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Protein skinhead-1

 SKN1_CAEEL              Reviewed;         623 AA.
P34707; Q8MPW2; Q8MPW3;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
27-MAY-2002, sequence version 2.
22-NOV-2017, entry version 163.
RecName: Full=Protein skinhead-1;
Name=skn-1; ORFNames=T19E7.2;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
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).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-623 (ISOFORM A), FUNCTION,
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=Bristol N2;
PubMed=1547503; DOI=10.1016/0092-8674(92)90078-Q;
Bowerman B., Eaton B.A., Priess J.R.;
"skn-1, a maternally expressed gene required to specify the fate of
ventral blastomeres in the early C. elegans embryo.";
Cell 68:1061-1075(1992).
[3]
SUBUNIT, SUBCELLULAR LOCATION, AND DNA-BINDING.
PubMed=7939715; DOI=10.1126/science.7939715;
Blackwell T.K., Bowerman B., Priess J.R., Weintraub H.;
"Formation of a monomeric DNA binding domain by Skn-1 bZIP and
homeodomain elements.";
Science 266:621-628(1994).
[4]
FUNCTION.
PubMed=11463373; DOI=10.1016/S1097-2765(01)00195-2;
Maduro M.F., Meneghini M.D., Bowerman B., Broitman-Maduro G.,
Rothman J.H.;
"Restriction of mesendoderm to a single blastomere by the combined
action of SKN-1 and a GSK-3beta homolog is mediated by MED-1 and -2 in
C. elegans.";
Mol. Cell 7:475-485(2001).
[5]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-164 AND SER-430, AND
MUTAGENESIS OF SER-164 AND SER-430.
PubMed=16166371; DOI=10.1101/gad.1324805;
Inoue H., Hisamoto N., An J.H., Oliveira R.P., Nishida E.,
Blackwell T.K., Matsumoto K.;
"The C. elegans p38 MAPK pathway regulates nuclear localization of the
transcription factor SKN-1 in oxidative stress response.";
Genes Dev. 19:2278-2283(2005).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20624915; DOI=10.1074/jbc.M110.146274;
Okuyama T., Inoue H., Ookuma S., Satoh T., Kano K., Honjoh S.,
Hisamoto N., Matsumoto K., Nishida E.;
"The ERK-MAPK pathway regulates longevity through SKN-1 and insulin-
like signaling in Caenorhabditis elegans.";
J. Biol. Chem. 285:30274-30281(2010).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=22216003; DOI=10.1371/journal.ppat.1002453;
Hoeven R.V., McCallum K.C., Cruz M.R., Garsin D.A.;
"Ce-Duox1/BLI-3 generated reactive oxygen species trigger protective
SKN-1 activity via p38 MAPK signaling during infection in C.
elegans.";
PLoS Pathog. 7:E1002453-E1002453(2011).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23106139; DOI=10.1111/jnc.12072;
VanDuyn N., Settivari R., LeVora J., Zhou S., Unrine J., Nass R.;
"The metal transporter SMF-3/DMT-1 mediates aluminum-induced dopamine
neuron degeneration.";
J. Neurochem. 124:147-157(2013).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23721876; DOI=10.1016/j.neuro.2013.05.014;
Settivari R., VanDuyn N., LeVora J., Nass R.;
"The Nrf2/SKN-1-dependent glutathione S-transferase pi homologue GST-1
inhibits dopamine neuron degeneration in a Caenorhabditis elegans
model of manganism.";
NeuroToxicology 38:51-60(2013).
[10]
FUNCTION.
PubMed=24385935; DOI=10.1371/journal.pgen.1004063;
Ghose P., Park E.C., Tabakin A., Salazar-Vasquez N., Rongo C.;
"Anoxia-reoxygenation regulates mitochondrial dynamics through the
hypoxia response pathway, SKN-1/Nrf, and stomatin-like protein STL-
1/SLP-2.";
PLoS Genet. 9:E1004063-E1004063(2013).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25688864; DOI=10.1371/journal.pone.0117444;
Mendes T.K., Novakovic S., Raymant G., Bertram S.E., Esmaillie R.,
Nadarajan S., Breugelmans B., Hofmann A., Gasser R.B.,
Colaiacovo M.P., Boag P.R.;
"Investigating the role of RIO protein kinases in Caenorhabditis
elegans.";
PLoS ONE 10:E0117444-E0117444(2015).
