ID   APL3_HYPCU              Reviewed;         187 AA.
AC   Q6VU70;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Apolipophorin-3;
DE   AltName: Full=Apolipophorin-III;
DE            Short=ApoLp-III;
DE   Flags: Precursor;
OS   Hyphantria cunea (Fall webworm moth) (Phalaena cunea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Erebidae; Arctiinae; Hyphantria.
OX   NCBI_TaxID=39466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15475296; DOI=10.1016/j.ibmb.2004.05.005;
RA   Kim H.-J., Je H.-J., Park S.-Y., Lee I.-H., Jin B.-R., Yun H.-K.,
RA   Yun C.-Y., Han Y.-S., Kang Y.-J., Seo S.-J.;
RT   "Immune activation of apolipophorin-III and its distribution in hemocyte
RT   from Hyphantria cunea.";
RL   Insect Biochem. Mol. Biol. 34:1011-1023(2004).
CC   -!- FUNCTION: Assists in the loading of diacylglycerol, generated from
CC       triacylglycerol stores in the fat body through the action of
CC       adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. It
CC       increases the lipid carrying capacity of lipophorin by covering the
CC       expanding hydrophobic surface resulting from diacylglycerol uptake. It
CC       thus plays a critical role in the transport of lipids during flight in
CC       several species of insects (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Equilibrium between a soluble monomer and a bound lipoprotein
CC       form. Apolipophorin-3 associates with lipophorin during lipid loading
CC       until each particle contains 9 or 14 molecules of apolipophorin-3 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Hemolymph.
CC   -!- SIMILARITY: Belongs to the insect apolipophorin-3 family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Lipid freight - Issue 59 of
CC       June 2005;
CC       URL="https://web.expasy.org/spotlight/back_issues/059";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY327106; AAQ24031.1; -; mRNA.
DR   AlphaFoldDB; Q6VU70; -.
DR   SMR; Q6VU70; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR010009; ApoLp-III.
DR   Pfam; PF07464; ApoLp-III; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Lipid transport; Secreted; Signal;
KW   Transport.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..22
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000002044"
FT   CHAIN           23..187
FT                   /note="Apolipophorin-3"
FT                   /id="PRO_0000002045"
SQ   SEQUENCE   187 AA;  20746 MW;  9B1B934661892869 CRC64;
     MAAKFIILLA LFALSQASVV RRDAPLANFL QDLEKRAADI QKTFSEQFQA ISNSKNVQDV
     NKAVKESSDV VLKQLSTLSS SLQSALTDAN GKAKEALEQT RQNLEKTAEE LRRAHPDVEK
     QANQLRDKLQ AAVQSTLQET QKLAKEVAAN MEQTNEKLAP KIKEAFEDFV KQAEAVQKKV
     HDAATKQ