ID   CREBA_DROME             Reviewed;         516 AA.
AC   P29747; Q24282; Q64M72; Q8MQX0; Q9VUQ4;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   24-JAN-2024, entry version 192.
DE   RecName: Full=Cyclic AMP response element-binding protein A;
DE            Short=cAMP response element-binding protein A;
DE            Short=dCREB-A;
DE   AltName: Full=Box B-binding factor 2;
DE            Short=BBF-2;
GN   Name=CrebA; Synonyms=Bbbf2; ORFNames=CG7450;
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], AND FUNCTION.
RC   STRAIN=Oregon-R; TISSUE=Embryo;
RX   PubMed=1532159; DOI=10.1101/gad.6.3.466;
RA   Abel T., Bhatt R., Maniatis T.;
RT   "A Drosophila CREB/ATF transcriptional activator binds to both fat
RT   body- and liver-specific regulatory elements.";
RL   Genes Dev. 6:466-480(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
RX   PubMed=1508208; DOI=10.1128/mcb.12.9.4123-4131.1992;
RA   Smolik S.M., Rose T.M., Goodman R.H.;
RT   "A cyclic AMP-responsive element-binding transcriptional activator in
RT   Drosophila melanogaster, dCREB-A, is a member of the leucine zipper
RT   family.";
RL   Mol. Cell. Biol. 12:4123-4131(1992).
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] OF 1-18.
RC   STRAIN=Berkeley; TISSUE=Embryo;
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   [6]
RP   SEQUENCE REVISION.
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-516.
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 (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-79 AND SER-82, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Transcriptional activator. Binds to fat body-specific
CC       enhancers of alcohol dehydrogenase (ADH) and yolk protein genes. BBF-2
CC       may play a role in fat body gene expression. It binds the consensus
CC       sequence 5'-T[AC]NACGTAN[TG]C-3'. {ECO:0000269|PubMed:1508208,
CC       ECO:0000269|PubMed:1532159}.
CC   -!- SUBUNIT: May bind DNA as heterodimers with other bZIP proteins.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: In all cell types examined, including developing
CC       salivary gland in embryos and in adults, brain and optic lobe cell
CC       bodies, salivary gland, midgut epithelial cells of the cardia, female
CC       ovarian columnar follicle cells and male seminal vesicle, ejaculatory
CC       duct, and ejaculatory bulb. {ECO:0000269|PubMed:1508208}.
CC   -!- DEVELOPMENTAL STAGE: Present throughout development.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU21396.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; X64429; CAA45771.1; -; mRNA.
DR   EMBL; M87038; AAA28427.1; -; mRNA.
DR   EMBL; AE014296; AAF49621.2; -; Genomic_DNA.
DR   EMBL; AY122251; AAU21396.1; ALT_SEQ; mRNA.
DR   EMBL; BT011074; AAR82739.1; -; mRNA.
DR   PIR; A42140; A42140.
DR   PIR; A44494; A44494.
DR   RefSeq; NP_524087.3; NM_079363.5.
DR   RefSeq; NP_996096.1; NM_206374.2.
DR   AlphaFoldDB; P29747; -.
DR   SMR; P29747; -.
DR   BioGRID; 65001; 10.
DR   ELM; P29747; -.
DR   IntAct; P29747; 5.
DR   STRING; 7227.FBpp0089339; -.
DR   iPTMnet; P29747; -.
DR   PaxDb; 7227-FBpp0089339; -.
DR   DNASU; 39682; -.
DR   EnsemblMetazoa; FBtr0075557; FBpp0075311; FBgn0004396.
DR   EnsemblMetazoa; FBtr0075558; FBpp0089339; FBgn0004396.
DR   GeneID; 39682; -.
DR   KEGG; dme:Dmel_CG7450; -.
DR   AGR; FB:FBgn0004396; -.
DR   CTD; 39682; -.
DR   FlyBase; FBgn0004396; CrebA.
DR   VEuPathDB; VectorBase:FBgn0004396; -.
DR   eggNOG; KOG0709; Eukaryota.
DR   HOGENOM; CLU_050111_1_0_1; -.
DR   InParanoid; P29747; -.
DR   OMA; MDDECYP; -.
DR   OrthoDB; 3679507at2759; -.
DR   PhylomeDB; P29747; -.
DR   BioGRID-ORCS; 39682; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; CrebA; fly.
DR   GenomeRNAi; 39682; -.
DR   PRO; PR:P29747; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0004396; Expressed in spermathecum and 53 other cell types or tissues.
DR   ExpressionAtlas; P29747; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR   GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR   GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005667; C:transcription regulator complex; IPI:FlyBase.
DR   GO; GO:0035497; F:cAMP response element binding; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:FlyBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0035293; P:chitin-based larval cuticle pattern formation; IMP:FlyBase.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IGI:FlyBase.
DR   GO; GO:0008363; P:larval chitin-based cuticle development; IMP:FlyBase.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007431; P:salivary gland development; IMP:FlyBase.
DR   CDD; cd14689; bZIP_CREB3; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   PANTHER; PTHR46004; CYCLIC AMP RESPONSE ELEMENT-BINDING PROTEIN A; 1.
DR   PANTHER; PTHR46004:SF3; CYCLIC AMP RESPONSE ELEMENT-BINDING PROTEIN A; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
DR   Genevisible; P29747; DM.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..516
FT                   /note="Cyclic AMP response element-binding protein A"
FT                   /id="PRO_0000076635"
FT   DOMAIN          441..504
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          213..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..463
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          469..476
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        221..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         75
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   CONFLICT        114
FT                   /note="Y -> C (in Ref. 1; CAA45771 and 2; AAA28427)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        277..278
FT                   /note="QQ -> HE (in Ref. 1; CAA45771)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        305
FT                   /note="D -> G (in Ref. 1; CAA45771 and 7; AAR82739)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        316
FT                   /note="L -> T (in Ref. 1; CAA45771)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        338..364
FT                   /note="APLSPNATVSISVANPAGGESSVRVSR -> RHCRPTQPFPSLWPIQPAVSH
FT                   PYGSA (in Ref. 1; CAA45771)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   516 AA;  56342 MW;  25EA48DAE2ACE7E6 CRC64;
     MEFYDGDLKD IWDSDLDPES LKISPDHDMH DWLFDRDVKD PTVILNDKLI SDALLNGTQP
     IKTEHSYSLS SDVDSLPDSP KSLQAKIEDM DDECFPAISP KTATNGRVTI DPKYLTFHVP
     PTHATPISRL SSNPALNTSV ADLTRSSGLQ SLQAHQPHHG SGSSHVVVAN LEHFQLPQHL
     YDNDCSSSVS SLRDGSMSPD ICSDIEIDES AIKDEPMSPD SSCPASPTSQ ASSSQHQLSL
     NLAHLQSEML FEPKHCGLLL TASSNSNNSL IKSQQRQQQI LGQDNLLMAK MEIKSEKQST
     SNSSDKSHAH GYGIPLTPPS SLPSDDSEGN LSPEHLFAPL SPNATVSISV ANPAGGESSV
     RVSRTAASIT RSSSGSASAS GSSTSSTVTT TRQPIHTPLI SSQPKGSTGT LLLTEEEKRT
     LLAEGYPIPQ KLPLTKAEEK SLKKIRRKIK NKISAQESRR KKKEYMDQLE RRVEILVTEN
     HDYKKRLEGL EETNANLLSQ LHKLQALVSK HNVKKS
//