CEBP_DROME
ID CEBP_DROME Reviewed; 449 AA.
AC Q02637; Q9W183;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=CCAAT/enhancer-binding protein;
DE Short=C/EBP;
DE AltName: Full=Slow border cell protein;
GN Name=slbo; ORFNames=CG4354;
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 [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=1394432; DOI=10.1016/0092-8674(92)90265-e;
RA Montell D.J., Rorth P., Spradling A.C.;
RT "Slow border cells, a locus required for a developmentally regulated cell
RT migration during oogenesis, encodes Drosophila C/EBP.";
RL Cell 71:51-62(1992).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=1459454; DOI=10.1101/gad.6.12a.2299;
RA Rorth P., Montell D.J.;
RT "Drosophila C/EBP: a tissue-specific DNA-binding protein required for
RT embryonic development.";
RL Genes Dev. 6:2299-2311(1992).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND UBIQUITINATION.
RX PubMed=10949024; DOI=10.1016/s1097-2765(05)00008-0;
RA Roerth P., Szabo K., Texido G.;
RT "The level of C/EBP protein is critical for cell migration during
RT Drosophila oogenesis and is tightly controlled by regulated degradation.";
RL Mol. Cell 6:23-30(2000).
RN [7]
RP FUNCTION, AND INTERACTION WITH TRBL.
RX PubMed=23305818; DOI=10.1016/j.ydbio.2012.12.016;
RA Masoner V., Das R., Pence L., Anand G., LaFerriere H., Zars T., Bouyain S.,
RA Dobens L.L.;
RT "The kinase domain of Drosophila Tribbles is required for turnover of fly
RT C/EBP during cell migration.";
RL Dev. Biol. 375:33-44(2013).
CC -!- FUNCTION: Required for the expression of gene products mediating border
CC cell migration (PubMed:1459454, PubMed:10949024, PubMed:23305818).
CC Among the DNA sequences that this protein binds with high affinity is a
CC conserved site within the promoter of its gene (PubMed:1459454).
CC {ECO:0000269|PubMed:10949024, ECO:0000269|PubMed:1459454,
CC ECO:0000269|PubMed:23305818}.
CC -!- SUBUNIT: Binds DNA as a dimer and can form stable heterodimers
CC (PubMed:1459454). Interacts with trbl (PubMed:23305818).
CC {ECO:0000269|PubMed:1459454, ECO:0000269|PubMed:23305818}.
CC -!- INTERACTION:
CC Q02637; Q9NIR3: crc; NbExp=2; IntAct=EBI-158748, EBI-15108419;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1459454}.
CC -!- DEVELOPMENTAL STAGE: At stage 9 detected in centrally located anterior
CC polar cells, and in border cells before and as they migrate (at protein
CC level). At stage 10, detected in centripetal cells and levels decrease
CC in border cells as they finish migrating (at protein level).
CC {ECO:0000269|PubMed:10949024}.
CC -!- PTM: Ubiquitination/deubiquitination regulates border cell migration.
CC Ubiquitination is stimulated by trbl, which leads to proteasomal
CC degradation and inhibits border cell migration. Deubiquitination by
CC Usp47, leads to its stabilization and promotes border cell migration.
CC {ECO:0000269|PubMed:10949024}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR EMBL; L00632; AAA28415.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF47194.1; -; Genomic_DNA.
DR EMBL; BT009992; AAQ22461.1; -; mRNA.
DR PIR; A43481; A43481.
DR RefSeq; NP_001286836.1; NM_001299907.1.
DR RefSeq; NP_523843.1; NM_079119.3.
DR AlphaFoldDB; Q02637; -.
DR SMR; Q02637; -.
DR BioGRID; 63463; 25.
DR IntAct; Q02637; 7.
DR STRING; 7227.FBpp0072179; -.
DR PaxDb; Q02637; -.
DR DNASU; 37889; -.
DR EnsemblMetazoa; FBtr0072272; FBpp0072179; FBgn0005638.
DR EnsemblMetazoa; FBtr0339359; FBpp0308452; FBgn0005638.
DR GeneID; 37889; -.
DR KEGG; dme:Dmel_CG4354; -.
DR CTD; 37889; -.
DR FlyBase; FBgn0005638; slbo.
DR VEuPathDB; VectorBase:FBgn0005638; -.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000171291; -.
DR HOGENOM; CLU_043327_3_1_1; -.
DR InParanoid; Q02637; -.
DR OMA; QQHRKHS; -.
DR OrthoDB; 1160648at2759; -.
DR PhylomeDB; Q02637; -.
DR Reactome; R-DME-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-DME-9616222; Transcriptional regulation of granulopoiesis.
DR SignaLink; Q02637; -.
DR BioGRID-ORCS; 37889; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37889; -.
DR PRO; PR:Q02637; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0005638; Expressed in embryonic epidermis (Drosophila) and 16 other tissues.
DR ExpressionAtlas; Q02637; baseline and differential.
DR Genevisible; Q02637; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..449
FT /note="CCAAT/enhancer-binding protein"
FT /id="PRO_0000076631"
FT DOMAIN 363..426
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 211..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..396
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 398..405
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 211..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 45..48
FT /note="Missing (in Ref. 1; AAA28415)"
FT /evidence="ECO:0000305"
FT CONFLICT 167..175
FT /note="PPSGMVSAA -> RRANGLGG (in Ref. 1; AAA28415)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 49420 MW; 6E56D7246C83C34C CRC64;
MLNMESPQMY ADAVQTLAQL DLKKEPPLQQ ATIGQITLTA MSTAQQQQQQ QQQQQQQQQQ
QQQQQQQQPQ QQTTDANNNT SQDAALLVKQ HAMHQMQQVA ALGSNNNLLQ KQMLQQYSTQ
TDLDELTTQE ITLDLQHLID DQFRDTETLG IFSDMVTSPG GLSATLPPSG MVSAAAKVLQ
QQTLRNQHGY GGRGGGGGAG GALAYMPQPV HATYNNSSDE NSSVGSDSST IKEEPIDPEY
RRHLQEAASQ QAAFMGNGAG LYNGYGSGAN GLTGGGNPLN GGNTTPSSNG SNGSTGSSNG
SQFTNLTTAN VLAHHNLPHL AAAAGAHNLL KQHSKLHAQQ QHQQHQQQQQ HRKHSNKHVD
KGTDEYRRRR ERNNIAVRKS REKAKVRSRE VEERVKSLLK EKDALIRQLG EMTNELQLHK
QIYMQLMNHA NPEVSRVCRS FLNTNEHSL
