ID   SAEG2_CAEEL             Reviewed;         305 AA.
AC   Q03615;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Suppressor of activated egl-4 protein 2 {ECO:0000312|WormBase:T23G5.6};
GN   Name=saeg-2 {ECO:0000312|WormBase:T23G5.6};
GN   ORFNames=T23G5.6 {ECO:0000312|WormBase:T23G5.6};
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].
RC   STRAIN=Bristol N2;
RX   PubMed=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
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]
RP   FUNCTION, IDENTIFICATION IN HISTONE DEACETYLASE COMPLEX, INTERACTION WITH
RP   ITSELF AND EGL-4, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=21573134; DOI=10.1371/journal.pgen.1002065;
RA   Hao Y., Xu N., Box A.C., Schaefer L., Kannan K., Zhang Y., Florens L.,
RA   Seidel C., Washburn M.P., Wiegraebe W., Mak H.Y.;
RT   "Nuclear cGMP-dependent kinase regulates gene expression via activity-
RT   dependent recruitment of a conserved histone deacetylase complex.";
RL   PLoS Genet. 7:E1002065-E1002065(2011).
CC   -!- FUNCTION: As a likely component of a histone deacetylase complex,
CC       together with saeg-1 and hda-2, functions downstream of the cAMP-
CC       dependent kinase egl-4 to regulate the expression of genes required for
CC       egg-laying and foraging (PubMed:21573134).
CC       {ECO:0000250|UniProtKB:Q9H147, ECO:0000269|PubMed:21573134}.
CC   -!- SUBUNIT: Interacts with phosphorylated egl-4. May interact with itself.
CC       May be a component of a histone deacetylase complex containing saeg-2,
CC       saeg-1 and hda-2. {ECO:0000269|PubMed:21573134}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21573134}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:21573134}.
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DR   EMBL; Z19158; CAA79572.2; -; Genomic_DNA.
DR   PIR; S28307; S28307.
DR   RefSeq; NP_499042.2; NM_066641.4.
DR   AlphaFoldDB; Q03615; -.
DR   SMR; Q03615; -.
DR   BioGRID; 41502; 4.
DR   STRING; 6239.T23G5.6; -.
DR   EPD; Q03615; -.
DR   PaxDb; Q03615; -.
DR   PeptideAtlas; Q03615; -.
DR   EnsemblMetazoa; T23G5.6.1; T23G5.6.1; WBGene00011964.
DR   GeneID; 176303; -.
DR   KEGG; cel:CELE_T23G5.6; -.
DR   UCSC; T23G5.6; c. elegans.
DR   CTD; 176303; -.
DR   WormBase; T23G5.6; CE37794; WBGene00011964; saeg-2.
DR   eggNOG; KOG4801; Eukaryota.
DR   GeneTree; ENSGT00510000047836; -.
DR   HOGENOM; CLU_912863_0_0_1; -.
DR   InParanoid; Q03615; -.
DR   OMA; TENDHRA; -.
DR   OrthoDB; 622558at2759; -.
DR   PhylomeDB; Q03615; -.
DR   PRO; PR:Q03615; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00011964; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR   InterPro; IPR041384; DNTTIP1_dimer.
DR   InterPro; IPR026064; TdIF1.
DR   PANTHER; PTHR23399; PTHR23399; 1.
DR   Pfam; PF18192; DNTTIP1_dimer; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Reference proteome.
FT   CHAIN           1..305
FT                   /note="Suppressor of activated egl-4 protein 2"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000065478"
FT   DNA_BIND        158..170
FT                   /note="A.T hook"
FT                   /evidence="ECO:0000255"
FT   REGION          138..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   305 AA;  35116 MW;  413D095D8F9A67EB CRC64;
     MRIVILDELL SREMDGSNDG SSARVNSLKH VIKRNKMDMA DDAPSSLDLM RRIFQAEISR
     EIHQIMERHT RTTLLPAIEN LRKNGHVVDE SVLNGLYCNI LEAAKKPYQK DPEPMPPICT
     NGNGFLDINS QEHENNLKRG YESDSSDVSG VSHCSDAKRR RGRPRKDEEA YRLEMTPPTM
     NEVIRWNPDR IDVNTRFITA TKIAQVMGMP PSILFNKYPR MFRYSCDEDD KNILHEQNLL
     IRAPGRCYLL VAEDARQLVP STYFQDVLNV SFLISEPLLS KIRQKAASTY EKYKVFLPTQ
     PNNYL