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Protein

Apolipophorin-3

Gene
N/A
Organism
Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. lipid binding Source: InterPro

GO - Biological processi

  1. lipid transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipophorin-3
Alternative name(s):
Apolipophorin-III
Short name:
ApoLp-III
OrganismiManduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Taxonomic identifieri7130 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaSphingidaeSphinginaeSphinginiManduca

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 235PRO_0000002047
Chaini24 – 189166Apolipophorin-3PRO_0000002048Add
BLAST

Keywords - PTMi

Cleavage on pair of basic residues

Expressioni

Tissue specificityi

Hemolymph.

Interactioni

Subunit structurei

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.

Structurei

Secondary structure

1
189
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 283Combined sources
Helixi34 – 5320Combined sources
Helixi64 – 8825Combined sources
Helixi95 – 11117Combined sources
Helixi112 – 1154Combined sources
Helixi118 – 1225Combined sources
Beta strandi125 – 1273Combined sources
Helixi128 – 15023Combined sources
Helixi158 – 1603Combined sources
Helixi161 – 18525Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EQ1NMR-A24-189[»]
SMRiP13276. Positions 24-189.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13276.

Family & Domainsi

Sequence similaritiesi

Belongs to the insect apolipophorin-3 family.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

InterProiIPR010009. ApoLp-III.
[Graphical view]
PfamiPF07464. ApoLp-III. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13276-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAKFVVVLA ACVALSHSAM VRRDAPAGGN AFEEMEKHAK EFQKTFSEQF
60 70 80 90 100
NSLVNSKNTQ DFNKALKDGS DSVLQQLSAF SSSLQGAISD ANGKAKEALE
110 120 130 140 150
QARQNVEKTA EELRKAHPDV EKEANAFKDK LQAAVQTTVQ ESQKLAKEVA
160 170 180
SNMEETNKKL APKIKQAYDD FVKHAEEVQK KLHEAATKQ
Length:189
Mass (Da):20,793
Last modified:January 1, 1990 - v1
Checksum:iB1412640AB622169
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17286 mRNA. Translation: AAA29301.1.
M79326 Genomic DNA. Translation: AAA29300.1.
PIRiA29793.

Cross-referencesi

Web resourcesi

Protein Spotlight

Lipid freight - Issue 59 of June 2005

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17286 mRNA. Translation: AAA29301.1.
M79326 Genomic DNA. Translation: AAA29300.1.
PIRiA29793.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EQ1NMR-A24-189[»]
SMRiP13276. Positions 24-189.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP13276.

Family and domain databases

InterProiIPR010009. ApoLp-III.
[Graphical view]
PfamiPF07464. ApoLp-III. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1986) [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(1990)
    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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 24-189.

Entry informationi

Entry nameiAPL3_MANSE
AccessioniPrimary (citable) accession number: P13276
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 1, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.