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P80703 (APL3_GALME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipophorin-3
Alternative name(s):
Apolipophorin-III
Short name=ApoLp-III
OrganismGalleria mellonella (Greater wax moth)
Taxonomic identifier7137 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaPyraloideaPyralidaeGalleriinaeGalleria

Protein attributes

Sequence length186 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. It increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It thus plays a critical role in the transport of lipids during flight in several species of insects. Has antibacterial activity against the Gram-positive bacteria L.monocytogenes (MIC=6.5 µM). Lacks antibacterial activity against the Gram-positive bacteria B.circulans, M.luteus, S.aureus, and S.lutea, and the Gram-negative bacteria E.coli D31, E.coli ATCC 25922, and S.typhimurium. Lacks antifungal activity against S.cerevisiae, P.pastoris, Z.marxianus, C.albicans, C.wickerhamii, A.niger, F.oxysporum, and T.harizianum. Ref.3

Subunit structure

Equilibrium between a soluble monomer and a bound lipoprotein form. Apolipophorin-3 associates with lipophorin during lipid loading until each particle contains 9 or 14 molecules of apolipophorin-3.

Subcellular location

Secreted Ref.3.

Tissue specificity

Hemolymph. Ref.3

Induction

By bacterial infection. Ref.3

Sequence similarities

Belongs to the insect apolipophorin-3 family.

Mass spectrometry

Molecular mass is 5712.7 Da from positions 136 - 186. Determined by ESI. The measured mass may be that of a peptide that is synthesized after immune challenge or a fragment of partial proteolytic digestion. Ref.3

Ontologies

Keywords
   Biological processImmunity
Innate immunity
Lipid transport
Transport
   Cellular componentSecreted
   DomainSignal
   Molecular functionAntibiotic
Antimicrobial
   PTMCleavage on pair of basic residues
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processdefense response to Gram-positive bacterium

Inferred from direct assay Ref.3. Source: UniProtKB

innate immune response

Inferred from direct assay Ref.3. Source: UniProtKB

lipid transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from direct assay Ref.3. Source: UniProtKB

   Molecular_functionlipid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 235
PRO_0000002042
Chain24 – 186163Apolipophorin-3
PRO_0000002043

Sequences

Sequence LengthMass (Da)Tools
P80703 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: C79B381E07F5C070

FASTA18620,453
        10         20         30         40         50         60 
MAAKYVFVVA ACSALAQAGI VRRDASTPLQ DLEKHAAEFQ KTFSEQLNAF TNSKDTKEFN 

        70         80         90        100        110        120 
TALKEGSDSV LQQLNALASS LQKALNDANG KAKEALEQTR TNLERTAEEL RRAHPDVERQ 

       130        140        150        160        170        180 
AGALRDRLQT AVQATVQETQ KLAKTVGANL EETNKKLAPQ IKSAYDDFVK QAQEVQKKLH 


EAASKQ 

« Hide

References

[1]"Functional expression of Galleria mellonella apolipophorin III."
Niere M., Dettloff M., Weise C., Meisslitzer C., Ziegler M., Wiesner A.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fat body.
[2]"Primary structure of apolipophorin-III from the greater wax moth, Galleria mellonella."
Weise C., Franke P., Kopacek P., Wiesner A.
J. Protein Chem. 17:633-641(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-186.
Tissue: Hemolymph.
[3]"Purification and characterization of eight peptides from Galleria mellonella immune hemolymph."
Cytrynska M., Mak P., Zdybicka-Barabas A., Suder P., Jakubowicz T.
Peptides 28:533-546(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 136-186, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, MASS SPECTROMETRY.
Tissue: Larval hemolymph.

Web resources

Protein Spotlight

Lipid freight - Issue 59 of June 2005

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ006975 mRNA. Translation: CAA07363.1.
PIRT09296.

3D structure databases

ProteinModelPortalP80703.
SMRP80703. Positions 29-186.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome3638. Gal m 24kD.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR010009. ApoLp-III.
[Graphical view]
PfamPF07464. ApoLp-III. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAPL3_GALME
AccessionPrimary (citable) accession number: P80703
Secondary accession number(s): O76946
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 15, 1998
Last modified: February 19, 2014
This is version 66 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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries