenic bacteria such as P.aeruginosa or E.faecalis, in
CC a nipi-3-dependent manner. {ECO:0000269|PubMed:34407394}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=P34707-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P34707-2; Sequence=VSP_011488, VSP_011489;
CC Name=c;
CC IsoId=P34707-3; Sequence=VSP_011487;
CC -!- TISSUE SPECIFICITY: Postembryonic intestinal cells.
CC {ECO:0000269|PubMed:1547503, ECO:0000269|PubMed:26920757}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:1547503}.
CC -!- DOMAIN: Alternative DNA-binding strategy due to lack of a leucine
CC zipper dimerization segment: DNA binding domain binds to its cognate
CC half-site, an N-terminal arm recognizes adjacent 5' AT-rich sequences
CC in the minor groove and the intervening residues stabilize interactions
CC of these two subdomains with DNA. {ECO:0000269|PubMed:9628487}.
CC -!- PTM: [Isoform a]: Cleaved by the aspartic protease ddi-1.
CC {ECO:0000269|PubMed:27528192}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown of all isoforms results
CC in a severe reduction in transcription of gst-4, gst-5, gst-7 and gcs-1
CC mRNAs during infection by P.aeruginosa or P.faecalis (PubMed:22216003).
CC Susceptibility to P.aeruginosa and P.faecalis is characterized by a
CC decrease in survival rate (PubMed:22216003).
CC {ECO:0000269|PubMed:22216003}.
CC -!- DISRUPTION PHENOTYPE: [Isoform a]: Viable, but there is failed
CC activation of the expression of the proteasomal subunit rpt-3 in all
CC tissues (PubMed:27528192). Treatment with the proteasome inhibitor
CC bortezomib or knockout with rpn-10 RNAi results in larval lethality
CC (PubMed:27528192). Double knockout with pbs-5 results in failed
CC expression the proteasomal subunit rpt-3 (PubMed:27528192). Also causes
CC a loss of transcription of riok-1 mRNA in intestine (PubMed:25688864).
CC Reduces life span (PubMed:20624915). Moderate increase in transcription
CC of ins-39 mRNA (PubMed:20624915). Moderate increase in CEP neuron death
CC in response to high Al(3+) levels (PubMed:23106139). RNAi-mediated
CC knockdown causes an increase in Mn(2+)-mediated dopaminergic CEP neuron
CC degeneration and a reduction in expression levels of glutathione S-
CC transferase gst-1 (PubMed:23721876). {ECO:0000269|PubMed:20624915,
CC ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:23106139,
CC ECO:0000269|PubMed:23721876, ECO:0000269|PubMed:25688864,
CC ECO:0000269|PubMed:27528192}.
CC -!- SIMILARITY: Belongs to the bZIP family. Skn1 subfamily. {ECO:0000305}.
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DR EMBL; BX284604; CCD62212.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD62213.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD62214.1; -; Genomic_DNA.
DR EMBL; M84359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A42143; A42143.
DR PIR; F88694; F88694.
DR RefSeq; NP_741404.1; NM_171345.4. [P34707-1]
DR RefSeq; NP_741405.1; NM_171346.3.
DR RefSeq; NP_741406.1; NM_171347.5. [P34707-2]
DR PDB; 1SKN; X-ray; 2.50 A; P=540-623.
DR PDBsum; 1SKN; -.
DR AlphaFoldDB; P34707; -.
DR SMR; P34707; -.
DR BioGRID; 42465; 25.
DR IntAct; P34707; 5.
DR STRING; 6239.T19E7.2a; -.
DR BindingDB; P34707; -.
DR ChEMBL; CHEMBL2146298; -.
DR iPTMnet; P34707; -.
DR PaxDb; P34707; -.
DR EnsemblMetazoa; T19E7.2a.1; T19E7.2a.1; WBGene00004804. [P34707-1]
DR EnsemblMetazoa; T19E7.2b.1; T19E7.2b.1; WBGene00004804. [P34707-2]
DR EnsemblMetazoa; T19E7.2c.1; T19E7.2c.1; WBGene00004804. [P34707-3]
DR GeneID; 177343; -.
DR KEGG; cel:CELE_T19E7.2; -.
DR UCSC; T19E7.2b; c. elegans. [P34707-1]
DR CTD; 177343; -.
DR WormBase; T19E7.2a; CE27591; WBGene00004804; skn-1. [P34707-1]
DR WormBase; T19E7.2b; CE31238; WBGene00004804; skn-1. [P34707-2]
DR WormBase; T19E7.2c; CE31239; WBGene00004804; skn-1. [P34707-3]
DR eggNOG; KOG3863; Eukaryota.
DR InParanoid; P34707; -.
DR OMA; TERPRAH; -.
DR OrthoDB; 1636216at2759; -.
DR Reactome; R-CEL-8951664; Neddylation.
DR Reactome; R-CEL-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-CEL-9759194; Nuclear events mediated by NFE2L2.
DR Reactome; R-CEL-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P34707; -.
DR EvolutionaryTrace; P34707; -.
DR PRO; PR:P34707; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004804; Expressed in pharyngeal muscle cell (C elegans) and 5 other tissues.
DR ExpressionAtlas; P34707; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:WormBase.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:WormBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0001708; P:cell fate specification; IMP:WormBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0048565; P:digestive tract development; IMP:UniProtKB.
DR GO; GO:0048566; P:embryonic digestive tract development; IMP:UniProtKB.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:WormBase.
DR GO; GO:0001714; P:endodermal cell fate specification; IMP:UniProtKB.
DR GO; GO:0048382; P:mesendoderm development; IMP:WormBase.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:UniProtKB.
DR GO; GO:1905804; P:positive regulation of cellular response to manganese ion; IMP:UniProtKB.
