HCP3L_CAEEL
ID HCP3L_CAEEL Reviewed; 261 AA.
AC P34440;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Histone H3-like centromeric protein cpar-1;
DE AltName: Full=CENP-A-related protein 1;
DE AltName: Full=Centromeric protein A related;
GN Name=cpar-1 {ECO:0000303|PubMed:16273096};
GN ORFNames=F54C8.2 {ECO:0000312|WormBase:F54C8.2};
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, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, 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 [4]
RP ERRATUM OF PUBMED:16273096.
RA Monen J., Maddox P.S., Hyndman F., Oegema K., Desai A.;
RL Nat. Cell Biol. 8:100-100(2006).
RN [5]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PROTEOLYTIC CLEAVAGE, AND
RP MUTAGENESIS OF 68-GLU--ARG-71.
RX PubMed=25919583; DOI=10.1371/journal.pone.0125382;
RA Monen J., Hattersley N., Muroyama A., Stevens D., Oegema K., Desai A.;
RT "Separase Cleaves the N-Tail of the CENP-A Related Protein CPAR-1 at the
RT Meiosis I Metaphase-Anaphase Transition in C. elegans.";
RL PLoS ONE 10:E0125382-E0125382(2015).
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. Required for recruitment and assembly
CC of kinetochore proteins, mitotic progression and chromosome
CC segregation. May serve as an epigenetic mark that propagates centromere
CC identity through replication and cell division. Not required for
CC chromosome segregation during meiosis. {ECO:0000269|PubMed:16273096}.
CC -!- SUBUNIT: Forms a nucleosome-like histone octamer containing two
CC molecules each of H2A, H2B, cpar-1 and H4 assembled in one cpar-1-H4
CC heterotetramer and two H2A-H2B heterodimers.
CC {ECO:0000250|UniProtKB:P49450}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16273096}. Chromosome
CC {ECO:0000269|PubMed:16273096, ECO:0000269|PubMed:25919583}.
CC Note=Localizes to chromosomes during meiotic prometaphase I and
CC metaphase I (PubMed:16273096, PubMed:25919583). Upon cleavage at the
CC onset of anaphase I, the C-terminus remains localized to chromosomes
CC (PubMed:25919583). The cleaved form transiently associates with
CC chromosome but not centromeres during embryonic mitosis
CC (PubMed:25919583). {ECO:0000269|PubMed:16273096,
CC ECO:0000269|PubMed:25919583}.
CC -!- DEVELOPMENTAL STAGE: Expressed in oocytes at the late
CC pachytene/diplotene stage and during the subsequent meiotic stages
CC (PubMed:16273096, PubMed:25919583). Expressed in polar bodies
CC (PubMed:25919583). Expressed at low levels in embryos (PubMed:16273096,
CC PubMed:25919583). {ECO:0000269|PubMed:16273096,
CC ECO:0000269|PubMed:25919583}.
CC -!- INDUCTION: Present at much lower (<5%) level than hcp-3 (at protein
CC level). {ECO:0000269|PubMed:16273096}.
CC -!- PTM: Cleaved at the onset of meiotic anaphase I, likely by separase
CC sep-1. {ECO:0000269|PubMed:25919583}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z22178; CAA80154.1; -; Genomic_DNA.
DR PIR; S40744; S40744.
DR RefSeq; NP_499073.1; NM_066672.4.
DR AlphaFoldDB; P34440; -.
DR SMR; P34440; -.
DR BioGRID; 50970; 4.
DR IntAct; P34440; 1.
DR STRING; 6239.F54C8.2; -.
DR EPD; P34440; -.
DR PaxDb; P34440; -.
DR EnsemblMetazoa; F54C8.2.1; F54C8.2.1; WBGene00010036.
DR GeneID; 186223; -.
DR KEGG; cel:CELE_F54C8.2; -.
DR UCSC; F54C8.2; c. elegans.
DR CTD; 186223; -.
DR WormBase; F54C8.2; CE00188; WBGene00010036; cpar-1.
DR eggNOG; KOG1745; Eukaryota.
DR GeneTree; ENSGT01050000244889; -.
DR HOGENOM; CLU_071908_0_0_1; -.
DR InParanoid; P34440; -.
DR OrthoDB; 1564596at2759; -.
DR PRO; PR:P34440; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010036; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
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:0000070; P:mitotic sister chromatid segregation; 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 Chromosome; DNA-binding; Nucleosome core; Nucleus; Reference proteome.
FT CHAIN 1..261
FT /note="Histone H3-like centromeric protein cpar-1"
FT /id="PRO_0000221378"
FT REGION 80..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..261
FT /note="H3-like"
FT COMPBIAS 94..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 71..72
FT /note="Cleavage; by sep-1"
FT /evidence="ECO:0000305|PubMed:25919583"
FT MUTAGEN 68..71
FT /note="EQAR->LQAQ: Loss of cleavage during meiosis I
FT metaphase-anaphase transition. No effect on chromosome
FT localization."
FT /evidence="ECO:0000269|PubMed:25919583"
SQ SEQUENCE 261 AA; 29085 MW; 2E7409FCE843C053 CRC64;
MADDGPIIEE IAEKNGRVAR IMQRLQHDTQ RVTSVPGFNT SATGYADLIA LLDQYKNDLE
AVGFNDLEQA RRRAPSVDIT VGSNSTNLVD YSHGRHDMPS HRRHDSSDEE ITAANSHHQS
PINVGNRNDT DGTNGRNGSR AGSSSSDRVR MIAGRNRISK TRRYRPGQKA LEEIRKYQES
EDLLIPKAPF ARLVREIMQT STPFSSDLRI RSDAINALQE ASEALLVQMF DGSSLISAHS
KRATLTTTDV QLYRRLCLPN L
