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Database: UniProt
Entry: A8WFJ9
LinkDB: A8WFJ9
Original site: A8WFJ9 
ID   ETS4_CAEEL              Reviewed;         437 AA.
AC   A8WFJ9; H2KYS4;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   07-OCT-2020, entry version 106.
DE   RecName: Full=Transcription factor ets-4 {ECO:0000303|PubMed:20862312};
GN   Name=ets-4 {ECO:0000303|PubMed:20862312, ECO:0000312|WormBase:F22A3.1b};
GN   ORFNames=F22A3.1 {ECO:0000312|WormBase:F22A3.1b};
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|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   [2] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   DOMAIN, AND DISRUPTION PHENOTYPE.
RX   PubMed=20862312; DOI=10.1371/journal.pgen.1001125;
RA   Thyagarajan B., Blaszczak A.G., Chandler K.J., Watts J.L., Johnson W.E.,
RA   Graves B.J.;
RT   "ETS-4 is a transcriptional regulator of life span in Caenorhabditis
RT   elegans.";
RL   PLoS Genet. 6:E1001125-E1001125(2010).
RN   [3] {ECO:0000305}
RP   FUNCTION, PHOSPHORYLATION AT SER-73, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP   OF SER-73.
RX   PubMed=26484536; DOI=10.1371/journal.pgen.1005603;
RA   Li C., Hisamoto N., Matsumoto K.;
RT   "Axon regeneration is regulated by Ets-C/EBP transcription complexes
RT   generated by activation of the cAMP/Ca2+ signaling pathways.";
RL   PLoS Genet. 11:E1005603-E1005603(2015).
RN   [4] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27746047; DOI=10.1016/j.devcel.2016.09.018;
RA   Habacher C., Guo Y., Venz R., Kumari P., Neagu A., Gaidatzis D.,
RA   Harvald E.B., Faergeman N.J., Gut H., Ciosk R.;
RT   "Ribonuclease-mediated control of body fat.";
RL   Dev. Cell 39:359-369(2016).
CC   -!- FUNCTION: Transcription factor which binds to 5'-GGAA/T-3' DNA
CC       consensus sequences (PubMed:20862312, PubMed:26484536). Both positively
CC       and negatively regulates the expression of target genes
CC       (PubMed:20862312). Plays a role in the regulation of adult lifespan,
CC       which may in part be through modulation of daf-16 activity
CC       (PubMed:20862312). Regulates the expression of genes such as svh-2 in
CC       response to axon injury and in addition, may function downstream of the
CC       cAMP signaling pathway to promote axon regeneration (PubMed:26484536).
CC       Regulates the expression of lipid metabolism genes and may also control
CC       the expression of the RNA-binding protein rege-1 which too has been
CC       implicated in the control of fat accumulation (PubMed:27746047).
CC       {ECO:0000269|PubMed:20862312, ECO:0000269|PubMed:26484536,
CC       ECO:0000269|PubMed:27746047}.
CC   -!- SUBUNIT: May interact with cebp-1. {ECO:0000269|PubMed:26484536}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20862312}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=b {ECO:0000312|WormBase:F22A3.1b};
CC         IsoId=A8WFJ9-1; Sequence=Displayed;
CC       Name=a {ECO:0000312|WormBase:F22A3.1a};
CC         IsoId=A8WFJ9-2; Sequence=VSP_058757, VSP_058758;
CC   -!- TISSUE SPECIFICITY: Expressed in cells of the anterior and posterior
CC       bulbs of the pharynx, seam cells, a few unidentified cells of the
CC       vulva, the hypodermis, several unidentified neurons, labial socket
CC       cells of the head and rectal cells. {ECO:0000269|PubMed:20862312}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in intestinal cells from the 3-fold
CC       stage of embryogenesis to adulthood. {ECO:0000269|PubMed:20862312}.
CC   -!- DOMAIN: The N-terminal part (1-345) is responsible for activating
CC       transcription, but this action may be modulated by the PNT domain which
CC       acts to repress transcription. {ECO:0000269|PubMed:20862312}.
CC   -!- PTM: Phosphorylation is required for axon regeneration.
CC       {ECO:0000269|PubMed:26484536}.
CC   -!- DISRUPTION PHENOTYPE: Delayed larval development and increased
CC       lifespan, but overall resulting animals have normal morphology and
CC       fecundity (PubMed:20862312). Reduced egg-laying rate, but older
CC       hermaphrodites produce more progeny (PubMed:20862312). Both decreased
CC       expression of genes, such as the lipoprotein vit-5, which is related to
CC       life span regulation, and increased expression of genes such as lys-7,
CC       which is a lysosomal protein (PubMed:20862312). Reduced expression of
CC       genes such as svh-2 in response to axon injury and as a result, there
CC       is reduced axon regeneration of D-type motor neurons (PubMed:26484536).
