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Protein

Cecropin-C

Gene

CecC

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

Functioni

Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria.

GO - Biological processi

  • antibacterial humoral response Source: FlyBase
  • defense response to bacterium Source: FlyBase
  • defense response to fungus Source: FlyBase
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • humoral immune response Source: FlyBase
  • innate immune response Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

Keywords - Biological processi

Immunity, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Cecropin-C
Gene namesi
Name:CecC
ORF Names:CG1373
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0000279. CecC.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
  • extracellular space Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Chaini24 – 6239Cecropin-CPRO_0000004848Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei62 – 621Arginine amideBy similarity

Keywords - PTMi

Amidation

Proteomic databases

PaxDbiO16829.

Expressioni

Tissue specificityi

In the anterior end of the larval hindgut and in other larval tissues that are undergoing histolysis.1 Publication

Developmental stagei

Expressed during metamorphosis in pupae.1 Publication

Inductioni

Induced as part of the humoral response to a bacterial invasion.1 Publication

Gene expression databases

BgeeiO16829.
GenevisibleiO16829. DM.

Interactioni

Protein-protein interaction databases

MINTiMINT-943709.
STRINGi7227.FBpp0084980.

Structurei

3D structure databases

ProteinModelPortaliO16829.
SMRiO16829. Positions 24-54.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cecropin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410KBRA. Eukaryota.
ENOG4110N0P. LUCA.
InParanoidiO16829.
OMAiGQTEAGW.
OrthoDBiEOG7K9K6B.
PhylomeDBiO16829.

Family and domain databases

InterProiIPR000875. Cecropin.
IPR020400. Cecropin_diptera.
[Graphical view]
PfamiPF00272. Cecropin. 1 hit.
[Graphical view]
ProDomiPD001670. Cecropin_diptera. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS00268. CECROPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O16829-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFYKIFVFV ALILAISIGQ SEAGWLKKLG KRIERIGQHT RDATIQGLGI
60
AQQAANVAAT ARG
Length:63
Mass (Da):6,813
Last modified:July 5, 2004 - v2
Checksum:i95686510DA767EDA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 1612KIFVF…LILAI → MIYVRVGRTQAS in strain: Z10.
Add
BLAST
Natural varianti5 – 51K → Q in strain: B205 and B208.
Natural varianti20 – 201Q → H in strain: Z10, Z18, Z22 and Z24.
Natural varianti25 – 251W → G in strain: Z10 and Z22.
Natural varianti26 – 261L → R in strain: Z24.
Natural varianti26 – 261L → W in strain: Z10, Z18 and Z22.
Natural varianti27 – 271K → R in strain: Z10 and Z18.
Natural varianti53 – 531Q → R in strain: B316.
Natural varianti54 – 541A → T in strain: B202.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11167 Genomic DNA. Translation: CAA77559.1.
AF019007 Genomic DNA. Translation: AAB82504.1.
AF019008 Genomic DNA. Translation: AAB82505.1.
AF019009 Genomic DNA. Translation: AAB82506.1.
AF019010 Genomic DNA. Translation: AAB82507.1.
AF019011 Genomic DNA. Translation: AAB82508.1.
AF019012 Genomic DNA. Translation: AAB82509.1.
AF019013 Genomic DNA. Translation: AAB82510.1.
AF019014 Genomic DNA. Translation: AAB82511.1.
AF019015 Genomic DNA. Translation: AAB82512.1.
AF019016 Genomic DNA. Translation: AAB82513.1.
AF019017 Genomic DNA. Translation: AAB82514.1.
AF019018 Genomic DNA. Translation: AAB82515.1.
AE014297 Genomic DNA. Translation: AAF57028.1.
AY113583 mRNA. Translation: AAM29588.1.
PIRiS23501.
RefSeqiNP_524591.1. NM_079852.3.
UniGeneiDm.20562.

Genome annotation databases

EnsemblMetazoaiFBtr0085616; FBpp0084980; FBgn0000279.
GeneIDi43599.
KEGGidme:Dmel_CG1373.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11167 Genomic DNA. Translation: CAA77559.1.
AF019007 Genomic DNA. Translation: AAB82504.1.
AF019008 Genomic DNA. Translation: AAB82505.1.
AF019009 Genomic DNA. Translation: AAB82506.1.
AF019010 Genomic DNA. Translation: AAB82507.1.
AF019011 Genomic DNA. Translation: AAB82508.1.
AF019012 Genomic DNA. Translation: AAB82509.1.
AF019013 Genomic DNA. Translation: AAB82510.1.
AF019014 Genomic DNA. Translation: AAB82511.1.
AF019015 Genomic DNA. Translation: AAB82512.1.
AF019016 Genomic DNA. Translation: AAB82513.1.
AF019017 Genomic DNA. Translation: AAB82514.1.
AF019018 Genomic DNA. Translation: AAB82515.1.
AE014297 Genomic DNA. Translation: AAF57028.1.
AY113583 mRNA. Translation: AAM29588.1.
PIRiS23501.
RefSeqiNP_524591.1. NM_079852.3.
UniGeneiDm.20562.

3D structure databases

ProteinModelPortaliO16829.
SMRiO16829. Positions 24-54.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-943709.
STRINGi7227.FBpp0084980.

Proteomic databases

PaxDbiO16829.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085616; FBpp0084980; FBgn0000279.
GeneIDi43599.
KEGGidme:Dmel_CG1373.

Organism-specific databases

CTDi43599.
FlyBaseiFBgn0000279. CecC.

Phylogenomic databases

eggNOGiENOG410KBRA. Eukaryota.
ENOG4110N0P. LUCA.
InParanoidiO16829.
OMAiGQTEAGW.
OrthoDBiEOG7K9K6B.
PhylomeDBiO16829.

Miscellaneous databases

GenomeRNAii43599.
PROiO16829.

Gene expression databases

BgeeiO16829.
GenevisibleiO16829. DM.

Family and domain databases

InterProiIPR000875. Cecropin.
IPR020400. Cecropin_diptera.
[Graphical view]
PfamiPF00272. Cecropin. 1 hit.
[Graphical view]
ProDomiPD001670. Cecropin_diptera. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS00268. CECROPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CecC, a cecropin gene expressed during metamorphosis in Drosophila pupae."
    Tryselius Y., Samakovlis C., Kimbrell D.A., Hultmark D.
    Eur. J. Biochem. 204:395-399(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Canton-S.
  2. "Molecular population genetics of Drosophila immune system genes."
    Clark A.G., Wang L.
    Genetics 147:713-724(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: B009, B101, B115, B202, B205, B208, B316, M31, Z10, Z18, Z22, Z24 and Z5.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiCECC_DROME
AccessioniPrimary (citable) accession number: O16829
Secondary accession number(s): O16830
, O16831, O16832, O16833, O16834, O16835, O16836, O16837, P29561, Q9VA89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 103 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.