[12]
FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND DISRUPTION
PHENOTYPE.
PubMed=27528192; DOI=10.7554/eLife.17721;
Lehrbach N.J., Ruvkun G.;
"Proteasome dysfunction triggers activation of SKN-1A/Nrf1 by the
aspartic protease DDI-1.";
Elife 5:0-0(2016).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 540-623.
PubMed=9628487; DOI=10.1038/nsb0698-484;
Rupert P.B., Daughdrill G.W., Bowerman B., Matthews B.W.;
"A new DNA-binding motif in the Skn-1 binding domain-DNA complex.";
Nat. Struct. Biol. 5:484-491(1998).
-!- FUNCTION: Transcription factor required to specify the fate of
ventral blastomeres in the early embryo, and postembryonically for
the development of the intestine. Directly regulates expression of
zygotically expressed med-1 and med-2 to direct mesendoderm
development (PubMed:1547503, PubMed:11463373). Required for stl-1
mRNA up-regulation in response to oxidative stress and anoxia.
Required for the up-regulation of gcs-1 and several glutathione-S-
transferase mRNAs in response to oxidative stress generated during
pathogenic bacterial infection (PubMed:22216003). In neurons,
involved in mitochondrial fusion and behavioral recovery during
reoxygenation (PubMed:24385935). Required for riok-1 mRNA
expression in the intestine (PubMed:25688864). Downstream of the
let-60/Ras, mek-2 and pmk-1 pathway, positively regulates lifespan
probably by preventing transcription of insulin-like peptides such
as ins-39 (PubMed:20624915). Prevents degeneration of dopaminergic
CEP neurons in response to high Al(3+) or Mn(2+) levels, probably
by promoting the expression of glutathione-S-transferase gst-1
(PubMed:23106139, PubMed:23721876). {ECO:0000269|PubMed:11463373,
ECO:0000269|PubMed:1547503, ECO:0000269|PubMed:20624915,
ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:23106139,
ECO:0000269|PubMed:23721876, ECO:0000269|PubMed:24385935,
ECO:0000269|PubMed:25688864}.
-!- FUNCTION: Isoform a: Directed by the ER-associated degradation
pathway (ERAD), mediates proteasomal homeostasis by regulating the
expression of proteasomal subunits such as rpt-3 to confer
resistance to proteasomal dysfunction.
{ECO:0000269|PubMed:27528192}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7939715}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16166371,
ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:7939715}.
Cytoplasm {ECO:0000269|PubMed:16166371,
ECO:0000269|PubMed:22216003}. Note=In absence of stress, localizes
in the cytoplasm of intestinal cells. Upon paraquat or arsenite
treatments or upon bacterial infection, localizes in the nucleus
(PubMed:16166371, PubMed:22216003). Nuclear localization is
regulated by pmk-1-mediated phosphorylation (PubMed:16166371).
{ECO:0000269|PubMed:16166371, ECO:0000269|PubMed:22216003}.
-!- SUBCELLULAR LOCATION: Isoform a: Nucleus
{ECO:0000269|PubMed:27528192}. Note=Localizes to the nucleus in
response to proteasomal dysfunction.
{ECO:0000269|PubMed:27528192}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=a;
IsoId=P34707-1; Sequence=Displayed;
Name=b;
IsoId=P34707-2; Sequence=VSP_011488, VSP_011489;
Note=No experimental confirmation available.;
Name=c;
IsoId=P34707-3; Sequence=VSP_011487;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Postembryonic intestinal cells.
{ECO:0000269|PubMed:1547503}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
{ECO:0000269|PubMed:1547503}.
