ID   APLP3_GALME             Reviewed;         186 AA.
AC   P80703; O76946;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Apolipophorin-3;
DE   AltName: Full=Apolipophorin-III;
DE            Short=ApoLp-III;
DE   Flags: Precursor;
OS   Galleria mellonella (Greater wax moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC   Pyralidae; Galleriinae; Galleria.
OX   NCBI_TaxID=7137;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fat body;
RA   Niere M., Dettloff M., Weise C., Meisslitzer C., Ziegler M., Wiesner A.;
RT   "Functional expression of Galleria mellonella apolipophorin III.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 24-186.
RC   TISSUE=Hemolymph;
RX   PubMed=9853677; DOI=10.1007/bf02780964;
RA   Weise C., Franke P., Kopacek P., Wiesner A.;
RT   "Primary structure of apolipophorin-III from the greater wax moth, Galleria
RT   mellonella.";
RL   J. Protein Chem. 17:633-641(1998).
RN   [3]
RP   PROTEIN SEQUENCE OF 136-186, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RC   TISSUE=Larval hemolymph;
RX   PubMed=17194500; DOI=10.1016/j.peptides.2006.11.010;
RA   Cytrynska M., Mak P., Zdybicka-Barabas A., Suder P., Jakubowicz T.;
RT   "Purification and characterization of eight peptides from Galleria
RT   mellonella immune hemolymph.";
RL   Peptides 28:533-546(2007).
RN   [4]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=29289504; DOI=10.1016/j.jinsphys.2017.12.009;
RA   Staczek S., Zdybicka-Barabas A., Mak P., Sowa-Jasilek A., Kedracka-Krok S.,
RA   Jankowska U., Suder P., Wydrych J., Grygorczuk K., Jakubowicz T.,
RA   Cytrynska M.;
RT   "Studies on localization and protein ligands of Galleria mellonella
RT   apolipophorin III during immune response against different pathogens.";
RL   J. Insect Physiol. 105:18-27(2017).
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. Has antibacterial activity against the
CC       Gram-positive bacteria L.monocytogenes (MIC=6.5 uM). Lacks
CC       antibacterial activity against the Gram-positive bacteria B.circulans,
CC       M.luteus, S.aureus, and S.lutea, and the Gram-negative bacteria E.coli
CC       D31, E.coli ATCC 25922, and S.typhimurium. Lacks antifungal activity
CC       against S.cerevisiae, P.pastoris, Z.marxianus, C.albicans,
CC       C.wickerhamii, A.niger, F.oxysporum, and T.harizianum.
CC       {ECO:0000269|PubMed:17194500}.
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.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17194500,
CC       ECO:0000269|PubMed:29289504}. Note=Secreted into hemolymph.
CC       {ECO:0000269|PubMed:29289504}.
CC   -!- TISSUE SPECIFICITY: Expressed in hemolymph (PubMed:17194500,
CC       PubMed:29289504). Also found in hemocytes and fat body
CC       (PubMed:29289504). {ECO:0000269|PubMed:17194500,
CC       ECO:0000269|PubMed:29289504}.
CC   -!- INDUCTION: By bacterial infection. {ECO:0000269|PubMed:17194500}.
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; AJ006975; CAA07363.1; -; mRNA.
DR   PIR; T09296; T09296.
DR   AlphaFoldDB; P80703; -.
DR   SMR; P80703; -.
DR   Allergome; 3638; Gal m 24kD.
DR   Proteomes; UP000504614; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
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   Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Immunity; Innate immunity; Lipid transport;
KW   Reference proteome; Secreted; Signal; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..23
FT                   /evidence="ECO:0000269|PubMed:9853677"
FT                   /id="PRO_0000002042"
FT   CHAIN           24..186
FT                   /note="Apolipophorin-3"
FT                   /id="PRO_0000002043"
SQ   SEQUENCE   186 AA;  20453 MW;  C79B381E07F5C070 CRC64;
     MAAKYVFVVA ACSALAQAGI VRRDASTPLQ DLEKHAAEFQ KTFSEQLNAF TNSKDTKEFN
     TALKEGSDSV LQQLNALASS LQKALNDANG KAKEALEQTR TNLERTAEEL RRAHPDVERQ
     AGALRDRLQT AVQATVQETQ KLAKTVGANL EETNKKLAPQ IKSAYDDFVK QAQEVQKKLH
     EAASKQ