CFDP1_MUNRE
ID CFDP1_MUNRE Reviewed; 298 AA.
AC Q4ADK4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Craniofacial development protein 1;
DE AltName: Full=Bucentaur;
GN Name=CFDP1; Synonyms=BCNT;
OS Muntiacus reevesi (Reeves' muntjac) (Cervus reevesi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Muntiacinae; Muntiacus.
OX NCBI_TaxID=9886;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RA Iwashita S., Kimura J., Fukuta K.;
RT "Gene organization of bcnt and p97bcnt genes.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role during embryogenesis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q9UEE9}.
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DR EMBL; AB213485; BAE19807.1; -; mRNA.
DR AlphaFoldDB; Q4ADK4; -.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR InterPro; IPR011421; BCNT-C.
DR InterPro; IPR027124; Swc5/CFDP1/2.
DR PANTHER; PTHR23227; PTHR23227; 1.
DR Pfam; PF07572; BCNT; 1.
DR PROSITE; PS51279; BCNT_C; 1.
PE 2: Evidence at transcript level;
KW Centromere; Chromosome; Developmental protein; Isopeptide bond;
KW Kinetochore; Methylation; Phosphoprotein; Ubl conjugation.
FT CHAIN 1..298
FT /note="Craniofacial development protein 1"
FT /id="PRO_0000212496"
FT DOMAIN 217..298
FT /note="BCNT-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00610"
FT REGION 1..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..216
FT /note="Hydrophilic"
FT REGION 191..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75UQ2"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75UQ2"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75UQ2"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT MOD_RES 218
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
SQ SEQUENCE 298 AA; 33340 MW; 265074ED68AB90B8 CRC64;
MEEFDSEDFS TSEEDEDYVP SGGEYSEDDI NELVKEDEVD GEEETQKTKG TKRKAESVLA
RKRKQGGLSL EEEGEEDANE ESGGSSSEEE DAATGQEKGI ESEDARKKKE DELWASFLND
VGPKSKVPPS THVKTGEETE ETSSSHLVKA EKLEKPQETE KVKITKVFDF AGEEVRVIKE
VDATSKEAKS FFKQNEKEKP QSNISSSVPS LSAGSGLKRS SGMSSLLGKI GAKKQKMSTL
EKSKLDWESF KEEEGIGEEL AIHNRGKEGY IERKAFLDRV DHRQFEIERD LRLSQMKP