CORTO_DROME
ID CORTO_DROME Reviewed; 550 AA.
AC P41046; Q24271; Q494K5; Q961I6; Q9VN76;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Centrosomal and chromosomal factor;
DE Short=CCF;
DE AltName: Full=Chromocentrosomin;
GN Name=corto; Synonyms=ccf; ORFNames=CG2530;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Oregon-R;
RX PubMed=9463384; DOI=10.1093/emboj/17.4.1063;
RA Kodjabachian L., Delaage M., Maurel C., Miassod R., Jacq B., Rosset R.;
RT "Mutations in ccf, a novel Drosophila gene encoding a chromosomal factor,
RT affect progression through mitosis and interact with Pc-G mutations.";
RL EMBO J. 17:1063-1075(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RA Takamura C., Imamura Y., Taira T., Iguchi-Ariga S., Ariga H.;
RT "Drosophila melanogaster cDNA which encodes a protein stimulating
RT transcription based on human CAAT motif.";
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-550.
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP INTERACTION WITH ESC; TRL; E(Z); SCM AND PH-P, IDENTIFICATION IN A COMPLEX
RP WITH PC, HOMODIMERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=12771214; DOI=10.1093/nar/gkg381;
RA Salvaing J., Lopez A., Boivin A., Deutsch J.S., Peronnet F.;
RT "The Drosophila Corto protein interacts with Polycomb-group proteins and
RT the GAGA factor.";
RL Nucleic Acids Res. 31:2873-2882(2003).
RN [8]
RP FUNCTION.
RX PubMed=18667003; DOI=10.1111/j.0018-0661.2008.02067.x;
RA Salvaing J., Mouchel-Vielh E., Bloyer S., Preiss A., Peronnet F.;
RT "Regulation of Abd-B expression by Cyclin G and Corto in the abdominal
RT epithelium of Drosophila.";
RL Hereditas 145:138-146(2008).
RN [9]
RP FUNCTION, INTERACTION WITH CYCG, AND SUBCELLULAR LOCATION.
RX PubMed=18286205; DOI=10.1371/journal.pone.0001658;
RA Salvaing J., Nagel A.C., Mouchel-Vielh E., Bloyer S., Maier D., Preiss A.,
RA Peronnet F.;
RT "The enhancer of trithorax and polycomb corto interacts with cyclin G in
RT Drosophila.";
RL PLoS ONE 3:E1658-E1658(2008).
CC -!- FUNCTION: Essential protein required for proper condensation of mitotic
CC chromosomes and progression through mitosis (PubMed:9463384). Binds to
CC specific polytene chromosome sites, many of which are shared with the
CC posterior sex combs (Psc) protein (PubMed:9463384). Involved in
CC maintaining Abd-B repression outside its normal expression domain
CC (PubMed:18667003, PubMed:18286205). {ECO:0000269|PubMed:18286205,
CC ECO:0000269|PubMed:18667003, ECO:0000269|PubMed:9463384}.
CC -!- SUBUNIT: Homodimer (PubMed:12771214). Interacts with esc, Trl, E(z),
CC scm and ph-p in vitro (PubMed:12771214). Found in vivo in an esc-
CC containing complex, which may be the Esc/E(z) complex
CC (PubMed:12771214). Also found in vivo in a Pc-containing complex that
CC may be the PRC1 complex, but does not interact with Pc directly
CC (PubMed:12771214). Interacts with cyclin CycG (PubMed:18286205).
CC {ECO:0000269|PubMed:12771214, ECO:0000269|PubMed:18286205}.
CC -!- INTERACTION:
CC P41046; P41046: corto; NbExp=2; IntAct=EBI-300379, EBI-300379;
CC P41046; P42124: E(z); NbExp=2; IntAct=EBI-300379, EBI-112315;
CC P41046; Q24338: esc; NbExp=3; IntAct=EBI-300379, EBI-88911;
CC P41046; P39769: ph-p; NbExp=2; IntAct=EBI-300379, EBI-300360;
CC P41046; Q9VHA0: Scm; NbExp=2; IntAct=EBI-300379, EBI-89256;
CC P41046; Q08605: Trl; NbExp=2; IntAct=EBI-300379, EBI-300317;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9463384}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:9463384}. Chromosome {ECO:0000269|PubMed:12771214,
CC ECO:0000269|PubMed:18286205}.
CC -!- DEVELOPMENTAL STAGE: Expressed during oogenesis, embryonic and larval
CC stages.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK92993.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA07853.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U35074; AAC13917.1; -; mRNA.
