ID   CENPB_SHEEP             Reviewed;         239 AA.
AC   P49451;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Major centromere autoantigen B;
DE   AltName: Full=Centromere protein B;
DE            Short=CENP-B;
DE   Flags: Fragment;
GN   Name=CENPB;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=8893808; DOI=10.1159/000134388;
RA   Burkin D.J., Jones C.A., Burkin H.R., McGrew J.A., Broad T.E.;
RT   "Sheep CENPB and CENPC genes show a high level of sequence similarity and
RT   conserved synteny with their human homologs.";
RL   Cytogenet. Cell Genet. 74:86-89(1996).
CC   -!- FUNCTION: Interacts with centromeric heterochromatin in chromosomes and
CC       binds to a specific 17 bp subset of alphoid satellite DNA, called the
CC       CENP-B box. May organize arrays of centromere satellite DNA into a
CC       higher-order structure which then directs centromere formation and
CC       kinetochore assembly in mammalian chromosomes.
CC       {ECO:0000250|UniProtKB:P07199}.
CC   -!- SUBUNIT: Antiparallel homodimer. Interacts with CENPT. Identified in a
CC       centromere complex containing histones H2A, H2B and H4, and at least
CC       CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1.
CC       {ECO:0000250|UniProtKB:P07199}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07199}.
CC       Chromosome, centromere {ECO:0000250|UniProtKB:P07199}.
CC   -!- PTM: Poly-ADP-ribosylated by PARP1. {ECO:0000250|UniProtKB:P27790}.
CC   -!- PTM: N-terminally methylated by METTL11A/NTM1. Alpha-N-methylation is
CC       stimulated in response extracellular stimuli, including increased cell
CC       density and heat shock, and seems to facilitate binding to CENP-B
CC       boxes. Chromatin-bound CENP-B is primarily trimethylated (By
CC       similarity). {ECO:0000250|UniProtKB:P07199}.
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DR   EMBL; U35655; AAA79098.1; -; mRNA.
DR   AlphaFoldDB; P49451; -.
DR   SMR; P49451; -.
DR   STRING; 9940.ENSOARP00000005057; -.
DR   eggNOG; KOG3105; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003696; F:satellite DNA binding; IEA:InterPro.
DR   Gene3D; 1.10.287.1090; -; 1.
DR   InterPro; IPR033062; CENP-B.
DR   InterPro; IPR015115; CenpB_C.
DR   InterPro; IPR034882; Dimerisation_CENP-B_sf.
DR   PANTHER; PTHR19303:SF25; PTHR19303:SF25; 1.
DR   Pfam; PF09026; CENP-B_dimeris; 1.
DR   SUPFAM; SSF101160; SSF101160; 1.
PE   2: Evidence at transcript level;
KW   ADP-ribosylation; Centromere; Chromosome; DNA-binding; Methylation;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           <1..239
FT                   /note="Major centromere autoantigen B"
FT                   /id="PRO_0000126127"
FT   REGION          28..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..239
FT                   /note="Homodimerization"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        45..113
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..181
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         37
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P07199"
FT   MOD_RES         39
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P07199"
FT   NON_TER         1
SQ   SEQUENCE   239 AA;  26436 MW;  259C6C72E7D9C135 CRC64;
     LGLMEVHFVA AAWQAVEPSD IAVCFREAGF GGGPNATITT ALKSEGEEEE EEEEEEEEEE
     GEGEEEEEED GEEEEEAGEG EELGEEEEVE EEGDVDTVEE EEEEEEESSS EGLEAEDWAQ
     GVVEAGGSFG GYGAQEEAQC PTLHFLEGEE DSESDSEEEE EDDDEDEDDE DDEEEDDEVP
     VPSFGEAMAY FAMVKRYLTS SPIDDRVQSH ILHLEHDLVH VTRKNHARQA GARGLGHQS