HCP3_CAEEL
ID HCP3_CAEEL Reviewed; 288 AA.
AC P34470;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Histone H3-like centromeric protein hcp-3;
DE AltName: Full=CENP-A homolog;
DE AltName: Full=CeCENP-A;
DE AltName: Full=Holocentric chromosome-binding protein 3;
GN Name=hcp-3 {ECO:0000312|WormBase:F58A4.3};
GN Synonyms=CENP-A {ECO:0000312|WormBase:F58A4.3};
GN ORFNames=F58A4.3 {ECO:0000312|WormBase:F58A4.3};
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=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
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, AND SUBCELLULAR LOCATION.
RX PubMed=10524621; DOI=10.1038/44062;
RA Buchwitz B.J., Ahmad K., Moore L.L., Roth M.B., Henikoff S.;
RT "A histone-H3-like protein in C. elegans.";
RL Nature 401:547-548(1999).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11402065; DOI=10.1083/jcb.153.6.1209;
RA Oegema K., Desai A., Rybina S., Kirkham M., Hyman A.A.;
RT "Functional analysis of kinetochore assembly in Caenorhabditis elegans.";
RL J. Cell Biol. 153:1209-1226(2001).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=12080088; DOI=10.1101/gad.989102;
RA Stear J.H., Roth M.B.;
RT "Characterization of HCP-6, a C. elegans protein required to prevent
RT chromosome twisting and merotelic attachment.";
RL Genes Dev. 16:1498-1508(2002).
RN [6]
RP FUNCTION.
RX PubMed=14522947; DOI=10.1101/gad.1126303;
RA Desai A., Rybina S., Mueller-Reichert T., Shevchenko A., Shevchenko A.,
RA Hyman A., Oegema K.;
RT "KNL-1 directs assembly of the microtubule-binding interface of the
RT kinetochore in C. elegans.";
RL Genes Dev. 17:2421-2435(2003).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15767665; DOI=10.1128/mcb.25.7.2583-2592.2005;
RA Moore L.L., Stanvitch G., Roth M.B., Rosen D.;
RT "HCP-4/CENP-C promotes the prophase timing of centromere resolution by
RT enabling the centromere association of HCP-6 in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 25:2583-2592(2005).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=16273096; DOI=10.1038/ncb1331;
RA Monen J., Maddox P.S., Hyndman F., Oegema K., Desai A.;
RT "Differential role of CENP-A in the segregation of holocentric C. elegans
RT chromosomes during meiosis and mitosis.";
RL Nat. Cell Biol. 7:1248-1255(2005).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16950114; DOI=10.1016/j.cub.2006.06.067;
RA Galy V., Askjaer P., Franz C., Lopez-Iglesias C., Mattaj I.W.;
RT "MEL-28, a novel nuclear-envelope and kinetochore protein essential for
RT zygotic nuclear-envelope assembly in C. elegans.";
RL Curr. Biol. 16:1748-1756(2006).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16950115; DOI=10.1016/j.cub.2006.07.071;
RA Fernandez A.G., Piano F.;
RT "MEL-28 is downstream of the Ran cycle and is required for nuclear-envelope
RT function and chromatin maintenance.";
RL Curr. Biol. 16:1757-1763(2006).
RN [11]
RP ERRATUM OF PUBMED:16950115.
RA Monen J., Maddox P.S., Hyndman F., Oegema K., Desai A.;
RL Nat. Cell Biol. 8:100-100(2006).
RN [12]
RP INTERACTION WITH KNL-2, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17339379; DOI=10.1083/jcb.200701065;
RA Maddox P.S., Hyndman F., Monen J., Oegema K., Desai A.;
RT "Functional genomics identifies a Myb domain-containing protein family
RT required for assembly of CENP-A chromatin.";
RL J. Cell Biol. 176:757-763(2007).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23684975; DOI=10.1016/j.cub.2013.04.028;
RA Bembenek J.N., Verbrugghe K.J., Khanikar J., Csankovszki G., Chan R.C.;
RT "Condensin and the spindle midzone prevent cytokinesis failure induced by
RT chromatin bridges in C. elegans embryos.";
RL Curr. Biol. 23:937-946(2013).
RN [14]
RP INTERACTION WITH LIN-53, AND SUBCELLULAR LOCATION.
RX PubMed=26904949; DOI=10.1016/j.celrep.2016.01.065;
RA Lee B.C., Lin Z., Yuen K.W.;
RT "RbAp46/48(LIN-53) is required for holocentromere assembly in
RT Caenorhabditis elegans.";
RL Cell Rep. 14:1819-1828(2016).
CC -!- FUNCTION: Histone H3-like variant which exclusively replaces
CC conventional H3 in the nucleosome core of centromeric chromatin at the
CC inner plate of the kinetochore (PubMed:10524621). Required for
CC recruitment and assembly of kinetochore proteins, mitotic progression
CC and chromosome segregation (PubMed:11402065, PubMed:14522947,
CC PubMed:16273096, PubMed:16950114, PubMed:16950115, PubMed:12080088,
CC PubMed:15767665). May serve as an epigenetic mark that propagates
CC centromere identity through replication and cell division (By
CC similarity). Might promote cleavage furrow stability during cytokinesis
CC (PubMed:23684975). Not required for chromosome segregation during
CC meiosis (PubMed:16273096). {ECO:0000250|UniProtKB:P49450,
CC ECO:0000269|PubMed:10524621, ECO:0000269|PubMed:11402065,
CC ECO:0000269|PubMed:12080088, ECO:0000269|PubMed:14522947,
CC ECO:0000269|PubMed:15767665, ECO:0000269|PubMed:16273096,
CC ECO:0000269|PubMed:16950114, ECO:0000269|PubMed:16950115,
CC ECO:0000269|PubMed:23684975}.
