CFDP1_BOVIN
ID CFDP1_BOVIN Reviewed; 297 AA.
AC Q8HXY9; Q2KIY4; Q8I031; Q8I033;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Craniofacial development protein 1;
DE AltName: Full=Bucentaur;
DE AltName: Full=h-type BCNT protein;
GN Name=CFDP1;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), TISSUE
RP SPECIFICITY, AND GENE DUPLICATION.
RC STRAIN=Jersey; TISSUE=Kidney;
RX PubMed=12832649; DOI=10.1093/molbev/msg168;
RA Iwashita S., Osada N., Itoh T., Sezaki M., Oshima K., Hashimoto E.,
RA Kitagawa-Arita Y., Takahashi I., Masui T., Hashimoto K., Makalowski W.;
RT "A transposable element-mediated gene divergence that directly produces a
RT novel type bovine Bcnt protein including the endonuclease domain of RTE-
RT 1.";
RL Mol. Biol. Evol. 20:1556-1563(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role during embryogenesis. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8HXY9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8HXY9-2; Sequence=VSP_016241;
CC -!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:12832649}.
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11952.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB081003; BAC11952.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AB081004; BAC11953.1; -; mRNA.
DR EMBL; AB081095; BAC15593.1; -; Genomic_DNA.
DR EMBL; BC112462; AAI12463.1; -; mRNA.
DR RefSeq; NP_776693.1; NM_174268.1. [Q8HXY9-1]
DR AlphaFoldDB; Q8HXY9; -.
DR STRING; 9913.ENSBTAP00000020504; -.
DR PaxDb; Q8HXY9; -.
DR PeptideAtlas; Q8HXY9; -.
DR PRIDE; Q8HXY9; -.
DR Ensembl; ENSBTAT00000072376; ENSBTAP00000069228; ENSBTAG00000015427. [Q8HXY9-1]
DR GeneID; 281682; -.
DR KEGG; bta:281682; -.
DR CTD; 10428; -.
DR VEuPathDB; HostDB:ENSBTAG00000015427; -.
DR eggNOG; KOG4776; Eukaryota.
DR GeneTree; ENSGT00390000018141; -.
DR HOGENOM; CLU_080190_0_0_1; -.
DR InParanoid; Q8HXY9; -.
DR OMA; LDWAAYV; -.
DR OrthoDB; 1372508at2759; -.
DR TreeFam; TF313182; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000015427; Expressed in dorsal thalamus and 104 other tissues.
DR ExpressionAtlas; Q8HXY9; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0044346; P:fibroblast apoptotic process; IEA:Ensembl.
DR GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
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 Alternative splicing; Developmental protein; Isopeptide bond; Methylation;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..297
FT /note="Craniofacial development protein 1"
FT /id="PRO_0000212491"
FT DOMAIN 216..297
FT /note="BCNT-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00610"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..215
FT /note="Hydrophilic"
FT REGION 190..222
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 90..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75UQ2"
FT MOD_RES 84
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 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT MOD_RES 217
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT VAR_SEQ 216..297
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12832649, ECO:0000303|Ref.2"
FT /id="VSP_016241"
SQ SEQUENCE 297 AA; 33355 MW; D4A944BC8740373C CRC64;
MEEFDSEDFS TSEEDEDYVP SGGEYSEDDI NELVKEDEVD GEEETQKTKG TKRKAESVLA
RKRKQGGLSL EEDEEDANEE SGGSSSEEED AATEQQKGVE SEDARKKKED ELWASFLNDV
GPKSKVPPST HVKTGEETEE TSSSHLVKAE RLEKPKETEK VKITKVFDFA GEEVRVIKEV
DATSKEAKSF FKQNEKEKPQ SNVPPAVPSL PAGSGLKRSS GMSSLLGKIG AKKQKMSTLE
KSKLDWESFK EEEGIGEELA IHNRGKEGYI ERKAFLDRVD HRQFEIERDL RLSKMKP
