SAEG1_CAEEL
ID SAEG1_CAEEL Reviewed; 900 AA.
AC Q20733;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Suppressor of activated egl-4 protein 1 {ECO:0000312|WormBase:F53H10.2a};
GN Name=saeg-1 {ECO:0000312|WormBase:F53H10.2a};
GN ORFNames=F53H10.2 {ECO:0000312|WormBase:F53H10.2a};
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, IDENTIFICATION IN HISTONE DEACETYLASE COMPLEX, INTERACTION WITH
RP EGL-4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP HIS-758.
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-2 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. {ECO:0000269|PubMed:21573134}.
CC -!- SUBUNIT: May be a component of a histone deacetylase complex containing
CC saeg-2, saeg-1 and hda-2. May interact with egl-4.
CC {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; BX284605; CAB01216.2; -; Genomic_DNA.
DR PIR; T22592; T22592.
DR RefSeq; NP_505769.2; NM_073368.7.
DR AlphaFoldDB; Q20733; -.
DR IntAct; Q20733; 11.
DR STRING; 6239.F53H10.2a; -.
DR EPD; Q20733; -.
DR PaxDb; Q20733; -.
DR EnsemblMetazoa; F53H10.2a.1; F53H10.2a.1; WBGene00010012.
DR GeneID; 179505; -.
DR KEGG; cel:CELE_F53H10.2; -.
DR UCSC; F53H10.2a; c. elegans.
DR CTD; 179505; -.
DR WormBase; F53H10.2a; CE32433; WBGene00010012; saeg-1.
DR eggNOG; KOG4167; Eukaryota.
DR GeneTree; ENSGT00940000169235; -.
DR InParanoid; Q20733; -.
DR OMA; KESWAST; -.
DR OrthoDB; 309974at2759; -.
DR PhylomeDB; Q20733; -.
DR SignaLink; Q20733; -.
DR PRO; PR:Q20733; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00010012; Expressed in larva and 4 other tissues.
DR ExpressionAtlas; Q20733; baseline and differential.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Metal-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..900
FT /note="Suppressor of activated egl-4 protein 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435740"
FT DOMAIN 451..544
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 560..611
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 736..758
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 758
FT /note="H->L: Reduced body size and egg-laying."
FT /evidence="ECO:0000269|PubMed:21573134"
SQ SEQUENCE 900 AA; 100969 MW; 74C9CA3077837B8C CRC64;
MPPPQHPPNY YAPRRSISTI TGPNRRDVDA FYQNNFPEKN GGSSGEHVPE YQASGQQHRP
SIMSGQSHQN NHLPTKNYSY EPLRFSPPNV TPPPLQFSTN TDGNRKNQRV RFNELPNYST
PNHYSVPPRK CSLAPNFFSS QNSHHMYPDQ YTPRTWQNNE FMPNHQVHPY HANHQQQHPQ
QHWRNQAASN GNHNPMYMRK HSAGHGIEIK LDHVDNPFGN PSHDMMDVTS GQPVKSEMLS
PIKMETTDPS QQIASPSFLM TSTSLLKQHL HKKSHHNVPS RKASIMALKS QLRTPRGTPL
NISTVPGTEL PYTPPPILAP MRNGSGLFCQ IVKSANSSLP VAEQSPDAPS CSTNGVDGDM
KHLMNGKKRS EDGDGPSRKN GFFYMAQQMN QTNFANELEA LRKESWASTS SADEKMQTER
KESLESIRKA SCMSDSYYEI EEGPKISDPN PHINLGKNYQ ARVKKWCDRQ VSTSERDAIE
DRDEIVFSSE ILQDIDPEQI TAFELLACSQ ACPRAGRNKE LALHLLMENK GNIEAAVEDL
LRSDTLDWEH YSSVFGYMYN DSVLWTPDEI YQFQDAIYQS EKDFDKVAVE LPGKSVKECV
QFYYTWKKDC PDDYRKLRNL RRKRQLLDIN LQKNQSEEPV VPAKKISIIE SGDSDNESNA
TDSSFIGNGH MEFRDRAFTS PMMSSPREEP IIGLSPSSKD LFGIQKNYQP TAPRAHHTPS
ASASKKGAQP SADGFFHCRL CDKCFEKVKS LNAHMKSHAM KARAEQEAKA HDAQVAAAAA
AQLTSAVGNV VGNPVATSPL NSFANGHLGI SIPSTIGNLT PQQLTPQQLN LNQQLQTQLN
SLSNQMSLNS PLTPQQQLQQ FTQQHLMARA MQQNLFQPVT STPLVQPTHP LIQAGLHSIN
