ID   CEC3_CAEEL              Reviewed;         339 AA.
AC   P45968;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Chromo domain-containing protein cec-3;
DE   AltName: Full=Epigenetic memory antagonism protein 1 {ECO:0000303|PubMed:24685137};
GN   Name=cec-3; Synonyms=eap-1 {ECO:0000303|PubMed:24685137};
GN   ORFNames=T09A5.8;
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=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]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24348272; DOI=10.1371/journal.pgen.1004017;
RA   Zheng C., Karimzadegan S., Chiang V., Chalfie M.;
RT   "Histone methylation restrains the expression of subtype-specific genes
RT   during terminal neuronal differentiation in Caenorhabditis elegans.";
RL   PLoS Genet. 9:E1004017-E1004017(2013).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF PHE-24.
RX   PubMed=24685137; DOI=10.1016/j.celrep.2014.02.044;
RA   Greer E.L., Beese-Sims S.E., Brookes E., Spadafora R., Zhu Y.,
RA   Rothbart S.B., Aristizabal-Corrales D., Chen S., Badeaux A.I., Jin Q.,
RA   Wang W., Strahl B.D., Colaiacovo M.P., Shi Y.;
RT   "A histone methylation network regulates transgenerational epigenetic
RT   memory in C. elegans.";
RL   Cell Rep. 7:113-126(2014).
CC   -!- FUNCTION: Specifically recognizes and binds methylated 'Lys-9' of
CC       histone H3 (H3K9me), with highest preference for trimethylated 'Lys-9'
CC       (H3K9me3) followed by dimethylated 'Lys-9' (H3K9me2) followed by
CC       monomethylated 'Lys-9' (H3K9me1) (PubMed:24685137). Plays a role in
CC       maintaining correct unc-4 expression in the VC motor neurons where unc-
CC       4 is expressed in the vulval but not in the non-vulval VC neurons
CC       (PubMed:24348272). {ECO:0000269|PubMed:24348272,
CC       ECO:0000269|PubMed:24685137}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:24685137}. Nucleus
CC       {ECO:0000269|PubMed:24685137}. Note=Colocalizes with H3K9me2/H3K9me3 in
CC       germline nuclei. {ECO:0000269|PubMed:24685137}.
CC   -!- TISSUE SPECIFICITY: Expressed in every cell of the embryo (at protein
CC       level). In adults, expressed predominantly in the head region and the
CC       germline. {ECO:0000269|PubMed:24685137}.
CC   -!- DISRUPTION PHENOTYPE: Expression of unc-4 in all 6 VC motor neurons in
CC       contrast to wild-type expression which is only detected in the vulval
CC       VC neurons, leading to hyperinhibition of HSN neuron activity and egg-
CC       laying defects (PubMed:24348272). RNAi-mediated knockdown in an spr-5
CC       mutant background suppresses progressive sterility and prevents
CC       accumulation of histone H3 'Lys-4' dimethylation (PubMed:24685137).
CC       {ECO:0000269|PubMed:24348272, ECO:0000269|PubMed:24685137}.
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DR   EMBL; Z36753; CAA85339.1; -; Genomic_DNA.
DR   PIR; T24725; T24725.
DR   RefSeq; NP_495652.1; NM_063251.6.
DR   AlphaFoldDB; P45968; -.
DR   BioGRID; 39598; 2.
DR   IntAct; P45968; 1.
DR   STRING; 6239.T09A5.8.1; -.
DR   iPTMnet; P45968; -.
DR   EPD; P45968; -.
DR   PaxDb; 6239-T09A5-8; -.
DR   PeptideAtlas; P45968; -.
DR   EnsemblMetazoa; T09A5.8.1; T09A5.8.1; WBGene00011636.
DR   GeneID; 174265; -.
DR   KEGG; cel:CELE_T09A5.8; -.
DR   UCSC; T09A5.8; c. elegans.
DR   AGR; WB:WBGene00011636; -.
DR   WormBase; T09A5.8; CE01089; WBGene00011636; cec-3.
DR   eggNOG; KOG1911; Eukaryota.
DR   HOGENOM; CLU_850545_0_0_1; -.
DR   InParanoid; P45968; -.
DR   OMA; FISRCEF; -.
DR   OrthoDB; 75895at2759; -.
DR   PRO; PR:P45968; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00011636; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0005721; C:pericentric heterochromatin; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00024; CD_CSD; 1.
DR   Gene3D; 2.40.50.40; -; 1.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   PANTHER; PTHR22812:SF164; CHROMO DOMAIN-CONTAINING PROTEIN CEC-3; 1.
DR   PANTHER; PTHR22812; CHROMOBOX PROTEIN; 1.
DR   Pfam; PF00385; Chromo; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
PE   1: Evidence at protein level;
KW   Chromosome; DNA-binding; Nucleus; Reference proteome.
FT   CHAIN           1..339
FT                   /note="Chromo domain-containing protein cec-3"
FT                   /id="PRO_0000080243"
FT   DOMAIN          24..84
FT                   /note="Chromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         24
FT                   /note="F->A: Disrupts binding to H3K9-methylated peptides."
FT                   /evidence="ECO:0000269|PubMed:24685137"
SQ   SEQUENCE   339 AA;  37736 MW;  9396D2A18C404241 CRC64;
     MSNEGSREES REPEAREGKS DEIFEVEKIL AHKVTDNLLV LQVRWLGYGA DEDTWEPEED
     LQECASEVVA EYYKKLKVTD KTELIELLQK QIKKNKSQKS KKRSKTVSDH ESNHDSDGSY
     GTPKTSKKSK KSAKNETPVS SKVPKVPTKA ALKSYEATVS GPVAPNNAKK AAMEVRDTRR
     NWLDEESSDD EAETTAPLSD VEKIASKVKV VKAVEEKAEE PVKRPSTPPK PREVVIKKDP
     SESPVASASS VIPTSKRKSI NAETSNGRQR TLAPPVIVKD ETTWTVDGIA RHTDVDNTKT
     KLILMTNSAT GERKVVEGRE AFELDGWALA KYLLDRCEF
//