CBXH1_CAEEL
ID CBXH1_CAEEL Reviewed; 184 AA.
AC G5EET5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Chromobox protein homolog hpl-1 {ECO:0000305};
DE AltName: Full=HP1-like heterochromatin protein 1 {ECO:0000312|WormBase:K08H2.6};
GN Name=hpl-1 {ECO:0000312|WormBase:K08H2.6};
GN ORFNames=K08H2.6 {ECO:0000312|WormBase:K08H2.6};
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|EMBL:AAC78602.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC78602.1};
RA Kurz T., Schulze E.;
RT "A Heterochromatin Protein 1 homolog in C.elegans.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2] {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 [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16905130; DOI=10.1016/j.ydbio.2006.06.039;
RA Schott S., Coustham V., Simonet T., Bedet C., Palladino F.;
RT "Unique and redundant functions of C. elegans HP1 proteins in post-
RT embryonic development.";
RL Dev. Biol. 298:176-187(2006).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=17967446; DOI=10.1016/j.ydbio.2007.09.035;
RA Simonet T., Dulermo R., Schott S., Palladino F.;
RT "Antagonistic functions of SET-2/SET1 and HPL/HP1 proteins in C. elegans
RT development.";
RL Dev. Biol. 312:367-383(2007).
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH HIS-24 AND HPL-2.
RX PubMed=22083954; DOI=10.1128/mcb.05229-11;
RA Studencka M., Konzer A., Moneron G., Wenzel D., Opitz L.,
RA Salinas-Riester G., Bedet C., Krueger M., Hell S.W., Wisniewski J.R.,
RA Schmidt H., Palladino F., Schulze E., Jedrusik-Bode M.;
RT "Novel roles of Caenorhabditis elegans heterochromatin protein HP1 and
RT linker histone in the regulation of innate immune gene expression.";
RL Mol. Cell. Biol. 32:251-265(2012).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=23028351; DOI=10.1371/journal.pgen.1002940;
RA Studencka M., Wesolowski R., Opitz L., Salinas-Riester G., Wisniewski J.R.,
RA Jedrusik-Bode M.;
RT "Transcriptional repression of Hox genes by C. elegans HP1/HPL and H1/HIS-
RT 24.";
RL PLoS Genet. 8:e1002940-e1002940(2012).
RN [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HISTONE H3; HPL-2;
RP HDA-1; LSD-1; SPR-5 AND RCOR-1.
RX PubMed=26476455; DOI=10.1093/nar/gkv1063;
RA Vandamme J., Sidoli S., Mariani L., Friis C., Christensen J., Helin K.,
RA Jensen O.N., Salcini A.E.;
RT "H3K23me2 is a new heterochromatic mark in Caenorhabditis elegans.";
RL Nucleic Acids Res. 43:9694-9710(2015).
CC -!- FUNCTION: Seems to be involved in transcriptional silencing in
CC heterochromatin-like complexes (By similarity). Involved in epigenetic
CC repression (By similarity). Probably does not act as global
CC transcriptional repressor (PubMed:23028351). Plays a role in linking
CC epigenetic regulation with the innate immune response
CC (PubMed:22083954). Acting in concert with chromobox protein homolog
CC hpl-2 and histone H1 protein his-24, involved in reproduction, somatic
CC gonad development, male tail development and vulval cell fate
CC decisions; perhaps as a result of modulating expression of Hox genes
CC mab-5 and egl-5 (PubMed:23028351, PubMed:16905130). Role in growth and
CC somatic gonad development is antagonized by histone-lysine N-
CC methyltransferase set-2/SET1 (PubMed:17967446). Required for larval
CC development, acting redundantly with hpl-2 (PubMed:26476455,
CC PubMed:16905130). Plays a role in the formation of the vulva and in
CC fertility, acting together with a CoREST-like complex, and hpl-2
CC (PubMed:26476455, PubMed:16905130). {ECO:0000250|UniProtKB:Q13185,
CC ECO:0000269|PubMed:16905130, ECO:0000269|PubMed:17967446,
CC ECO:0000269|PubMed:22083954, ECO:0000269|PubMed:23028351,
CC ECO:0000269|PubMed:26476455}.
CC -!- SUBUNIT: Interacts with histone demethylase spr-5 (PubMed:26476455).
