ID   CACT_DROYA              Reviewed;         489 AA.
AC   P83757;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 1.
DT   23-FEB-2022, entry version 69.
DE   RecName: Full=NF-kappa-B inhibitor cactus;
GN   Name=cact;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245 {ECO:0000312|EMBL:AAQ65041.1};
RN   [1] {ECO:0000312|EMBL:AAQ65041.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12930753; DOI=10.1093/genetics/164.4.1471;
RA   Schlenke T.A., Begun D.J.;
RT   "Natural selection drives Drosophila immune system evolution.";
RL   Genetics 164:1471-1480(2003).
CC   -!- FUNCTION: Involved in the formation of the dorsoventral pattern. It
CC       inhibits nuclear translocation of the dorsal morphogen in the dorsal
CC       region of the embryo. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; AY352231; AAQ65041.1; -; Genomic_DNA.
DR   EMBL; AY352228; AAQ65041.1; JOINED; Genomic_DNA.
DR   EMBL; AY352229; AAQ65041.1; JOINED; Genomic_DNA.
DR   EMBL; AY352230; AAQ65041.1; JOINED; Genomic_DNA.
DR   STRING; 7245.FBpp0264376; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR   GO; GO:0031594; C:neuromuscular junction; IEA:EnsemblMetazoa.
DR   GO; GO:0071212; C:subsynaptic reticulum; IEA:EnsemblMetazoa.
DR   GO; GO:0051059; F:NF-kappaB binding; IEA:EnsemblMetazoa.
DR   GO; GO:0019730; P:antimicrobial humoral response; IEA:EnsemblMetazoa.
DR   GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; IEA:EnsemblMetazoa.
DR   GO; GO:0046843; P:dorsal appendage formation; ISS:UniProtKB.
DR   GO; GO:0009950; P:dorsal/ventral axis specification; IEA:EnsemblMetazoa.
DR   GO; GO:0002789; P:negative regulation of antifungal peptide production; IEA:EnsemblMetazoa.
DR   GO; GO:0045611; P:negative regulation of hemocyte differentiation; IEA:EnsemblMetazoa.
DR   GO; GO:0045751; P:negative regulation of Toll signaling pathway; IEA:EnsemblMetazoa.
DR   GO; GO:0007399; P:nervous system development; IEA:EnsemblMetazoa.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   3: Inferred from homology;
KW   ANK repeat; Cytoplasm; Developmental protein; Phosphoprotein; Repeat.
FT   CHAIN           1..489
FT                   /note="NF-kappa-B inhibitor cactus"
FT                   /id="PRO_0000067056"
FT   REPEAT          220..252
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000305"
FT   REPEAT          256..285
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000305"
FT   REPEAT          287..316
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000305"
FT   REPEAT          350..379
FT                   /note="ANK 4"
FT                   /evidence="ECO:0000305"
FT   REPEAT          384..413
FT                   /note="ANK 5"
FT                   /evidence="ECO:0000305"
FT   REGION          23..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         45
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         135
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         174
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         308
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         384
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   489 AA;  52539 MW;  947B61E005B222D4 CRC64;
     MPSPTKAAEA ATKATATSDC SCSAASVEER GPVNAANPSS TXATSGKIGG KTQDQTAAIN
     KPKEFAVPNE TSDSGFISGP QSSQICSEEI VPDSEEQDKN QQQSAPQKEQ PVVLDSGIID
     EEEEHQDTTT ATADSMRLKH SADTGIPQWT VESHLVNRGE QLNNLGQSSS TQITGRSKFQ
     SSTASTANAN PSGXGATSSA PPSSINIXNA WEQFYQQNDD GDTPXHLACI SGSVEVVAAL
     IRMAPHPCLL NIQNDVAQTP LHLAALTAQP NIMRILLLAG AEVRDRHGNT ALHLSCIAGE
     KQCVRALTEE FGATEIHEAH RQYGHRSNDK AVSSLSFARL PADLEIRNYD GERCVHLAAE
     AGHIDILRIL VSHGADINAR EGKSGRTPLH IAIEGCNEDL ANFLLDECEK LNLETATYAG
     LTAYQFACIM NKSRMQNILE KRGAETVTPP DSDYDSSDIE DLDDTKMYDR FGDPRYFVSY
     NGGNPMTVA