ID   APLP1_GALME             Reviewed;          23 AA.
AC   C0HKF3;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Apolipophorin-1 {ECO:0000303|PubMed:29289504};
DE   AltName: Full=Apolipophorin-I {ECO:0000303|PubMed:29289504};
DE            Short=apoLp-I {ECO:0000303|PubMed:29289504};
DE   Flags: Fragment;
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 {ECO:0000303|PubMed:29289504};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Hemolymph {ECO:0000303|PubMed:29289504};
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: Constitutes the major component of lipophorin, which mediates
CC       transport for various types of lipids in hemolymph. Acts by forming
CC       lipoprotein particles that bind lipoproteins and lipids (By
CC       similarity). {ECO:0000250|UniProtKB:Q9V496}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29289504}.
CC       Note=Secreted into hemolymph. {ECO:0000269|PubMed:29289504}.
CC   -!- TISSUE SPECIFICITY: Expressed in hemolymph.
CC       {ECO:0000269|PubMed:29289504}.
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   AlphaFoldDB; C0HKF3; -.
DR   Proteomes; UP000504614; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lipid transport; Lipid-binding;
KW   Reference proteome; Secreted; Transport.
FT   CHAIN           1..>23
FT                   /note="Apolipophorin-1"
FT                   /evidence="ECO:0000269|PubMed:29289504"
FT                   /id="PRO_0000443524"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         23
FT                   /evidence="ECO:0000303|PubMed:29289504"
SQ   SEQUENCE   23 AA;  2606 MW;  5437BD4D2B0B0E1F CRC64;
     SVKSEVDNFD KHLKAESAPF NNE