-!- DOMAIN: Alternative DNA-binding strategy due to lack of a leucine
zipper dimerization segment: DNA binding domain binds to its
cognate half-site, an N-terminal arm recognizes adjacent 5' AT-
rich sequences in the minor groove and the intervening residues
stabilize interactions of these two subdomains with DNA.
{ECO:0000269|PubMed:9628487}.
-!- PTM: Isoform a: Cleaved by the aspartic protease ddi-1.
{ECO:0000269|PubMed:27528192}.
-!- DISRUPTION PHENOTYPE: Isoform a: Viable, but there is failed
activation of the expression of the proteasomal subunit rpt-3 in
all tissues (PubMed:27528192). Treatment with the proteasome
inhibitor bortezomib or knockout with rpn-10 RNAi results in
larval lethality (PubMed:27528192). Double knockout with pbs-5
results in failed expression the proteasomal subunit rpt-3
(PubMed:27528192). RNAi-mediated knockdown of all isoforms results
in a severe reduction in transcription of gst-4, gst-5, gst-7 and
gcs-1 mRNAs during infection by P.aeruginosa or P.faecalis
(PubMed:22216003). Susceptibility to P.aeruginosa and P.faecalis
is characterized by a decrease in survival rate (PubMed:22216003).
Also causes a loss of transcription of riok-1 mRNA in intestine
(PubMed:25688864). Reduces life span (PubMed:20624915). Moderate
increase in transcription of ins-39 mRNA (PubMed:20624915).
Moderate increase in CEP neuron death in response to high Al(3+)
levels (PubMed:23106139). RNAi-mediated knockdown causes an
increase in Mn(2+)-mediated dopaminergic CEP neuron degeneration
and a reduction in expression levels of glutathione S-transferase
gst-1 (PubMed:23721876). {ECO:0000269|PubMed:20624915,
ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:23106139,
ECO:0000269|PubMed:23721876, ECO:0000269|PubMed:25688864,
ECO:0000269|PubMed:27528192}.
-!- SIMILARITY: Belongs to the bZIP family. Skn1 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; FO080233; CCD62212.1; -; Genomic_DNA.
EMBL; FO080233; CCD62213.1; -; Genomic_DNA.
EMBL; FO080233; CCD62214.1; -; Genomic_DNA.
EMBL; M84359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A42143; A42143.
PIR; F88694; F88694.
RefSeq; NP_741404.1; NM_171345.4. [P34707-1]
RefSeq; NP_741405.1; NM_171346.3. [P34707-3]
RefSeq; NP_741406.1; NM_171347.5. [P34707-2]
UniGene; Cel.23037; -.
PDB; 1SKN; X-ray; 2.50 A; P=540-623.
PDBsum; 1SKN; -.
ProteinModelPortal; P34707; -.
SMR; P34707; -.
BioGrid; 42465; 5.
IntAct; P34707; 5.
MINT; MINT-1094083; -.
STRING; 6239.T19E7.2a.2; -.
BindingDB; P34707; -.
ChEMBL; CHEMBL2146298; -.
iPTMnet; P34707; -.
PaxDb; P34707; -.
EnsemblMetazoa; T19E7.2a; T19E7.2a; WBGene00004804. [P34707-1]
GeneID; 177343; -.
KEGG; cel:CELE_T19E7.2; -.
UCSC; T19E7.2b; c. elegans. [P34707-1]
CTD; 177343; -.
WormBase; T19E7.2a; CE27591; WBGene00004804; skn-1. [P34707-1]
WormBase; T19E7.2b; CE31238; WBGene00004804; skn-1. [P34707-2]
WormBase; T19E7.2c; CE31239; WBGene00004804; skn-1. [P34707-3]
eggNOG; KOG3863; Eukaryota.
eggNOG; ENOG410ZGMS; LUCA.
GeneTree; ENSGT00510000052725; -.
HOGENOM; HOG000021747; -.
InParanoid; P34707; -.
KO; K05638; -.
OMA; CNQVNIT; -.
OrthoDB; EOG091G02EB; -.
SignaLink; P34707; -.
EvolutionaryTrace; P34707; -.
PRO; PR:P34707; -.
