CENPC_SHEEP
ID CENPC_SHEEP Reviewed; 402 AA.
AC P49453;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Centromere protein C;
DE Short=CENP-C;
DE AltName: Full=Centromere autoantigen C;
DE AltName: Full=Centromere protein C 1;
DE Short=CENP-C 1;
DE Flags: Fragment;
GN Name=CENPC; Synonyms=CENPC1;
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: Component of the CENPA-NAC (nucleosome-associated) complex, a
CC complex that plays a central role in assembly of kinetochore proteins,
CC mitotic progression and chromosome segregation. The CENPA-NAC complex
CC recruits the CENPA-CAD (nucleosome distal) complex and may be involved
CC in incorporation of newly synthesized CENPA into centromeres. CENPC
CC recruits DNA methylation and DNMT3B to both centromeric and
CC pericentromeric satellite repeats and regulates the histone code in
CC these regions. {ECO:0000250|UniProtKB:Q03188}.
CC -!- SUBUNIT: Oligomer. Component of the CENPA-NAC complex, at least
CC composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The
CC CENPA-NAC complex interacts with the CENPA-CAD complex, composed of
CC CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Binds to
CC DAXX. Interacts with DNMT3B. Interacts directly with CENPA. Identified
CC in a centromere complex containing histones H2A, H2B and H4, and at
CC least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1
CC (By similarity). Interacts with MEIKIN (By similarity).
CC {ECO:0000250|UniProtKB:P49452, ECO:0000250|UniProtKB:Q03188}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03188}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q03188}.
CC Chromosome, centromere {ECO:0000250|UniProtKB:Q03188}. Note=Localizes
CC exclusively in the kinetochore domain of centromeres.
CC {ECO:0000250|UniProtKB:Q03188}.
CC -!- DOMAIN: The MIF2 homology domain II targets centromeres and binds the
CC alpha satellite DNA in vivo. The MIF2 homology domain III can induce
CC CENPC dimerization/oligomerization. {ECO:0000250|UniProtKB:P49452}.
CC -!- SIMILARITY: Belongs to the CENP-C/MIF2 family. {ECO:0000305}.
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DR EMBL; U35657; AAA79099.1; -; mRNA.
DR AlphaFoldDB; P49453; -.
DR SMR; P49453; -.
DR STRING; 9940.ENSOARP00000007315; -.
DR PRIDE; P49453; -.
DR eggNOG; ENOG502RYQH; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005721; C:pericentric heterochromatin; ISS:UniProtKB.
DR GO; GO:0019237; F:centromeric DNA binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0051382; P:kinetochore assembly; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR028386; CENP-C/Mif2/cnp3.
DR InterPro; IPR025974; Mif2/CENP-C_cupin.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR16684; PTHR16684; 1.
DR Pfam; PF11699; CENP-C_C; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; DNA-binding;
KW Isopeptide bond; Kinetochore; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN <1..402
FT /note="Centromere protein C"
FT /id="PRO_0000089476"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..218
FT /note="MIF2 homology domain II"
FT /evidence="ECO:0000250"
FT REGION 349..402
FT /note="MIF2 homology domain III"
FT /evidence="ECO:0000250"
FT MOTIF 25..42
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 239..257
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03188"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q03188"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03188"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03188"
FT CROSSLNK 1
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03188"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03188"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03188"
FT NON_TER 1
SQ SEQUENCE 402 AA; 45065 MW; 9EA59F16C3EA89AB CRC64;
KSEQSSFSSS SSVRNELSVY HNSRQKPPAE KTNQSSKNIG KKAAPFKKQK RANKGSSGAQ
VLYAKDSGGA QNESLRSNEA DLAKKKNPNP SGDTGSSKNQ DSMAAQNVHQ KSQMSVETCT
TPSKSNLILE SLGLQFFGRE VTLFRLKNYL TSERHSDVDD NVVQENLNDS RGEIPDSTPE
SKMHHKLVLP SYTPNVRRTM RTRSKPLEYW RGERIDYQAR PSGGFVIGGI LSPDTVSSKR
KAKGNLGRII TTANRKRICL ENAPIKNKFM VNLNIPLGDP LQPTRVKDPE TQETVLMDLI
RPRDTYQFCV EHDELKVYKT LDTPFFSSGK LIIGPLQEKG KQHVGLDTLV FYVNLGYLLC
TLHETPYIVT TGDSFYVPSG NYYNIKNLLN EERVLLFTQI KS
