CEC4_CAEEL
ID CEC4_CAEEL Reviewed; 270 AA.
AC Q19972;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Chromo domain-containing protein cec-4 {ECO:0000305};
GN Name=cec-4 {ECO:0000312|WormBase:F32E10.2};
GN ORFNames=F32E10.2 {ECO:0000312|WormBase:F32E10.2};
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|EMBL:CCD70433.1,
RC 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, INTERACTION WITH HISTONE H3 LYS-9, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TYR-87 AND
RP TYR-111.
RX PubMed=26607792; DOI=10.1016/j.cell.2015.10.066;
RA Gonzalez-Sandoval A., Towbin B.D., Kalck V., Cabianca D.S., Gaidatzis D.,
RA Hauer M.H., Geng L., Wang L., Yang T., Wang X., Zhao K., Gasser S.M.;
RT "Perinuclear anchoring of H3K9-methylated chromatin stabilizes induced cell
RT fate in C. elegans embryos.";
RL Cell 163:1333-1347(2015).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31118512; DOI=10.1038/s41586-019-1243-y;
RA Cabianca D.S., Munoz-Jimenez C., Kalck V., Gaidatzis D., Padeken J.,
RA Seeber A., Askjaer P., Gasser S.M.;
RT "Active chromatin marks drive spatial sequestration of heterochromatin in
RT C. elegans nuclei.";
RL Nature 569:734-739(2019).
CC -!- FUNCTION: Chromatin anchor protein which binds to methylated lysine
CC residues on histone H3, thereby recruiting heterochromatin to the
CC nuclear periphery, especially in embryonic cells, with a lesser role in
CC differentiated cells (PubMed:26607792, PubMed:31118512). May be
CC required for the correct positioning of chromatin and nucleoli in
CC embryos (PubMed:26607792). {ECO:0000269|PubMed:26607792,
CC ECO:0000269|PubMed:31118512}.
CC -!- SUBUNIT: Interacts with mono-, di- and tri-methylated 'Lys-9' residues
CC on histone H3. Weakly interacts with methylated 'Lys-37' residues on
CC histone H3. {ECO:0000269|PubMed:26607792}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:26607792}. Membrane {ECO:0000305|PubMed:26607792};
CC Peripheral membrane protein {ECO:0000305|PubMed:26607792}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages from
CC embryogenesis to adulthood. Evenly expressed in most tissues during the
CC L1 stage of larval development, however, expression is weak in the
CC intestine and high in muscle. {ECO:0000269|PubMed:26607792}.
CC -!- DISRUPTION PHENOTYPE: Reduced anchoring of heterochromatin to the
CC nuclear periphery which is exacerbated on an mrg-1 mutant background
CC and is partially blocked by RNAi-mediated knockdown of cbp-1 or atf-8
CC (PubMed:26607792, PubMed:31118512). Altered nucleolar localization with
CC nucleoli positioned away from the nuclear periphery (PubMed:26607792).
CC When exposed to hlh-1, a transcription factor that induces muscle
CC differentiation, 25% of embryos continue to develop and the embryonic
CC cells do not transdifferentiate into muscle-like cells like their wild-
CC type counterparts (PubMed:26607792). {ECO:0000269|PubMed:26607792,
CC ECO:0000269|PubMed:31118512}.
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DR EMBL; BX284604; CCD70433.1; -; Genomic_DNA.
DR PIR; B88734; B88734.
DR RefSeq; NP_501231.1; NM_068830.6.
DR AlphaFoldDB; Q19972; -.
DR STRING; 6239.F32E10.2; -.
DR EPD; Q19972; -.
DR PaxDb; Q19972; -.
DR PeptideAtlas; Q19972; -.
DR EnsemblMetazoa; F32E10.2.1; F32E10.2.1; WBGene00017990.
DR EnsemblMetazoa; F32E10.2.2; F32E10.2.2; WBGene00017990.
DR GeneID; 177536; -.
DR KEGG; cel:CELE_F32E10.2; -.
DR UCSC; F32E10.2; c. elegans.
DR CTD; 177536; -.
DR WormBase; F32E10.2; CE04475; WBGene00017990; cec-4.
DR eggNOG; KOG1911; Eukaryota.
DR HOGENOM; CLU_1046720_0_0_1; -.
DR InParanoid; Q19972; -.
DR OrthoDB; 1628171at2759; -.
DR PRO; PR:Q19972; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00017990; Expressed in embryo and 4 other tissues.
DR GO; GO:0000793; C:condensed chromosome; IBA:GO_Central.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:WormBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; IDA:WormBase.
DR GO; GO:0097240; P:chromosome attachment to the nuclear envelope; IMP:WormBase.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:WormBase.
DR InterPro; IPR037948; Cec-4.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR PANTHER; PTHR10503; PTHR10503; 1.
DR Pfam; PF00385; Chromo; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Membrane; Nucleus; Reference proteome.
FT CHAIN 1..270
FT /note="Chromo domain-containing protein cec-4"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435681"
FT DOMAIN 87..147
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 87
FT /note="Y->A: Abolishes binding to the tri-methylated 'Lys-
FT 9' residues on histone H3; when associated with A-111."
FT /evidence="ECO:0000269|PubMed:26607792"
FT MUTAGEN 111
FT /note="Y->A: Abolishes binding to the tri-methylated 'Lys-
FT 9' residues on histone H3; when associated with A-87."
FT /evidence="ECO:0000269|PubMed:26607792"
SQ SEQUENCE 270 AA; 31072 MW; 3FC640C358424844 CRC64;
MAKKTVEGEH GTPKTNFTKK ETSKNHDDFK KIIGHKVVEE HYVEYEVELT SGKTITATEF
DFKGDDSLLS TYKKKVTKQS DDSSGEYAVE RVLAHRKVKG SPLYLVQWKG YPHPVWNSEM
WEEDLDNCKD LLAAYKKHQE DLKIAQTPKK TPSKTPKKTP KSLKRRALTP SDDEEEAGPI
APEPKKTPKQ STKKLKRTTS PETNLVEKSK KKAIPDLENH TLDQEKNDVI ERVEEIQEDE
DDDDEQREEV VTTAPVETKS RWGFGSWKWF