Proteomes; UP000001940; Chromosome IV.
Bgee; WBGene00004804; -.
ExpressionAtlas; P34707; baseline and differential.
GO; GO:0005783; C:endoplasmic reticulum; IDA:WormBase.
GO; GO:0005739; C:mitochondrion; IDA:WormBase.
GO; GO:0005634; C:nucleus; IDA:WormBase.
GO; GO:0030544; F:Hsp70 protein binding; IPI:WormBase.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:WormBase.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:UniProtKB.
GO; GO:0001708; P:cell fate specification; IMP:WormBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
GO; GO:0048566; P:embryonic digestive tract development; IMP:UniProtKB.
GO; GO:0009880; P:embryonic pattern specification; IMP:WormBase.
GO; GO:0001714; P:endodermal cell fate specification; IMP:UniProtKB.
GO; GO:0048382; P:mesendoderm development; IMP:WormBase.
GO; GO:0007275; P:multicellular organism development; IMP:UniProtKB.
GO; GO:1901215; P:negative regulation of neuron death; IMP:UniProtKB.
GO; GO:1905804; P:positive regulation of cellular response to manganese ion; IMP:UniProtKB.
GO; GO:1900409; P:positive regulation of cellular response to oxidative stress; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:WormBase.
GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IMP:WormBase.
GO; GO:0006990; P:positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response; IMP:WormBase.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0009408; P:response to heat; IEP:WormBase.
GO; GO:0006979; P:response to oxidative stress; IEP:WormBase.
GO; GO:1901562; P:response to paraquat; IGI:UniProtKB.
GO; GO:0000303; P:response to superoxide; IMP:WormBase.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.880.10; -; 1.
InterPro; IPR004827; bZIP.
InterPro; IPR004826; bZIP_Maf.
InterPro; IPR008917; TF_DNA-bd_sf.
Pfam; PF03131; bZIP_Maf; 1.
SUPFAM; SSF47454; SSF47454; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
Cytoplasm; Developmental protein; DNA-binding; Nucleus;
Phosphoprotein; Reference proteome; Stress response; Transcription;
Transcription regulation; Translation regulation.
CHAIN 1 623 Protein skinhead-1.
/FTId=PRO_0000076639.
REGION 540 623 Basic motif. {ECO:0000250}.
MOD_RES 164 164 Phosphoserine; by pmk-1.
{ECO:0000269|PubMed:16166371}.
MOD_RES 430 430 Phosphoserine; by pmk-1.
{ECO:0000269|PubMed:16166371}.
VAR_SEQ 1 313 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_011488.
VAR_SEQ 1 90 Missing (in isoform c). {ECO:0000305}.
/FTId=VSP_011487.
VAR_SEQ 314 389 FDNKQQHPVINNVSLSEGIVYNQANLTEMQEMRDSCNQVSI
STIPTTSTAQPETLFNVTDSQTVEQWLPTEVVPND -> MS
LPSDFASSLLASSTTTNTTNTAPAAVNSFDEQEEESKKILN
MYLQMFNQQQVDQHGHHHQHPYAYSGVSSTFDR (in
isoform b). {ECO:0000305}.
/FTId=VSP_011489.
MUTAGEN 164 164 S->A: Abolishes phosphorylation by pmk-1.
Loss of nuclear translocation and
increased susceptibility in response to
arsenite treatment; when associated with
A-340. {ECO:0000269|PubMed:16166371}.
MUTAGEN 430 430 S->A: Abolishes phosphorylation by pmk-1.
Loss of nuclear translocation and
increased susceptibility in response to
arsenite treatment; when associated with
A-74. {ECO:0000269|PubMed:16166371}.
HELIX 550 557 {ECO:0000244|PDB:1SKN}.
HELIX 564 569 {ECO:0000244|PDB:1SKN}.
HELIX 572 581 {ECO:0000244|PDB:1SKN}.
HELIX 586 615 {ECO:0000244|PDB:1SKN}.
TURN 616 618 {ECO:0000244|PDB:1SKN}.
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


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