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P13276 (APL3_MANSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. 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·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
OrganismManduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Taxonomic identifier7130 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaSphingidaeSphinginaeSphinginiManduca

Protein attributes

Sequence length189 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.

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.

Tissue specificity

Hemolymph.

Sequence similarities

Belongs to the insect apolipophorin-3 family.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentSecreted
   DomainRepeat
Signal
   PTMCleavage on pair of basic residues
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processlipid transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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_0000002047
Chain24 – 189166Apolipophorin-3
PRO_0000002048

Secondary structure

.................. 189
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13276 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: B1412640AB622169

FASTA18920,793
        10         20         30         40         50         60 
MAAKFVVVLA ACVALSHSAM VRRDAPAGGN AFEEMEKHAK EFQKTFSEQF NSLVNSKNTQ 

        70         80         90        100        110        120 
DFNKALKDGS DSVLQQLSAF SSSLQGAISD ANGKAKEALE QARQNVEKTA EELRKAHPDV 

       130        140        150        160        170        180 
EKEANAFKDK LQAAVQTTVQ ESQKLAKEVA SNMEETNKKL APKIKQAYDD FVKHAEEVQK 


KLHEAATKQ 

« Hide

References

[1]"Primary structure and comparative sequence analysis of an insect apolipoprotein. Apolipophorin-III from Manduca sexta."
Cole K.D., Warnakulasuriya F.G.J.P., Boguski M.S., Freeman M., Gordon J.I., Clark W.A., Law J.H., Wells M.A.
J. Biol. Chem. 262:11794-11800(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"The structure of the apolipophorin-III gene from Manduca sexta."
Cole K.D., Smith A.F., Wells M.A.
Insect Biochem. 20:381-388(1991)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein."
Wang J., Sykes B.D., Ryan R.O.
Proc. Natl. Acad. Sci. U.S.A. 99:1188-1193(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 24-189.

Web resources

Protein Spotlight

Lipid freight - Issue 59 of June 2005

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17286 mRNA. Translation: AAA29301.1.
M79326 Genomic DNA. Translation: AAA29300.1.
PIRA29793.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EQ1NMR-A24-189[»]
ProteinModelPortalP13276.
SMRP13276. Positions 24-189.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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

Other

EvolutionaryTraceP13276.

Entry information

Entry nameAPL3_MANSE
AccessionPrimary (citable) accession number: P13276
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: February 19, 2014
This is version 81 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references