SDC1_CAEEL
ID SDC1_CAEEL Reviewed; 1201 AA.
AC P24349; Q20672;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Zinc finger protein sdc-1;
DE AltName: Full=Egg-laying defective protein 16;
GN Name=sdc-1; Synonyms=egl-16; ORFNames=F52E10.1;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Bristol N2;
RX PubMed=2027384; DOI=10.1038/351065a0;
RA Nonet M.L., Meyer B.J.;
RT "Early aspects of Caenorhabditis elegans sex determination and dosage
RT compensation are regulated by a zinc-finger protein.";
RL Nature 351:65-68(1991).
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 A SDC COMPLEX, INTERACTION WITH SDC-2 AND
RP SDC-3, AND SUBCELLULAR LOCATION.
RX PubMed=11937488; DOI=10.1101/gad.972702;
RA Chu D.S., Dawes H.E., Lieb J.D., Chan R.C., Kuo A.F., Meyer B.J.;
RT "A molecular link between gene-specific and chromosome-wide transcriptional
RT repression.";
RL Genes Dev. 16:796-805(2002).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22393255; DOI=10.1128/mcb.06546-11;
RA Wells M.B., Snyder M.J., Custer L.M., Csankovszki G.;
RT "Caenorhabditis elegans dosage compensation regulates histone H4 chromatin
RT state on X chromosomes.";
RL Mol. Cell. Biol. 32:1710-1719(2012).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23884442; DOI=10.1242/dev.094292;
RA Webster C.M., Wu L., Douglas D., Soukas A.A.;
RT "A non-canonical role for the C. elegans dosage compensation complex in
RT growth and metabolic regulation downstream of TOR complex 2.";
RL Development 140:3601-3612(2013).
CC -!- FUNCTION: Embryonic transcription factor regulating downstream genes
CC involved specifically in the sex determination and dosage compensation
CC pathways, or regulating other genes involved in the coordinate control
CC of both processes (PubMed:2027384). Component of the SDC complex that
CC functions in sex determination and in X chromosome dosage compensation
CC specifically in hermaphrodite (XX) animals (PubMed:11937488). Involved
CC in the recruitment of the condensin I-like dosage compensation complex
CC to the male sex-determining autosomal gene her-1, thereby contributing
CC to its repression and initiating hermaphrodite sexual development
CC (PubMed:11937488). Similarly, might contribute to X-linked gene
CC repression through recruitment of the dosage compensation complex to
CC the X chromosomes in hermaphrodites (PubMed:11937488). Seems to be
CC involved in the depletion of histone H4 lysine 16 acetylation (H4K16ac)
CC on dosage compensated X chromosomes (PubMed:22393255). Plays a role in
CC developmental rate and body fat regulation downstream of the TOR
CC complex 2 pathway (PubMed:23884442). {ECO:0000269|PubMed:11937488,
CC ECO:0000269|PubMed:2027384, ECO:0000269|PubMed:22393255,
CC ECO:0000269|PubMed:23884442}.
CC -!- SUBUNIT: Component of the SDC complex, which consists of sdc-1, sdc-2
CC and sdc-3. Within the complex, interacts with sdc-2 and sdc-3.
CC {ECO:0000269|PubMed:11937488}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11937488,
CC ECO:0000305|PubMed:22393255}. Chromosome {ECO:0000269|PubMed:11937488}.
CC Note=Localizes to X chromosomes in hermaphrodite (XX) animals.
CC {ECO:0000269|PubMed:11937488}.
CC -!- DISRUPTION PHENOTYPE: In the TOR complex 2 mutant background rict-1,
CC RNAi-mediated knockdown suppresses the growth delay and elevated body
CC fat index. {ECO:0000269|PubMed:23884442}.
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DR EMBL; X58520; CAA41410.1; -; Genomic_DNA.
DR EMBL; Z54282; CAA91056.2; -; Genomic_DNA.
DR PIR; G89734; G89734.
DR PIR; S15093; A33165.
DR RefSeq; NP_510650.2; NM_078249.5.
DR AlphaFoldDB; P24349; -.
DR BioGRID; 46586; 3.
DR ComplexPortal; CPX-3888; SDC complex.
DR STRING; 6239.F52E10.1; -.
DR EPD; P24349; -.
DR PaxDb; P24349; -.
DR PeptideAtlas; P24349; -.
