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Protein

NF-kappa-B inhibitor cactus

Gene

cact

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the formation of the dorsoventral pattern. It inhibits nuclear translocation of the dorsal morphogen in the dorsal region of the embryo. Acts as a negative regulator of the NF-kappa-B (rel) signaling pathway. Cact is degraded by ird5, this is essential for NF-kappa-B (rel) activation.4 Publications

GO - Molecular functioni

  • transcription factor binding Source: FlyBase

GO - Biological processi

  • antifungal humoral response Source: FlyBase
  • antimicrobial humoral response Source: FlyBase
  • cellular response to DNA damage stimulus Source: FlyBase
  • cytoplasmic sequestering of transcription factor Source: FlyBase
  • defense response Source: FlyBase
  • dorsal/ventral axis specification Source: UniProtKB
  • dorsal appendage formation Source: FlyBase
  • hemopoiesis Source: FlyBase
  • immune response Source: FlyBase
  • innate immune response Source: FlyBase
  • negative regulation of protein import into nucleus Source: FlyBase
  • nervous system development Source: FlyBase
  • oogenesis Source: FlyBase
  • phagocytosis Source: FlyBase
  • positive regulation of antifungal peptide biosynthetic process Source: FlyBase
  • response to fungus Source: FlyBase
  • Toll signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Enzyme and pathway databases

ReactomeiR-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-202424. Downstream TCR signaling.
R-DME-209560. NF-kB is activated and signals survival.
R-DME-2871837. FCERI mediated NF-kB activation.
R-DME-5607764. CLEC7A (Dectin-1) signaling.
SignaLinkiQ03017.

Names & Taxonomyi

Protein namesi
Recommended name:
NF-kappa-B inhibitor cactus
Gene namesi
Name:cact
ORF Names:CG5848
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000250. cact.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • neuromuscular junction Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 500500NF-kappa-B inhibitor cactusPRO_0000067055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451Phosphoserine; by PKCSequence analysis
Modified residuei144 – 1441Phosphoserine; by PKCSequence analysis
Modified residuei183 – 1831Phosphothreonine; by PKCSequence analysis
Modified residuei293 – 2931Phosphothreonine; by PKCSequence analysis
Modified residuei319 – 3191Phosphothreonine; by PKCSequence analysis
Modified residuei395 – 3951Phosphoserine; by PKCSequence analysis

Post-translational modificationi

Activated ird5 phosphorylates cact.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ03017.
PRIDEiQ03017.

PTM databases

iPTMnetiQ03017.

Expressioni

Tissue specificityi

Expressed in ovary (at protein level).

Developmental stagei

Expressed during embryogenesis (at protein level). Isoform A is expressed in ovaries and 0-1 hour embryos. After 2-3 hours unphosphorylated zygotic protein is expressed. Between 4-8 hours phosphorylated zygotic protein is expressed. After 12 hours the amount of unphosphorylated zygotic protein increases until, by the end of embryogenesis, it is the most abundant form of cactus.1 Publication

Gene expression databases

BgeeiQ03017.
ExpressionAtlasiQ03017. differential.
GenevisibleiQ03017. DM.

Interactioni

Subunit structurei

Phosphorylated isoform A binds to dorsal (dl); inhibits dl translocation to the nucleus and therefore from binding to DNA. In vitro, interacts with ird5. Interacts with cactin and kappa-B-Ras.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
dlP153304EBI-200600,EBI-198375
ird5Q9VEZ52EBI-200600,EBI-148871
krzQ9V3932EBI-200600,EBI-100228

GO - Molecular functioni

  • transcription factor binding Source: FlyBase

Protein-protein interaction databases

BioGridi60980. 42 interactions.
DIPiDIP-17846N.
IntActiQ03017. 12 interactions.
MINTiMINT-301064.
STRINGi7227.FBpp0080402.

Structurei

3D structure databases

ProteinModelPortaliQ03017.
SMRiQ03017. Positions 174-495.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati229 – 26133ANK 1Add
BLAST
Repeati265 – 29430ANK 2Add
BLAST
Repeati298 – 32730ANK 3Add
BLAST
Repeati361 – 39030ANK 4Add
BLAST
Repeati395 – 42430ANK 5Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi120 – 13617Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi469 – 4757Asp/Glu-rich (acidic)

Sequence similaritiesi

Belongs to the NF-kappa-B inhibitor family.Curated
Contains 5 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00550000074527.
InParanoidiQ03017.
KOiK09259.
OMAiDGERCVH.
OrthoDBiEOG7W154S.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q03017-1) [UniParc]FASTAAdd to basket

Also known as: B, D, Maternal/zygotic

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPSPTKAAEA ATKATATSDC SCSAASVEQR APSNAANPSS SLATSGKIGG
60 70 80 90 100
KTQDQTAAIN KQKEFAVPNE TSDSGFISGP QSSQIFSEEI VPDSEEQDKD
110 120 130 140 150
QQESAPQKEQ PVVLDSGIID EEEDQEEQEK EEEHQDTTTA TADSMRLKHS
160 170 180 190 200
ADTGIPQWTV ESHLVSRGEQ LNNLGQSSST QITGRSKVQS STASTANANP
210 220 230 240 250
SGSGATSSAP PSSINIMNAW EQFYQQNDDG DTPLHLACIS GSVDVVAALI
260 270 280 290 300
RMAPHPCLLN IQNDVAQTPL HLAALTAQPN IMRILLLAGA EPTVRDRHGN
310 320 330 340 350
TALHLSCIAG EKQCVRALTE KFGATEIHEA HRQYGHRSND KAVSSLSYAC
360 370 380 390 400
LPADLEIRNY DGERCVHLAA EAGHIDILRI LVSHGADINA REGKSGRTPL
410 420 430 440 450
HIAIEGCNED LANFLLDECE KLNLETATYA GLTAYQFACI MNKSRMQNIL
460 470 480 490 500
EKRGAETVTP PDSDYDSSDI EDLDDTKMYD RFGDPRYFVS YNGGNPMTVA
Length:500
Mass (Da):53,818
Last modified:November 2, 2001 - v2
Checksum:i9E9711B97CDB499F
GO
Isoform C (identifier: Q03017-2) [UniParc]FASTAAdd to basket

Also known as: Zygotic

The sequence of this isoform differs from the canonical sequence as follows:
     478-500: MYDRFGDPRYFVSYNGGNPMTVA → VSVTA

Show »
Length:482
Mass (Da):51,636
Checksum:i334A444730896055
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961A → G in AAA85908 (PubMed:1423618).Curated
Sequence conflicti196 – 1961A → G in AAA28407 (PubMed:1423619).Curated
Sequence conflicti222 – 2221Q → R in AAA28407 (PubMed:1423619).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei478 – 50023MYDRF…PMTVA → VSVTA in isoform C. CuratedVSP_000286Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04964 mRNA. Translation: AAA85908.1.
L03367 Genomic DNA. Translation: AAA28407.1.
L03368 Genomic DNA. Translation: AAA28408.1.
AE014134 Genomic DNA. Translation: AAN10936.1.
AE014134 Genomic DNA. Translation: AAN10937.1.
AE014134 Genomic DNA. Translation: AAS64714.1.
AY069399 mRNA. Translation: AAL39544.1.
PIRiA44269.
B44268.
RefSeqiNP_001260496.1. NM_001273567.1. [Q03017-1]
NP_476942.1. NM_057594.4. [Q03017-1]
NP_476943.1. NM_057595.4. [Q03017-2]
NP_723960.1. NM_165152.2. [Q03017-1]
NP_995721.1. NM_205999.2. [Q03017-1]
UniGeneiDm.2150.

