Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P36193 (DROS_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length64 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Antibacterial peptide with strong anti-Gram-negative bacteria activity.

Subcellular location

Secreted.

Tissue specificity

In hemolymph 6 hours after immune challenge, levels of expression increase for first 24 hours and persist for the following two weeks. Ref.8

Developmental stage

Expressed in larvae and in adults.

Induction

By bacterial infection. Ref.8

Post-translational modification

O-glycosylation is essential for full biological activity.

Sequence similarities

Belongs to the drosocin family.

Mass spectrometry

Molecular mass is 2401.9 Da from positions 22 - 40. Determined by MALDI. With monosaccharide on Thr-32. Ref.8

Molecular mass is 2564.4 Da from positions 22 - 40. Determined by MALDI. With disaccharide on Ser-28 and Thr-32. Ref.8

Sequence caution

The sequence AAM29584.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 212
PRO_0000004958
Peptide22 – 4019Drosocin Ref.1
PRO_0000004959
Propeptide43 – 6422 Potential
PRO_0000004960

Amino acid modifications

Glycosylation281O-linked (GalNAc...) Ref.8
Glycosylation321O-linked (GalNAc...) Ref.1

Natural variations

Natural variant521T → A in strain: 2CPA1, 2CPA12, 2CPA51, 2CPA105, 2CPA118, 2CPA122, 8B, 8D, 8E, 8F, 8G, 9A, 9B, 9C, 9D, 9E, 9F, 9G, 9H, 10B, 10F, 10G, 10H and Oregon-R. Ref.1 Ref.2 Ref.3
Natural variant641A → V in strain: 2CPA51. Ref.3

Experimental info

Sequence conflict171G → A in CAA79936. Ref.1
Sequence conflict171G → A in CAA67062. Ref.2
Sequence conflict171G → A in AAO72465. Ref.3
Sequence conflict171G → A in AAO72466. Ref.3
Sequence conflict171G → A in AAO72467. Ref.3
Sequence conflict171G → A in AAO72468. Ref.3
Sequence conflict171G → A in AAO72469. Ref.3
Sequence conflict171G → A in AAO72470. Ref.3
Sequence conflict171G → A in AAO72471. Ref.3
Sequence conflict171G → A in AAO72472. Ref.3
Sequence conflict171G → A in AAO72473. Ref.3
Sequence conflict171G → A in AAO72474. Ref.3
Sequence conflict171G → A in AAO72475. Ref.3
Sequence conflict171G → A in AAO72476. Ref.3
Sequence conflict171G → A in AAO72502. Ref.3
Sequence conflict171G → A in AAO72503. Ref.3
Sequence conflict171G → A in AAO72504. Ref.3
Sequence conflict171G → A in AAO72505. Ref.3
Sequence conflict171G → A in AAO72506. Ref.3
Sequence conflict171G → A in AAO72507. Ref.3
Sequence conflict171G → A in AAO72508. Ref.3
Sequence conflict171G → A in AAO72509. Ref.3
Sequence conflict171G → A in AAO72510. Ref.3
Sequence conflict171G → A in AAO72511. Ref.3
Sequence conflict171G → A in AAO72512. Ref.3
Sequence conflict171G → A in AAO72513. Ref.3
Sequence conflict171G → A in AAO72514. Ref.3
Sequence conflict171G → A in AAO72515. Ref.3
Sequence conflict171G → A in AAO72516. Ref.3
Sequence conflict171G → A in AAO72517. Ref.3
Sequence conflict171G → A in AAO72518. Ref.3
Sequence conflict171G → A in AAO72519. Ref.3
Sequence conflict171G → A in AAO72520. Ref.3
Sequence conflict171G → A in AAO72521. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P36193 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: D715F5BA52FDAD17

FASTA647,085
        10         20         30         40         50         60 
MKFTIVFLLL ACVFAMGVAT PGKPRPYSPR PTSHPRPIRV RREALAIEDH LTQAAIRPPP 


