CFDP1_RAT
ID CFDP1_RAT Reviewed; 295 AA.
AC Q75UQ2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Craniofacial development protein 1;
DE AltName: Full=Bucentaur;
GN Name=Cfdp1; Synonyms=Bcnt;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Head;
RA Nakashima K., Kubo Y., Iwashita S.;
RT "Diversity and analysis of novel type protein with interspersed repeated
RT sequence region.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-83 AND SER-84, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May play a role during embryogenesis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q9UEE9}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB125856; BAD01499.1; -; mRNA.
DR EMBL; BC067246; AAH67246.1; -; mRNA.
DR RefSeq; NP_955410.1; NM_199378.3.
DR AlphaFoldDB; Q75UQ2; -.
DR SMR; Q75UQ2; -.
DR STRING; 10116.ENSRNOP00000026249; -.
DR iPTMnet; Q75UQ2; -.
DR PhosphoSitePlus; Q75UQ2; -.
DR jPOST; Q75UQ2; -.
DR PaxDb; Q75UQ2; -.
DR PRIDE; Q75UQ2; -.
DR Ensembl; ENSRNOT00000112483; ENSRNOP00000083789; ENSRNOG00000019326.
DR GeneID; 292027; -.
DR KEGG; rno:292027; -.
DR UCSC; RGD:735080; rat.
DR CTD; 10428; -.
DR RGD; 735080; Cfdp1.
DR eggNOG; KOG4776; Eukaryota.
DR GeneTree; ENSGT00390000018141; -.
DR HOGENOM; CLU_080190_0_0_1; -.
DR InParanoid; Q75UQ2; -.
DR OMA; LDWAAYV; -.
DR OrthoDB; 1372508at2759; -.
DR PhylomeDB; Q75UQ2; -.
DR TreeFam; TF313182; -.
DR PRO; PR:Q75UQ2; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000019326; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; Q75UQ2; baseline and differential.
DR Genevisible; Q75UQ2; RN.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
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 1: Evidence at protein level;
KW Centromere; Chromosome; Developmental protein; Isopeptide bond;
KW Kinetochore; Methylation; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..295
FT /note="Craniofacial development protein 1"
FT /id="PRO_0000212497"
FT DOMAIN 214..295
FT /note="BCNT-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00610"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..213
FT /note="Hydrophilic"
FT REGION 188..219
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 71..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT MOD_RES 215
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
SQ SEQUENCE 295 AA; 32969 MW; 60F604F3BCED5885 CRC64;
MEEFDSEDFS TSDEDEDYVP SGGEYSEDDV NELVKEDEVD GEEQAEKTKG KRRKAQSIPA
RKRKQSGLLL DEEEDGEEDS GGSSREEDEE EQEGGLGSET SRKKKEDELW ASFLNDVGTK
SKAASSSQVK VAEETEETSS SKPLVKADEL EKPKESEKVK ITKVFDFAGE EVRVTKEVDA
TSKEAKSFLK QTEKEKPQAL VTSAATPPPA GSGIKRTSGM SSLLGKIGAK KQKMSTLEKS
KLDWESFKEE EGIGEELAIH NRGKEGYIER KAFLERVDHR QFEIERDLRL SKMKP
