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P10891 (DEFI_PROTE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 26, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 namesRecommended name:
Phormicin
Alternative name(s):
Insect defensin A/B
OrganismProtophormia terraenovae (Northern blowfly) (Lucilia terraenovae)
Taxonomic identifier34676 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaOestroideaCalliphoridaeChrysomyinaeProtophormia

Protein attributes

Sequence length94 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the anti Gram-positive activity of immune hemolymph of P.terraenovae.

Subcellular location

Secreted.

Sequence similarities

Belongs to the invertebrate defensin family. Type 1 subfamily.

Ontologies

Keywords
   Biological processImmunity
Innate immunity
   Cellular componentSecreted
   DomainSignal
   Molecular functionAntibiotic
Antimicrobial
Defensin
   PTMCleavage on pair of basic residues
Disulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processdefense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 5431
PRO_0000006748
Chain55 – 9440Phormicin
PRO_0000006749

Amino acid modifications

Disulfide bond57 ↔ 84 Ref.3
Disulfide bond70 ↔ 90 Ref.3
Disulfide bond74 ↔ 92 Ref.3

Natural variations

Natural variant861G → R in defensin B.

Secondary structure

..... 94
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10891 [UniParc].

Last modified November 1, 1991. Version 2.
Checksum: CE24ED83D7CBE6D9

FASTA9410,110
        10         20         30         40         50         60 
MKFFMVFVVT FCLAVCFVSQ SLAIPADAAN DAHFVDGVQA LKEIEPELHG RYKRATCDLL 

        70         80         90 
SGTGINHSAC AAHCLLRGNR GGYCNGKGVC VCRN 

« Hide

References

[1]"Insect immunity: expression of the two major inducible antibacterial peptides, defensin and diptericin, in Phormia terranovae."
Dimarcq J.-L., Zachary D., Hoffmann J.A., Hoffmann D., Reichhart J.-M.
EMBO J. 9:2507-2515(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Insect immunity: isolation from immune blood of the dipteran Phormia terranovae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides."
Lambert J., Keppi E., Dimarcq J.-L., Wicker C., Reichhart J.-M., Dunbar B., Lepage P., van Dorsselaer A., Hoffmann J.A., Fothergill J., Hoffmann D.
Proc. Natl. Acad. Sci. U.S.A. 86:262-266(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 55-94.
Tissue: Hemolymph.
[3]"Determination of disulfide bridges in natural and recombinant insect defensin A."
Lepage P., Bitsch F., Roecklin D., Keppi E., Dimarcq J.-L., Reichhart J.-M., Hoffmann J.A., Roitsch C., van Dorsselaer A.
Eur. J. Biochem. 196:735-742(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[4]"Progress in multidimensional NMR investigations of peptide and protein 3-D structures in solution. From structure to functional aspects."
Bonmatin J.-M., Genest M., Petit M.-C., Gincel E., Simorre J.-P., Cornet B., Gallet X., Caille A., Labbe H., Vovelle F., Ptak M.
Biochimie 74:825-836(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[5]"Refined three-dimensional solution structure of insect defensin A."
Cornet B., Bonmatin J.-M., Hetru C., Hoffmann J.A., Ptak M., Vovelle F.
Structure 3:435-448(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 55-94.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55546 mRNA. Translation: CAA39152.1.
PIRS12558.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ICANMR-A55-94[»]
ProteinModelPortalP10891.
SMRP10891. Positions 55-94.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

TCDB1.C.47.1.2. the insect/fungal defensin (insect/fungal defensin) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.30.10. 1 hit.
InterProIPR017982. Defensin_insect.
IPR001542. Defensin_invertebrate/fungal.
IPR003614. Scorpion_toxin-like.
[Graphical view]
PfamPF01097. Defensin_2. 1 hit.
[Graphical view]
PRINTSPR00271. DEFENSIN.
SMARTSM00505. Knot1. 1 hit.
[Graphical view]
SUPFAMSSF57095. SSF57095. 1 hit.
PROSITEPS51378. INVERT_DEFENSINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10891.

Entry information

Entry nameDEFI_PROTE
AccessionPrimary (citable) accession number: P10891
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1991
Last modified: June 26, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references