CC -!- SUBUNIT: Forms a nucleosome-like histone octamer containing two
CC molecules each of H2A, H2B, hcp-3 and H4 assembled in one hcp-3-H4
CC heterotetramer and two H2A-H2B heterodimers. The hcp-3-H4
CC heterotetramer is more compact and structurally more rigid than
CC corresponding H3-H4 heterotetramers (By similarity). Interacts with
CC knl-2 (PubMed:17339379). Interacts with lin-53 (PubMed:26904949).
CC {ECO:0000250|UniProtKB:P49450, ECO:0000269|PubMed:17339379,
CC ECO:0000269|PubMed:26904949}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10524621,
CC ECO:0000269|PubMed:11402065}. Chromosome, centromere
CC {ECO:0000269|PubMed:12080088, ECO:0000269|PubMed:15767665,
CC ECO:0000269|PubMed:17339379, ECO:0000269|PubMed:26904949}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:11402065}. Note=Requires
CC knl-2 and lin-53 for chromatin localization (PubMed:17339379,
CC PubMed:26904949). Co-localizes with hcp-6 at prophase, metaphase, and
CC anaphase chromosomes (PubMed:12080088, PubMed:15767665).
CC {ECO:0000269|PubMed:11402065, ECO:0000269|PubMed:12080088,
CC ECO:0000269|PubMed:15767665, ECO:0000269|PubMed:17339379,
CC ECO:0000269|PubMed:26904949}.
CC -!- INDUCTION: Present at higher lower (>95%) level than cpar-1 (at protein
CC level). {ECO:0000269|PubMed:16273096}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown impacts chromosome
CC segregation leading to abnormal chromatin distribution
CC (PubMed:16950114, PubMed:17339379). Disrupts mel-28 localization to
CC kinetochores (PubMed:16950115). Leads to cleavage furrow regression and
CC failed cytokinesis during the second embryonic division
CC (PubMed:23684975). RNAi-mediated knockdown abolishes the localization
CC of hcp-6 at the centromeres of mitotic chromosomes (PubMed:12080088).
CC {ECO:0000269|PubMed:12080088, ECO:0000269|PubMed:16950114,
CC ECO:0000269|PubMed:16950115, ECO:0000269|PubMed:17339379,
CC ECO:0000269|PubMed:23684975}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR EMBL; BX284603; CAA80160.1; -; Genomic_DNA.
DR PIR; S40975; S40975.
DR RefSeq; NP_499128.1; NM_066727.6.
DR AlphaFoldDB; P34470; -.
DR SMR; P34470; -.
DR BioGRID; 41554; 38.
DR DIP; DIP-27043N; -.
DR IntAct; P34470; 2.
DR STRING; 6239.F58A4.3; -.
DR EPD; P34470; -.
DR PaxDb; P34470; -.
DR PeptideAtlas; P34470; -.
DR EnsemblMetazoa; F58A4.3.1; F58A4.3.1; WBGene00001831.
DR GeneID; 176359; -.
DR KEGG; cel:CELE_F58A4.3; -.
DR UCSC; F58A4.3; c. elegans.
DR CTD; 176359; -.
DR WormBase; F58A4.3; CE00219; WBGene00001831; hcp-3.
DR eggNOG; KOG1745; Eukaryota.
DR GeneTree; ENSGT01050000244889; -.
DR HOGENOM; CLU_071908_0_0_1; -.
DR InParanoid; P34470; -.
DR OMA; ANDYTEA; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; P34470; -.
DR PRO; PR:P34470; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001831; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:WormBase.
DR GO; GO:0000776; C:kinetochore; IMP:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0070199; P:establishment of protein localization to chromosome; IMP:UniProtKB.
DR GO; GO:0051382; P:kinetochore assembly; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:WormBase.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:WormBase.
DR GO; GO:0046603; P:negative regulation of mitotic centrosome separation; IMP:UniProtKB.
DR GO; GO:0098813; P:nuclear chromosome segregation; IMP:UniProtKB.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; IMP:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 1: Evidence at protein level;
KW Centromere; Chromosome; DNA-binding; Kinetochore; Nucleosome core; Nucleus;
KW Reference proteome.
FT CHAIN 1..288
FT /note="Histone H3-like centromeric protein hcp-3"
FT /id="PRO_0000221377"
FT REGION 96..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..288
FT /note="H3-like"
FT COMPBIAS 145..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 288 AA; 32997 MW; 38E53D8E08F0415C CRC64;
MADDTPIIEE IAEQNESVTR IMQRLKHDMQ RVTSVPGFNT SAAGVNDLID ILNQYKKELE
DDAANDYTEA HIHKIRLVTG KRNQYVLKLK QAEDEYHARK EQARRRASSM DFTVGRNSTN
LVDYSHGRHH MPSYRRHDSS DEENYSMDGT NGDGNRAGPS NPDRGNRTGP SSSDRVRMRA
GRNRVTKTRR YRPGQKALEE IRKYQKTEDL LIQKAPFARL VREIMQTSTP FGADCRIRSD
AISALQEAAE AFLVEMFEGS SLISTHAKRV TLMTTDIQLY RRLCLRHL