ILPA 

« Hide

References

« Hide 'large scale' references
[1]"A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution."
Bulet P., Dimarcq J.-L., Hetru C., Lagueux M., Charlet M., Hegy G., van Dorsselaer A., Hoffmann J.A.
J. Biol. Chem. 268:14893-14897(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-40, VARIANT ALA-52, GLYCOSYLATION AT THR-32.
Strain: Oregon-R.
[2]"Cloning of the gene encoding the antibacterial peptide drosocin involved in Drosophila immunity. Expression studies during the immune response."
Charlet M., Lagueux M., Reichhart J.-M., Hoffmann D., Braun A., Meister M.
Eur. J. Biochem. 241:699-706(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-52.
Strain: Oregon-R.
[3]"Molecular population genetics of inducible antibacterial peptide genes in Drosophila melanogaster."
Lazzaro B.P., Clark A.G.
Mol. Biol. Evol. 20:914-923(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-52 AND VAL-64.
Strain: 10B, 10C, 10D, 10F, 10G, 10H, 2CPA1, 2CPA103, 2CPA105, 2CPA118, 2CPA12, 2CPA122, 2CPA129, 2CPA14, 2CPA43, 2CPA46, 2CPA51, 2CPA7, 8B, 8C, 8D, 8E, 8F, 8G, 9A, 9B, 9C, 9D, 9E, 9F, 9G and 9H.
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[6]"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.
[7]Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[8]"Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time-of-flight mass spectrometry study."
Uttenweiler-Joseph S., Moniatte M., Lagueux M., van Dorsselaer A., Hoffmann J.A., Bulet P.
Proc. Natl. Acad. Sci. U.S.A. 95:11342-11347(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-28, INDUCTION, MASS SPECTROMETRY, TISSUE SPECIFICITY.
[9]"Conformational studies by NMR of the antimicrobial peptide, drosocin, and its non-glycosylated derivative: effects of glycosylation on solution conformation."
McManus A.M., Otvos L. Jr., Hoffmann R., Craik D.J.
Biochemistry 38:705-714(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z21942 Genomic DNA. Translation: CAA79936.1.
X98416 Genomic DNA. Translation: CAA67062.1.
AY224606 Genomic DNA. Translation: AAO72465.1.
AY224607 Genomic DNA. Translation: AAO72466.1.
AY224608 Genomic DNA. Translation: AAO72467.1.
AY224609 Genomic DNA. Translation: AAO72468.1.
AY224610 Genomic DNA. Translation: AAO72469.1.
AY224611 Genomic DNA. Translation: AAO72470.1.
AY224612 Genomic DNA. Translation: AAO72471.1.
AY224613 Genomic DNA. Translation: AAO72472.1.
AY224614 Genomic DNA. Translation: AAO72473.1.
AY224615 Genomic DNA. Translation: AAO72474.1.
AY224616 Genomic DNA. Translation: AAO72475.1.
AY224617 Genomic DNA. Translation: AAO72476.1.
AY224643 Genomic DNA. Translation: AAO72502.1.
AY224644 Genomic DNA. Translation: AAO72503.1.
AY224645 Genomic DNA. Translation: AAO72504.1.
AY224646 Genomic DNA. Translation: AAO72505.1.
AY224647 Genomic DNA. Translation: AAO72506.1.
AY224648 Genomic DNA. Translation: AAO72507.1.
AY224649 Genomic DNA. Translation: AAO72508.1.
AY224650 Genomic DNA. Translation: AAO72509.1.
AY224651 Genomic DNA. Translation: AAO72510.1.
AY224652 Genomic DNA. Translation: AAO72511.1.
AY224653 Genomic DNA. Translation: AAO72512.1.
AY224654 Genomic DNA. Translation: AAO72513.1.
AY224655 Genomic DNA. Translation: AAO72514.1.
AY224656 Genomic DNA. Translation: AAO72515.1.
AY224657 Genomic DNA. Translation: AAO72516.1.
AY224658 Genomic DNA. Translation: AAO72517.1.
AY224659 Genomic DNA. Translation: AAO72518.1.
AY224660 Genomic DNA. Translation: AAO72519.1.
AY224661 Genomic DNA. Translation: AAO72520.1.
AY224662 Genomic DNA. Translation: AAO72521.1.
AE013599 Genomic DNA. Translation: AAF58216.1.
AY113579 mRNA. Translation: AAM29584.2. Different initiation.
PIRA47103. S35984.
RefSeqNP_001246324.1. NM_001259395.1.
NP_523744.1. NM_079020.4.
UniGeneDm.19928.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4EZRX-ray1.90B33-40[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0087436; FBpp0086566; FBgn0010388.
FBtr0309055; FBpp0301076; FBgn0010388.
GeneID36635.
KEGGdme:Dmel_CG10816.

Organism-specific databases

CTD36635.
FlyBaseFBgn0010388. Dro.

Phylogenomic databases

eggNOGNOG246969.
InParanoidP36193.
OMAPGKPRPY.
OrthoDBEOG7P02N0.
PhylomeDBP36193.

Gene expression databases

BgeeP36193.

Family and domain databases

ProtoNetSearch...

Other

GenomeRNAi36635.
NextBio799611.

Entry information

Entry nameDROS_DROME
AccessionPrimary (citable) accession number: P36193
Secondary accession number(s): Q53ZZ5 expand/collapse secondary AC list , Q867T5, Q86BV9, Q9V749
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase