ID   APL3_MELSA              Reviewed;          23 AA.
AC   P86829;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   11-DEC-2019, entry version 8.
DE   RecName: Full=Apolipophorin-3 {ECO:0000250|UniProtKB:P13276};
DE   AltName: Full=Apolipophorin-III;
DE            Short=ApoLp-III {ECO:0000250|UniProtKB:P13276};
DE   Flags: Fragment;
OS   Melanoplus sanguinipes (Migratory grasshopper).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC   Acridoidea; Acrididae; Melanoplinae; Melanoplini; Melanoplus.
OX   NCBI_TaxID=65742;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Hemolymph;
RA   Jones N.T., Montemayor T.T., Greenburg B., Rankin M.A.;
RL   Submitted (SEP-2010) to UniProtKB.
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).
CC       {ECO:0000250|UniProtKB:P13276}.
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|UniProtKB:P13276}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the insect apolipophorin-3 family.
CC       {ECO:0000255}.
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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; Lipid transport; Secreted; Transport.
FT   CHAIN           1..>23
FT                   /note="Apolipophorin-3"
FT                   /id="PRO_0000402827"
FT   NON_TER         23
SQ   SEQUENCE   23 AA;  2381 MW;  8907ADC88E74F368 CRC64;
     DAAQVPDFAT AVQNLXHTLS EAA