DR EMBL; D43795; BAA07853.1; ALT_FRAME; mRNA.
DR EMBL; AE014297; AAF52073.1; -; Genomic_DNA.
DR EMBL; BT023771; AAZ41779.1; -; mRNA.
DR EMBL; AY051569; AAK92993.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001246921.1; NM_001259992.2.
DR RefSeq; NP_001246922.1; NM_001259993.3.
DR RefSeq; NP_001246923.1; NM_001259994.2.
DR RefSeq; NP_001287166.1; NM_001300237.1.
DR RefSeq; NP_524231.2; NM_079507.4.
DR AlphaFoldDB; P41046; -.
DR BioGRID; 65830; 24.
DR DIP; DIP-22699N; -.
DR IntAct; P41046; 6.
DR STRING; 7227.FBpp0300441; -.
DR PaxDb; P41046; -.
DR DNASU; 40616; -.
DR EnsemblMetazoa; FBtr0078844; FBpp0078485; FBgn0010313.
DR EnsemblMetazoa; FBtr0308118; FBpp0300440; FBgn0010313.
DR EnsemblMetazoa; FBtr0308119; FBpp0300441; FBgn0010313.
DR EnsemblMetazoa; FBtr0308120; FBpp0300442; FBgn0010313.
DR EnsemblMetazoa; FBtr0345141; FBpp0311362; FBgn0010313.
DR GeneID; 40616; -.
DR KEGG; dme:Dmel_CG2530; -.
DR CTD; 40616; -.
DR FlyBase; FBgn0010313; corto.
DR VEuPathDB; VectorBase:FBgn0010313; -.
DR eggNOG; ENOG502S1QD; Eukaryota.
DR HOGENOM; CLU_465608_0_0_1; -.
DR InParanoid; P41046; -.
DR OMA; ELPNQPK; -.
DR OrthoDB; 1548184at2759; -.
DR PhylomeDB; P41046; -.
DR SignaLink; P41046; -.
DR BioGRID-ORCS; 40616; 0 hits in 1 CRISPR screen.
DR ChiTaRS; corto; fly.
DR GenomeRNAi; 40616; -.
DR PRO; PR:P41046; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0010313; Expressed in cleaving embryo and 57 other tissues.
DR ExpressionAtlas; P41046; baseline and differential.
DR Genevisible; P41046; DM.
DR GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0035098; C:ESC/E(Z) complex; IPI:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; IPI:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060429; P:epithelium development; IGI:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IC:UniProtKB.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:FlyBase.
DR GO; GO:0010468; P:regulation of gene expression; IDA:FlyBase.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; DNA-binding; Mitosis; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..550
FT /note="Centrosomal and chromosomal factor"
FT /id="PRO_0000079256"
FT REGION 21..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 20..44
FT /evidence="ECO:0000255"
FT COILED 105..126
FT /evidence="ECO:0000255"
FT COILED 239..274
FT /evidence="ECO:0000255"
FT COMPBIAS 21..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 134
FT /note="A -> T (in Ref. 1; AAC13917)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..372
FT /note="GA -> EQ (in Ref. 1; AAC13917)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 58771 MW; 41D79F0A107A582D CRC64;
MTMAACYANY DMSSLSHGMS ALSALQQQQQ QQQQQHSQTQ QQHHHQQQQQ HMYHAAVAAH
QQQLLQQQQQ QQHHRHHHQP ANTSSSSNSR HSHAAATQTQ VAAAVANSRQ QQQQQQQQQQ
QQQQQQTASS NSNAAPAPSP QKDYSIPLHV DCSVEYELPN QPKPPAGQRV EPLLMIHPCY
FRKMESQRRS PFVNNMHATA RAVSSSSLSS GAALGGGGSG AAVATAPSSS AARRGARAAT
SAQQQQQQQQ RYQQQQQQLR QQHQQMSQMS QQAHYPQQQS SLVRQHQQQQ QQQQQQQRAS
SNQSQRQSQS QSQSQSHAAN SAAAAAAQAS IAAAAAGQWD QLAALAARTA LTPHHMLHPH
SHYAAKGSGG GAGGGKRDAM ISGSYGQTAV ASGKLQQSQV QQQQPQQQQQ HCLPPPPWDA
TSMLMDRSPM ATVPSNYQAG PDTNPMRLYS ATPTAGAASG GSASVGGGGA VSGAGATGAV
NTATDKLSGK YRQYLRSQRM HPYAAAASLN LAAAAAAAGQ TSFVPFSSAA TAVAATPTFQ
HLPQISCYNV
