ID   APL3_SPOLT              Reviewed;         188 AA.
AC   O77248;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Apolipophorin-3;
DE   AltName: Full=Apolipophorin-III;
DE            Short=ApoLp-III;
DE   Flags: Precursor;
OS   Spodoptera litura (Asian cotton leafworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Amphipyrinae; Spodoptera.
OX   NCBI_TaxID=69820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-28, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Fat body;
RX   PubMed=9880904;
RX   DOI=10.1002/(sici)1520-6327(1998)39:4<166::aid-arch4>3.0.co;2-t;
RA   Kim E., Kim S.H., Choi C.S., Park Y.I., Kim H.R.;
RT   "Cloning and expression of apolipophorin-III from the common cutworm,
RT   Spodoptera litura.";
RL   Arch. Insect Biochem. Physiol. 39:166-173(1998).
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: Expressed in fat body and secreted in hemolymph.
CC       Also expressed in ovary and testis at lower levels.
CC       {ECO:0000269|PubMed:9880904}.
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";
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DR   EMBL; AF094582; AAC63377.1; -; mRNA.
DR   AlphaFoldDB; O77248; -.
DR   SMR; O77248; -.
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   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Lipid transport; Secreted; Signal; Transport.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..22
FT                   /evidence="ECO:0000269|PubMed:9880904"
FT                   /id="PRO_0000002049"
FT   CHAIN           23..188
FT                   /note="Apolipophorin-3"
FT                   /id="PRO_0000002050"
SQ   SEQUENCE   188 AA;  20649 MW;  7A8AE366DF8E432C CRC64;
     MVAKLFVLVA CIALSHAAMV RRDAPPANTL LQDIEKHAAE IHKTFSEQLN SIANSKNTQE
     VNKAIKDGSD SVLQQLSALS SSLQSAMTDA NAKAKTALEQ ARQNLEKTAE DLRKSHPDVE
     RQAGELRTKL QAAVQNTAQE VQKLAKEVAS NVEETNEKLA PKLKEAYENF SKHVEEVQKK
     VHEAASKQ