DR GO; GO:1900409; P:positive regulation of cellular response to oxidative stress; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IMP:WormBase.
DR GO; GO:0006990; P:positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response; IMP:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0009408; P:response to heat; IEP:WormBase.
DR GO; GO:0006979; P:response to oxidative stress; IEP:WormBase.
DR GO; GO:1901562; P:response to paraquat; IGI:UniProtKB.
DR GO; GO:0000303; P:response to superoxide; IMP:WormBase.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR Pfam; PF03131; bZIP_Maf; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cytoplasm;
KW Developmental protein; DNA-binding; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation; Translation regulation.
FT CHAIN 1..623
FT /note="Protein skinhead-1"
FT /id="PRO_0000076639"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..623
FT /note="Basic motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 10..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 164
FT /note="Phosphoserine; by pmk-1"
FT /evidence="ECO:0000269|PubMed:16166371,
FT ECO:0000269|PubMed:26920757"
FT MOD_RES 430
FT /note="Phosphoserine; by pmk-1"
FT /evidence="ECO:0000269|PubMed:16166371,
FT ECO:0000269|PubMed:26920757"
FT VAR_SEQ 1..313
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_011488"
FT VAR_SEQ 1..90
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_011487"
FT VAR_SEQ 314..389
FT /note="FDNKQQHPVINNVSLSEGIVYNQANLTEMQEMRDSCNQVSISTIPTTSTAQP
FT ETLFNVTDSQTVEQWLPTEVVPND -> MSLPSDFASSLLASSTTTNTTNTAPAAVNSF
FT DEQEEESKKILNMYLQMFNQQQVDQHGHHHQHPYAYSGVSSTFDR (in isoform
FT b)"
FT /evidence="ECO:0000305"
FT /id="VSP_011489"
FT MUTAGEN 164
FT /note="S->A: Abolishes phosphorylation by pmk-1. Loss of
FT nuclear translocation and increased susceptibility in
FT response to arsenite treatment; when associated with A-430.
FT Loss of nuclear translocation in a trx-1(ok1449) mutant
FT background; when associated with A-430."
FT /evidence="ECO:0000269|PubMed:16166371,
FT ECO:0000269|PubMed:26920757"
FT MUTAGEN 237
FT /note="E->K: In lax188; small body size, transcriptional
FT up-regulation of genes related to metabolism and adaptation
FT to starvation, increased length of the reproductive period
FT and slower growth recovery following starvation-induced
FT arrest at the L1 larval stage."
FT /evidence="ECO:0000269|PubMed:23040073"
FT MUTAGEN 240..623
FT /note="Missing: In zu67; abolishes induction of gcs-1, gst-
FT 4 and gst-7 in combination with RNAi-mediated knockdown of
FT hcf-1."
FT /evidence="ECO:0000269|PubMed:22568582"
FT MUTAGEN 245
FT /note="S->L: In lax120; small body size, transcriptional
FT up-regulation of genes related to metabolism and adaptation
FT to starvation, increased length of the reproductive period
FT and slower growth recovery following starvation-induced
FT arrest at the L1 larval stage."
FT /evidence="ECO:0000269|PubMed:23040073"
FT MUTAGEN 430
FT /note="S->A: Abolishes phosphorylation by pmk-1. Loss of
FT nuclear translocation and increased susceptibility in
FT response to arsenite treatment; when associated with A-164.
FT Loss of nuclear translocation in a trx-1(ok1449) mutant
FT background; when associated with A-164."
FT /evidence="ECO:0000269|PubMed:16166371,
FT ECO:0000269|PubMed:26920757"
FT MUTAGEN 553..623
FT /note="Missing: In zu135; susceptibility to P.aeruginosa or
FT E.faecalis is characterized by a decrease in survival
FT rate."
FT /evidence="ECO:0000269|PubMed:34407394"
FT HELIX 550..557
FT /evidence="ECO:0007829|PDB:1SKN"
FT HELIX 564..569
FT /evidence="ECO:0007829|PDB:1SKN"
FT HELIX 572..581
FT /evidence="ECO:0007829|PDB:1SKN"
FT HELIX 586..615
FT /evidence="ECO:0007829|PDB:1SKN"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:1SKN"
SQ SEQUENCE 623 AA; 70709 MW; 31A70303AB7CC691 CRC64;
MGGSSRRQRS TSATRRDDKR RRRQCFSSVA DDEEETTSIY GVSSIFIWIL ATSSLILVIS
SPSSNTSIQS SSYDRITTKH LLDNISPTFK MYTDSNNRNF DEVNHQHQQE QDFNGQSKYD
YPQFNRPMGL RWRDDQRMME YFMSNGPVET VPVMPILTEH PPASPFGRGP STERPTTSSR
YEYSSPSLED IDLIDVLWRS DIAGEKGTRQ VAPADQYECD LQTLTEKSTV APLTAEENAR
YEDLSKGFYN GFFESFNNNQ YQQKHQQQQR EQIKTPTLEH PTQKAELEDD LFDEDLAQLF
EDVSREEGQL NQLFDNKQQH PVINNVSLSE GIVYNQANLT EMQEMRDSCN QVSISTIPTT
STAQPETLFN VTDSQTVEQW LPTEVVPNDV FPTSNYAYIG MQNDSLQAVV SNGQIDYDHS
YQSTGQTPLS PLIIGSSGRQ QQTQTSPGSV TVTATATQSL FDPYHSQRHS FSDCTTDSSS
TCSRLSSESP RYTSESSTGT HESRFYGKLA PSSGSRYQRS SSPRSSQSSI KIARVVPLAS
GQRKRGRQSK DEQLASDNEL PVSAFQISEM SLSELQQVLK NESLSEYQRQ LIRKIRRRGK
NKVAARTCRQ RRTDRHDKMS HYI