DR EnsemblMetazoa; F52E10.1a.1; F52E10.1a.1; WBGene00004745.
DR GeneID; 181701; -.
DR UCSC; F52E10.1; c. elegans.
DR CTD; 181701; -.
DR WormBase; F52E10.1a; CE41321; WBGene00004745; sdc-1.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_270770_0_0_1; -.
DR InParanoid; P24349; -.
DR OMA; QEIWPLK; -.
DR OrthoDB; 1318335at2759; -.
DR PRO; PR:P24349; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004745; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; P24349; baseline and differential.
DR GO; GO:0000228; C:nuclear chromosome; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000805; C:X chromosome; IDA:ComplexPortal.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0042464; P:dosage compensation by hypoactivation of X chromosome; IMP:WormBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007530; P:sex determination; IMP:WormBase.
DR GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Chromosome; Developmental protein; Differentiation; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Sexual differentiation;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1201
FT /note="Zinc finger protein sdc-1"
FT /id="PRO_0000046890"
FT ZN_FING 117..139
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 145..168
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 233..254
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 268..290
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 486..513
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 521..543
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 652..674
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1164..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 16
FT /note="D -> V (in Ref. 1; CAA41410)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="Q -> QLQ (in Ref. 1; CAA41410)"
FT /evidence="ECO:0000305"
FT CONFLICT 942..943
FT /note="KT -> FS (in Ref. 1; CAA41410)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1201 AA; 139056 MW; 026761BB11B70CE3 CRC64;
MSDEEDIDES FEIEEDGISI TDARGNSLKA QQIAGKERNL DPEADDLEVV VNFYEAGDGT
FQLQLPKLTA VKPVDKVNDV LDFINFDKKV CDGIHSSIKL VSQRDQTGPA PFPKHKLTCA
HCDWSFDNVM KLVRHRGVHK NVGVYMCQVC LTLFGHTYNL FMHWRTSCSQ TSTTATDIEI
QKAETPYLHR NVLNVLGSLN RASQYYCTGG YVFLPSDWCI TNKEIVMEKD HMSSCHLCHL
PVPNKFLEAH GNVHRGRFRI DGRIYGDYFC HICGTVFIEQ DNLFKHWRLH CEEVIAYTPV
DQYLSNTELA TLAWLVLQTT ISQADIECLR VSSSLITEKL AKEHAERHGI ANSMHKYYHF
PQEIWPLKTF VNLDLVNDAI PISGENSFKI KDPKRPVHIM NLLATACPGF YATGKTFNMI
CSTKKSESDT KKVYRVILRY TTEGSVIQSY DFTARSFPKL RVDSETPEGV FSHPLADFNV
ESNEAIVCHK CDSKKLTITF STEVRLKYHL LRHSESRKDG YHCAICKIIV YNRSHEEHWI
NDCIPLQKLY RDQKDRECFD AEFAAKCASI IKKLRIRTLI RWKERANEDW VETKQTPDRI
GEDFAIKFQV GTTALKTLMA GLEEHYKNAQ ARHEAYKYSE ENFLPPLSTP VVVCFHCGTR
CHYTLLHDHL DYCHYWPRNK RLVNEEFHKW KKNGCRNTWR VMKSVAEAMQ IEVPFISEEQ
YSKILDYHTY FCNDTRYKVQ DSINNWNDCS TIRDVDLSEK LSVAEIVQKG EDSVMAPEPD
IIKNVYFPSA RIITDNMLLR MTEINLNDVV QRDPITKEEL TGKFKEVQDE QDAILFGDYR
AVLRSKGIMV NSISDFVAPP DELAKAKASQ ESAGQESVDH RNRREREFIQ QYMGKDLALE
AAARENGRLV EVDEEAEDYE LTPKELNARR LVERNRHREM CKTRCEHGEY DYEKFKARQV
PINPAKMKER KYLTRVVHES GPDDDVCPDE PENNIIAFSP KYENSLSDFR ISAIGFREKY
LADDKKKRNG IPIRKMTEAQ KGVALDYDTL MARHGGRPDV IMNPAGTVFV GGFVFDRKPT
CQDNMQTVYV LRNGYAHRYR IYHCEDTNGI YKFVWPQEQS FDPDSLAKSA RVRMVKQVKS
PEHMIHHIEE IDESIGHNYR LNRKRRNSET REHELIELDT DDLNEPSTSD GRYSFGHHGY
R