CC       RNAi-mediated knockdown results in reduced expression of the RNA-
CC       binding protein rege-1 (PubMed:27746047). {ECO:0000269|PubMed:20862312,
CC       ECO:0000269|PubMed:26484536, ECO:0000269|PubMed:27746047}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
DR   EMBL; BX284606; CCD64581.1; -; Genomic_DNA.
DR   EMBL; BX284606; CCD64575.1; -; Genomic_DNA.
DR   RefSeq; NP_001123137.1; NM_001129665.2.
DR   RefSeq; NP_509099.2; NM_076698.4. [A8WFJ9-2]
DR   SMR; A8WFJ9; -.
DR   IntAct; A8WFJ9; 1.
DR   STRING; 6239.F22A3.1b; -.
DR   iPTMnet; A8WFJ9; -.
DR   PaxDb; A8WFJ9; -.
DR   EnsemblMetazoa; F22A3.1a.1; F22A3.1a.1; WBGene00017687. [A8WFJ9-2]
DR   EnsemblMetazoa; F22A3.1a.2; F22A3.1a.2; WBGene00017687. [A8WFJ9-2]
DR   EnsemblMetazoa; F22A3.1a.3; F22A3.1a.3; WBGene00017687. [A8WFJ9-2]
DR   EnsemblMetazoa; F22A3.1b.1; F22A3.1b.1; WBGene00017687. [A8WFJ9-1]
DR   GeneID; 180927; -.
DR   UCSC; F22A3.1b; c. elegans. [A8WFJ9-1]
DR   CTD; 180927; -.
DR   WormBase; F22A3.1a; CE34001; WBGene00017687; ets-4. [A8WFJ9-2]
DR   WormBase; F22A3.1b; CE41797; WBGene00017687; ets-4. [A8WFJ9-1]
DR   eggNOG; KOG3805; Eukaryota.
DR   GeneTree; ENSGT00940000157549; -.
DR   HOGENOM; CLU_736166_0_0_1; -.
DR   InParanoid; A8WFJ9; -.
DR   OMA; KIESSHH; -.
DR   OrthoDB; 837296at2759; -.
DR   PhylomeDB; A8WFJ9; -.
DR   PRO; PR:A8WFJ9; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00017687; Expressed in material anatomical entity and 5 other tissues.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR003118; Pointed_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF02198; SAM_PNT; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SMART; SM00251; SAM_PNT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   PROSITE; PS51433; PNT; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..437
FT                   /note="Transcription factor ets-4"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000438864"
FT   DOMAIN          120..202
FT                   /note="PNT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT   DNA_BIND        349..432
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:26484536"
FT   VAR_SEQ         1..54
FT                   /note="Missing (in isoform a)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058757"
FT   VAR_SEQ         201..207
FT                   /note="Missing (in isoform a)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058758"
FT   MUTAGEN         73
FT                   /note="S->A: Abolishes phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:26484536"
FT   MUTAGEN         73
FT                   /note="S->E: Phosphomimetic mutant which may allow for
FT                   association with cebp-1."
FT                   /evidence="ECO:0000269|PubMed:26484536"
SQ   SEQUENCE   437 AA;  49766 MW;  67685E3586878DB2 CRC64;
     MNGTGSVGHR WNSLSPEPHS GTESTASTPF VKSEFPFDDD LFGIDQVNNV KPHPMDMPCN
     LPIQPIEYNR RFSKDADHST FVKNEIEENI LNFNVNPEIA QDNGLDTQQI DIYRDLILRH
     LIQDISTTCA KLGLPNDFYL WSSEHGARWI NEMCMQFNLQ PPRNCSITGI DLLGMSQKDF
     EMILPAGGDT LHAQLQVWKT GTSDYVKAFE NYHPPVTVQS SGMTAAENNM QSKTNWLAST
     NNQTNNMAAA ENPNHPFFNG NGGYPNMSMS SFFQQGTVLP SPSNSDTSSN GSSQDMNDDD
     IDLHMNNSNC GFSNFFHNQG YMNSPIDAMC NGSEGDDDER AYTRHQGTVH LWQFIRELLD
     QPKQYSACVR WVDRDEGTFK IESSLLLARY WGQRKNRSQM NYDKLSRSLR QYYKKGIIQK
     PEKKQRLVYK FLPPYNL
//
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