CFDP1_MOUSE
ID CFDP1_MOUSE Reviewed; 295 AA.
AC O88271; O70565; Q9JMA5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Craniofacial development protein 1;
DE AltName: Full=27 kDa craniofacial protein;
DE AltName: Full=Bucentaur;
DE AltName: Full=Protein Cp27;
GN Name=Cfdp1; Synonyms=Bcnt, Cfdp, Cp27;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9602175; DOI=10.1016/s0378-1119(98)00136-x;
RA Takahashi I., Nobukuni T., Ohmori H., Kobayashi M., Tanaka S., Ohshima K.,
RA Okada N., Masui T., Hashimoto K., Iwashita S.;
RT "Existence of a bovine LINE repetitive insert that appears in the cDNA of
RT bovine protein BCNT in ruminant, but not in human, genomes.";
RL Gene 211:387-394(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=10415329; DOI=10.1016/s0378-1119(99)00220-6;
RA Diekwisch T.G.H., Marches F., Williams A., Luan X.;
RT "Cloning, gene expression, and characterization of CP27, a novel gene in
RT mouse embryogenesis.";
RL Gene 235:19-30(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-266.
RC STRAIN=129/SvJ;
RX PubMed=11368901; DOI=10.1016/s0378-1119(01)00422-x;
RA Iwashita S., Itoh T., Takeda H., Sugimoto Y., Takahashi I., Nobukuni T.,
RA Sezaki M., Masui T., Hashimoto K.;
RT "Gene organization of bovine BCNT that contains a portion corresponding to
RT an endonuclease domain derived from an RTE-1 (Bov-B LINE), non-LTR
RT retrotransposable element: duplication of an intramolecular repeat unit
RT downstream of the truncated RTE-1.";
RL Gene 268:59-66(2001).
RN [6]
RP FUNCTION.
RX PubMed=11992732; DOI=10.1016/s0378-1119(01)00868-x;
RA Diekwisch T.G.H., Luan X.;
RT "CP27 function is necessary for cell survival and differentiation during
RT tooth morphogenesis in organ culture.";
RL Gene 287:141-147(2002).
RN [7]
RP FUNCTION.
RX PubMed=12153613; DOI=10.1046/j.1365-2184.2002.00238.x;
RA Luan X., Diekwisch T.G.H.;
RT "CP27 affects viability, proliferation, attachment and gene expression in
RT embryonic fibroblasts.";
RL Cell Prolif. 35:207-219(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND SER-246, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role during embryogenesis. May modulate tooth
CC organogenesis since alterations of this protein function affect tooth
CC organs size as well as individual cell fate and survival. In embryonic
CC cells, blockage of the function results in increased number of
CC apoptotic cells, reduced proliferation, alterations in cell shape and
CC fibronection matrix synthesis. {ECO:0000269|PubMed:10415329,
CC ECO:0000269|PubMed:11992732, ECO:0000269|PubMed:12153613}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q9UEE9}.
CC -!- TISSUE SPECIFICITY: Expressed in lung, liver and heart, with higher
CC expression in teeth. {ECO:0000269|PubMed:10415329}.
CC -!- DEVELOPMENTAL STAGE: Detected at 8 dpc in developing organs, including
CC brain, heart, lung and intestines. Expressed at 14 dpc and 16 dpc at
CC the periphery of developing organs such as bones and teeth.
CC {ECO:0000269|PubMed:10415329}.
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DR EMBL; AB010828; BAA31696.1; -; mRNA.
DR EMBL; Y08219; CAA69396.1; -; mRNA.
DR EMBL; AK160532; BAE35849.1; -; mRNA.
DR EMBL; AK133989; BAE21971.1; -; mRNA.
DR EMBL; BC005589; AAH05589.1; -; mRNA.
DR EMBL; AB033766; BAA94844.1; -; Genomic_DNA.
DR CCDS; CCDS22680.1; -.
DR RefSeq; NP_035931.1; NM_011801.1.
DR AlphaFoldDB; O88271; -.
DR BioGRID; 204753; 1.
DR IntAct; O88271; 1.
DR MINT; O88271; -.
DR STRING; 10090.ENSMUSP00000034432; -.
DR iPTMnet; O88271; -.
DR PhosphoSitePlus; O88271; -.
DR EPD; O88271; -.
DR jPOST; O88271; -.
DR MaxQB; O88271; -.
DR PaxDb; O88271; -.
DR PeptideAtlas; O88271; -.
DR PRIDE; O88271; -.
DR ProteomicsDB; 281115; -.
DR Antibodypedia; 30309; 271 antibodies from 26 providers.
DR DNASU; 23837; -.
DR Ensembl; ENSMUST00000034432; ENSMUSP00000034432; ENSMUSG00000031954.
DR GeneID; 23837; -.
DR KEGG; mmu:23837; -.
DR UCSC; uc009nmx.1; mouse.
DR CTD; 10428; -.
DR MGI; MGI:1344403; Cfdp1.
DR VEuPathDB; HostDB:ENSMUSG00000031954; -.
DR eggNOG; KOG4776; Eukaryota.
DR GeneTree; ENSGT00390000018141; -.
DR HOGENOM; CLU_080190_0_0_1; -.
DR InParanoid; O88271; -.
DR OMA; LDWAAYV; -.
DR OrthoDB; 1372508at2759; -.
DR PhylomeDB; O88271; -.
DR TreeFam; TF313182; -.
DR BioGRID-ORCS; 23837; 18 hits in 72 CRISPR screens.
DR ChiTaRS; Cfdp1; mouse.
DR PRO; PR:O88271; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O88271; protein.
DR Bgee; ENSMUSG00000031954; Expressed in otic placode and 270 other tissues.
DR Genevisible; O88271; MM.
DR GO; GO:0005604; C:basement membrane; TAS:MGI.
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; IDA:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0044346; P:fibroblast apoptotic process; IDA:MGI.
DR GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IDA:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
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_0000212495"
FT DOMAIN 214..295
FT /note="BCNT-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00610"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..213
FT /note="Hydrophilic"
FT REGION 188..217
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 72..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 135..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75UQ2"
FT MOD_RES 83
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 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UEE9"
FT CONFLICT 94
FT /note="G -> A (in Ref. 2; CAA69396)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="K -> E (in Ref. 2; CAA69396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 32921 MW; 245D161EA56F9DB0 CRC64;
MEEFDSEDFS TSDEDEDYLP SGGEYSEDDV NELVKEDEVD GEEQAEKTKG KRRKAQGIPA
RKRKQSGLLL EEEEDGKEDS GGSSSEEDEE EQEGGLGSEN ARKKKEDELW ASFLNDVGPK
SKAAPGSQTK VAEETEEISS NKPLVKADEL DKPRESEKVK ITKVFDFAGE EVRVTKEVDA
ASKEAKSFLK QTEREKPQAL VTSPATPLPA GSGIKRASGM SSLLGKIGAK KQKMSTLEKS
KLDWESFKEE EGIGEELAIH NRGKEGYIER KAFLDRVDHR QFEIERDLRL SKMKP
