CENPA_BOVIN
ID CENPA_BOVIN Reviewed; 138 AA.
AC P49449;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Histone H3-like centromeric protein A;
DE AltName: Full=Centromere protein A;
DE Short=CENP-A;
GN Name=CENPA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-125.
RX PubMed=7962047; DOI=10.1083/jcb.127.3.581;
RA Sullivan K.F., Hechenberger M., Masri K.;
RT "Human CENP-A contains a histone H3 related histone fold domain that is
RT required for targeting to the centromere.";
RL J. Cell Biol. 127:581-592(1994).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=2023923; DOI=10.1073/pnas.88.9.3734;
RA Palmer D.K., O'Day K., Trong H.L., Charbonneau H., Margolis R.L.;
RT "Purification of the centromere-specific protein CENP-A and demonstration
RT that it is a distinctive histone.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3734-3738(1991).
CC -!- FUNCTION: Histone H3-like nucleosomal protein that is specifically
CC found in centromeric nucleosomes. Replaces conventional H3 in the
CC nucleosome core of centromeric chromatin at the inner plate of the
CC kinetochore. The presence of CENPA subtly modifies the nucleosome
CC structure and the way DNA is wrapped around the nucleosome and gives
CC rise to protruding DNA ends that are less well-ordered and rigid
CC compared to nucleosomes containing histone H3. May serve as an
CC epigenetic mark that propagates centromere identity through replication
CC and cell division. Required for recruitment and assembly of kinetochore
CC proteins, and as a consequence required for progress through mitosis,
CC chromosome segregation and cytokinesis. {ECO:0000250|UniProtKB:P49450}.
CC -!- SUBUNIT: Component of centromeric nucleosomes, where DNA is wrapped
CC around a histone octamer core. The octamer contains two molecules each
CC of H2A, H2B, CENPA and H4 assembled in one CENPA-H4 heterotetramer and
CC two H2A-H2B heterodimers. CENPA modulates the DNA-binding
CC characteristics of nucleosomes so that protruding DNA ends have higher
CC flexibility than in nucleosomes containing conventional histone H3.
CC Inhibits binding of histone H1 to nucleosomes, since histone H1 binds
CC preferentially to rigid DNA linkers that protrude from nucleosomes.
CC Nucleosomes containing CENPA also contain histone H2A variants such as
CC MACROH2A and H2A.Z/H2AZ1. The CENPA-H4 heterotetramer is more compact
CC and structurally more rigid than corresponding H3-H4 heterotetramers.
CC Can assemble into nucleosomes that contain both CENPA and histone H3.3;
CC these nucleosomes interact with a single CENPC chain. Heterotrimer
CC composed of HJURP, CENPA and histone H4, where HJURP interacts with the
CC dimer formed by CENPA and histone H4 and prevents tetramerization of
CC CENPA and H4. Component of the CENPA-NAC complex, at least composed of
CC CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. Interacts (via CATD
CC domain) with HJURP; the interaction is direct and is required for its
CC localization to centromeres. Interacts with CENPC, CENPN and CENPT;
CC interaction is direct. Part of a centromere complex consisting of
CC CENPA, CENPT and CENPW. Identified in centromere complexes containing
CC histones H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT,
CC CENPN, HJURP, SUPT16H, SSRP1 and RSF1. Can self-associate. The CENPA-H4
CC heterotetramer can bind DNA by itself (in vitro). Interacts with CDK1,
CC PPP1CA and RBBP7. {ECO:0000250|UniProtKB:P49450}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49450}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P49450}.
CC Chromosome, centromere {ECO:0000250|UniProtKB:P49450}. Note=Localizes
CC exclusively in the kinetochore domain of centromeres. Occupies a
CC compact domain at the inner kinetochore plate stretching across 2
CC thirds of the length of the constriction but encompassing only one
CC third of the constriction width and height.
CC {ECO:0000250|UniProtKB:P49450}.
CC -!- DOMAIN: The CATD (CENPA targeting domain) region is responsible for the
CC more compact structure of nucleosomes containing CENPA. It is necessary
CC and sufficient to mediate the localization into centromeres.
CC {ECO:0000250|UniProtKB:P49450}.
CC -!- PTM: Trimethylated by NTMT1 at the N-terminal glycine after cleavage of
CC Met-1. Methylation is low before incorporation into nucleosomes and
CC increases with cell cycle progression, with the highest levels in
CC mitotic nucleosomes. {ECO:0000250|UniProtKB:P49450}.
CC -!- PTM: Poly-ADP-ribosylated by PARP1. {ECO:0000250|UniProtKB:O35216}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR EMBL; CB455530; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U14519; AAA57417.1; -; mRNA.
DR PIR; I46071; I46071.
DR AlphaFoldDB; P49449; -.
DR SMR; P49449; -.
DR STRING; 9913.ENSBTAP00000032858; -.
DR PaxDb; P49449; -.
DR PRIDE; P49449; -.
DR eggNOG; KOG1745; Eukaryota.
DR InParanoid; P49449; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 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 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 ADP-ribosylation; Centromere; Chromosome; Direct protein sequencing;
KW DNA-binding; Kinetochore; Methylation; Nucleosome core; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49450"
FT CHAIN 2..138
FT /note="Histone H3-like centromeric protein A"
FT /id="PRO_0000221372"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..52
FT /note="Important for flexibility of DNA ends that protrude
FT from nucleosomes"
FT /evidence="ECO:0000250|UniProtKB:P49450"
FT REGION 39..138
FT /note="H3-like"
FT REGION 73..114
FT /note="CATD"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine"
FT /evidence="ECO:0000250|UniProtKB:P49450"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49450"
SQ SEQUENCE 138 AA; 15678 MW; 56E551F0697AC4A3 CRC64;
MGPRRQKRKP ETPRRRPASP APAAPRPTPS LGTSSRPLAR RRHTVLKEIR TLQKTTHLLL
RKSPFCRLAR EICVQFTRGV DFNWQAQALL ALQEAAEAFL VHLFEDAYLL SLHAGRVTLF
PKDVQLARRI RGIQEGLG
