ID   CFDP1_TRAJA             Reviewed;         298 AA.
AC   Q60FC2; Q588U7; Q867A5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Craniofacial development protein 1;
DE   AltName: Full=Bucentaur;
DE   AltName: Full=h-type BCNT protein;
GN   Name=CFDP1;
OS   Tragulus javanicus (Lesser Malay chevrotain) (Lesser mouse deer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Tragulina; Tragulidae;
OC   Tragulus.
OX   NCBI_TaxID=9849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RA   Ueno S., Kimura J., Kurohmaru M., Fukuta K., Iwashita S.;
RT   "Gene organization of the chevrotain bcnt whose paralogue in ruminantia
RT   includes an endonuclease domain of RTE-1 in the protein.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Ueno S., Nakashima K., Osada N., Kubo Y., Ohshima K., Tanaka K., Endo H.,
RA   Kimura J., Kurohmaru M., Fukuta K., David L., Iwashita S.;
RT   "The diversification of the paralogous Bcnt gene in ruminants was
RT   accompanied by the recruitment of an endonuclease domain from a
RT   retrotransposable element-1.";
RL   Submitted (OCT-2004) 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}.
CC   -!- MISCELLANEOUS: Gene duplication of the ancestral BCNT gene leads to the
CC       h-type BCNT (CFDP1) gene and the p97BCNT (CFDP2) gene. The latter
CC       contains a region derived from the endonuclease domain of a
CC       retrotransposable element RTE-1. This repetitive sequence associated
CC       with the BCNT gene is specific to Ruminantia.
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DR   EMBL; AB103377; BAC57061.1; -; Genomic_DNA.
DR   EMBL; AB192410; BAD93709.1; -; Genomic_DNA.
DR   EMBL; AB192411; BAD60811.1; -; mRNA.
DR   AlphaFoldDB; Q60FC2; -.
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_0000212498"
FT   DOMAIN          217..298
FT                   /note="BCNT-C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00610"
FT   REGION          1..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..216
FT                   /note="Hydrophilic"
FT   REGION          179..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..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..196
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         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   CROSSLNK        149
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT   CONFLICT        92
FT                   /note="T -> A (in Ref. 1; BAD93709)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        207
FT                   /note="A -> T (in Ref. 1; BAD93709)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   298 AA;  33610 MW;  DCD363E773A950BB CRC64;
     MEEFDSEDFS TSEEDEDYVP SGGEYSEDDI NELVKEDEVD VEEETHIIKG TKRKAERFMP
     RKRKQGGLSL EEEDEEDAGR ESGGSGSEEE DTATEQEEGT ESEDARKKKE DELWASFLND
     VGPKSKVPPS TPVKTGEETE ETSSSNLVKA EEQEKPKETE KVKITKVFDF AGEEVRVTKE
     VDPTSKEAKS FFKQSEKEKP QPNVPSAVSS LPAGSGLKRS SGMSSLLGKI GAKKQKMSTL
     EKSKLDWENF KEEEGIAEEL AIHNRGKEGY IERKAFLDRV DHRQFEIERD LRLSKMKP