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P10762 (APL3_LOCMI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. 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-3b
Alternative name(s):
Apolipophorin-IIIb
Short name=ApoLp-IIIb
OrganismLocusta migratoria (Migratory locust)
Taxonomic identifier7004 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraOrthopteroideaOrthopteraCaeliferaAcridomorphaAcridoideaAcrididaeOedipodinaeLocusta

Protein attributes

Sequence length179 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 14 molecules of apolipophorin-3 in L.migratoria (5 molecules of apolipophorin-3a and 9 of apolipophorin-3b).

Subcellular location

Secreted.

Tissue specificity

Hemolymph.

Miscellaneous

Two isoforms of apolipophorin-3 (a and b) have been found and occur in a ratio of 5a:9b in the hemolymph.

Sequence similarities

Belongs to the insect apolipophorin-3 family.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentSecreted
   DomainRepeat
Signal
   PTMGlycoprotein
   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.2
Chain17 – 179163Apolipophorin-3b
PRO_0000002046

Regions

Repeat30 – 4011
Repeat41 – 5212
Repeat53 – 608
Repeat61 – 7818
Repeat79 – 8911
Repeat90 – 9910
Repeat100 – 11314
Repeat114 – 12714
Repeat128 – 14013
Repeat141 – 15111
Repeat152 – 16514
Repeat166 – 17914

Amino acid modifications

Glycosylation341N-linked (GlcNAc...)
Glycosylation1011N-linked (GlcNAc...)

Experimental info

Sequence conflict951R → A in AAA29282. Ref.1
Sequence conflict111 – 1144AQPA → LNLQ in AAA29282. Ref.1
Sequence conflict133 – 1408TSQPRPSV → DIATKTQAS in AAA29282. Ref.1

Secondary structure

................. 179
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10762 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 43F38EA477DF5079

FASTA17919,113
        10         20         30         40         50         60 
MNTLLAVLML AVAAQARPDA AGHVNIAEAV QQLNHTIVNA AHELHETLGL PTPDEALNLL 

        70         80         90        100        110        120 
TEQANAFKTK IAEVTTSLKQ EAEKHQGSVA EQLNRFARNL NNSIHDAATS AQPADQLNSL 

       130        140        150        160        170 
QSALTNVGHQ WQTSQPRPSV AQEAWAPVQS ALQEAAEKTK EAAANLQNSI QSAVQKPAN 

« Hide

References

[1]"Primary structure of apolipophorin-III from the migratory locust, Locusta migratoria. Potential amphipathic structures and molecular evolution of an insect apolipoprotein."
Kanost M.R., Boguski M.S., Freeman M., Gordon J.I., Wyatt G.R., Wells M.A.
J. Biol. Chem. 263:10568-10573(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Different isoforms of an apoprotein (apolipophorin III) associate with lipoproteins in Locusta migratoria."
van der Horst D.J., van Doorn J.M., Voshol H., Kanost M.R., Ziegler R., Beenakkers A.M.T.
Eur. J. Biochem. 196:509-517(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-58.
[3]"Molecular structure of an apolipoprotein determined at 2.5-A resolution."
Breiter D.R., Kanost M.R., Benning M.M., Wesenberg G., Law J.H., Wells M.A., Rayment I., Holden H.M.
Biochemistry 30:603-608(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Protein Spotlight

Lipid freight - Issue 59 of June 2005

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03888 mRNA. Translation: AAA29282.1.
PIRA28992.
S14101.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AEPX-ray2.70A20-179[»]
1LS4NMR-A1-179[»]
ProteinModelPortalP10762.
SMRP10762. Positions 17-179.
ModBaseSearch...
MobiDBSearch...

PTM databases

UniCarbKBP10762.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Other

EvolutionaryTraceP10762.

Entry information

Entry nameAPL3_LOCMI
AccessionPrimary (citable) accession number: P10762
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: February 19, 2014
This is version 86 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