ID   APL3_HELVI              Reviewed;          35 AA.
AC   P86356;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Apolipophorin-3 {ECO:0000250|UniProtKB:P13276};
DE   AltName: Full=Apolipophorin-III {ECO:0000303|PubMed:12031477};
DE            Short=ApoLp-III {ECO:0000303|PubMed:12031477};
DE   Flags: Fragment;
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, INDUCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Hemolymph {ECO:0000269|PubMed:12031477};
RX   PubMed=12031477; DOI=10.1016/s1096-4959(02)00064-7;
RA   Chung K.T., Ourth D.D.;
RT   "Purification and characterization of apolipophorin III from immune
RT   hemolymph of Heliothis virescens pupae.";
RL   Comp. Biochem. Physiol. 132:505-514(2002).
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). Has hemagglutinating
CC       activity towards rabbit erythrocytes. {ECO:0000250|UniProtKB:P13276,
CC       ECO:0000269|PubMed:12031477}.
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|UniProtKB:P13276}.
CC   -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000305}.
CC   -!- INDUCTION: By bacterial infection. {ECO:0000269|PubMed:12031477}.
CC   -!- MASS SPECTROMETRY: Mass=17965.9; Mass_error=5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12031477};
CC   -!- SIMILARITY: Belongs to the insect apolipophorin-3 family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P86356; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hemagglutinin; Lipid transport; Secreted;
KW   Transport.
FT   CHAIN           1..>35
FT                   /note="Apolipophorin-3"
FT                   /id="PRO_0000392512"
FT   NON_TER         35
FT                   /evidence="ECO:0000303|PubMed:12031477"
SQ   SEQUENCE   35 AA;  3830 MW;  D81AA1DA36230787 CRC64;
     DAPASPLADI EKHAAEFQKT ISEQFNSLVN SKNTQ