CC Interacts with chromobox protein homolog hpl-2 (PubMed:26476455,
CC PubMed:22083954). Interacts with histone H3 tails methylated at 'Lys-9'
CC (H3K9me3) and 'Lys-23'(H3K23me2) (PubMed:26476455). Interacts with
CC histone H1 variant his-24 (when monomethylated at 'Lys-14'); the
CC interaction is direct (PubMed:22083954). May interact with the REST
CC corepressor rcor-1, histone deacetylase hda-1, and the histone
CC demethylase lsd-1 (PubMed:26476455). {ECO:0000269|PubMed:22083954,
CC ECO:0000269|PubMed:26476455}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16905130,
CC ECO:0000269|PubMed:26476455}. Note=Partially co-localizes with histone
CC H3 tails methylated at 'Lys-9' (H3K9me3) and 'Lys-23'(H3K23me2) in
CC chromatin (PubMed:26476455). Localizes to distinct nuclear foci, not
CC overlapping significantly with hpl-2, in embryonic cells
CC (PubMed:26476455, PubMed:16905130). {ECO:0000269|PubMed:16905130,
CC ECO:0000269|PubMed:26476455}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos at about the 50 cell stage
CC (PubMed:16905130). Expressed in most, but not all cells of larvae and
CC adults, especially in neuronal and hypodermal cells (PubMed:16905130).
CC {ECO:0000269|PubMed:16905130}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in a hpl-2 mutant
CC background causes larval arrest. {ECO:0000269|PubMed:16905130}.
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DR EMBL; AF056580; AAC78602.1; -; mRNA.
DR EMBL; BX284606; CAA94152.1; -; Genomic_DNA.
DR PIR; T23518; T23518.
DR RefSeq; NP_510199.1; NM_077798.4.
DR AlphaFoldDB; G5EET5; -.
DR SMR; G5EET5; -.
DR IntAct; G5EET5; 1.
DR STRING; 6239.K08H2.6; -.
DR EPD; G5EET5; -.
DR PaxDb; G5EET5; -.
DR PeptideAtlas; G5EET5; -.
DR EnsemblMetazoa; K08H2.6.1; K08H2.6.1; WBGene00001995.
DR GeneID; 181450; -.
DR KEGG; cel:CELE_K08H2.6; -.
DR CTD; 181450; -.
DR WormBase; K08H2.6; CE06164; WBGene00001995; hpl-1.
DR eggNOG; KOG1911; Eukaryota.
DR GeneTree; ENSGT00940000175144; -.
DR HOGENOM; CLU_045874_1_2_1; -.
DR InParanoid; G5EET5; -.
DR OMA; YIKWQGF; -.
DR OrthoDB; 1628171at2759; -.
DR PhylomeDB; G5EET5; -.
DR Reactome; R-CEL-73772; RNA Polymerase I Promoter Escape.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001995; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0000792; C:heterochromatin; IDA:WormBase.
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:0019899; F:enzyme binding; IPI:WormBase.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0007281; P:germ cell development; IGI:WormBase.
DR GO; GO:0008406; P:gonad development; IGI:WormBase.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IGI:WormBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0040027; P:negative regulation of vulval development; IGI:WormBase.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:0040010; P:positive regulation of growth rate; IGI:WormBase.
DR GO; GO:0045595; P:regulation of cell differentiation; IGI:WormBase.
DR GO; GO:0000003; P:reproduction; IGI:WormBase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR017984; Chromo_dom_subgr.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR008251; Chromo_shadow_dom.
DR InterPro; IPR023779; Chromodomain_CS.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF01393; Chromo_shadow; 1.
DR PRINTS; PR00504; CHROMODOMAIN.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00300; ChSh; 1.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..184
FT /note="Chromobox protein homolog hpl-1"
FT /id="PRO_0000455618"
FT DOMAIN 37..95
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 184 AA; 20885 MW; 9E8F95510A95EDF7 CRC64;
MSRQNPVRST RGNSLRAREA QQAQDAPLFQ ESSSNVFVVE KVLNKRLTRG GSEYYIKWQG
FPESECSWEP IENLQCDRMI QEYEKEAAKR TTRKRRYSPQ PSTSSSAELQ PSTSDEWAGK
TLKTIIGITK APGELHFLCK FSDDSVHLIP LREANVRFPS QVIKFYETRL VLQGVSPTIP
GGMS