Genome annotation databases

EnsemblMetazoaiFBtr0080844; FBpp0080402; FBgn0000250. [Q03017-1]
FBtr0080845; FBpp0080403; FBgn0000250. [Q03017-1]
FBtr0080847; FBpp0089296; FBgn0000250. [Q03017-1]
FBtr0337081; FBpp0308004; FBgn0000250. [Q03017-1]
GeneIDi34969.
KEGGidme:Dmel_CG5848.
UCSCiCG5848-RA. d. melanogaster. [Q03017-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04964 mRNA. Translation: AAA85908.1.
L03367 Genomic DNA. Translation: AAA28407.1.
L03368 Genomic DNA. Translation: AAA28408.1.
AE014134 Genomic DNA. Translation: AAN10936.1.
AE014134 Genomic DNA. Translation: AAN10937.1.
AE014134 Genomic DNA. Translation: AAS64714.1.
AY069399 mRNA. Translation: AAL39544.1.
PIRiA44269.
B44268.
RefSeqiNP_001260496.1. NM_001273567.1. [Q03017-1]
NP_476942.1. NM_057594.4. [Q03017-1]
NP_476943.1. NM_057595.4. [Q03017-2]
NP_723960.1. NM_165152.2. [Q03017-1]
NP_995721.1. NM_205999.2. [Q03017-1]
UniGeneiDm.2150.

3D structure databases

ProteinModelPortaliQ03017.
SMRiQ03017. Positions 174-495.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60980. 42 interactions.
DIPiDIP-17846N.
IntActiQ03017. 12 interactions.
MINTiMINT-301064.
STRINGi7227.FBpp0080402.

PTM databases

iPTMnetiQ03017.

Proteomic databases

PaxDbiQ03017.
PRIDEiQ03017.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080844; FBpp0080402; FBgn0000250. [Q03017-1]
FBtr0080845; FBpp0080403; FBgn0000250. [Q03017-1]
FBtr0080847; FBpp0089296; FBgn0000250. [Q03017-1]
FBtr0337081; FBpp0308004; FBgn0000250. [Q03017-1]
GeneIDi34969.
KEGGidme:Dmel_CG5848.
UCSCiCG5848-RA. d. melanogaster. [Q03017-1]

Organism-specific databases

CTDi34969.
FlyBaseiFBgn0000250. cact.

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00550000074527.
InParanoidiQ03017.
KOiK09259.
OMAiDGERCVH.
OrthoDBiEOG7W154S.

Enzyme and pathway databases

ReactomeiR-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-202424. Downstream TCR signaling.
R-DME-209560. NF-kB is activated and signals survival.
R-DME-2871837. FCERI mediated NF-kB activation.
R-DME-5607764. CLEC7A (Dectin-1) signaling.
SignaLinkiQ03017.

Miscellaneous databases

GenomeRNAii34969.
PROiQ03017.

Gene expression databases

BgeeiQ03017.
ExpressionAtlasiQ03017. differential.
GenevisibleiQ03017. DM.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cactus, a gene involved in dorsoventral pattern formation of Drosophila, is related to the I kappa B gene family of vertebrates."
    Geisler R., Bergmann A., Hiromi Y., Nuesslein-Volhard C.
    Cell 71:613-621(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION.
  2. "Characterization of the Drosophila cactus locus and analysis of interactions between cactus and dorsal proteins."
    Kidd S.
    Cell 71:623-635(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH DL, ALTERNATIVE SPLICING (ISOFORMS A AND C).
    Strain: Oregon-R.
    Tissue: Embryo.
  3. "An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region."
    Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.
    , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.
    Genetics 153:179-219(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Embryo.
  7. "Lipopolysaccharide-activated kinase, an essential component for the induction of the antimicrobial peptide genes in Drosophila melanogaster cells."
    Kim Y.-S., Han S.-J., Ryu J.-H., Choi K.-H., Hong Y.-S., Chung Y.-H., Perrot S., Raibaud A., Brey P.T., Lee W.-J.
    J. Biol. Chem. 275:2071-2079(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IRD5, PHOSPHORYLATION.
  8. "Cactin, a conserved protein that interacts with the Drosophila IkappaB protein cactus and modulates its function."
    Lin P., Huang L.H., Steward R.
    Mech. Dev. 94:57-65(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CACTIN.
  9. "A subclass of Ras proteins that regulate the degradation of IkappaB."
    Fenwick C., Na S.-Y., Voll R.E., Zhong H., Im S.-Y., Lee J.W., Ghosh S.
    Science 287:869-873(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KAPPA-B-RAS.

Entry informationi

Entry nameiCACT_DROME
AccessioniPrimary (citable) accession number: Q03017
Secondary accession number(s): A4V0S3, Q0E8Q3, Q9V3M6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 2, 2001
Last modified: July 6, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.