ID   APLP_GALME              Reviewed;        1515 AA.
AC   Q68YP1;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Apolipophorin {ECO:0000303|PubMed:16386790};
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:0000312|EMBL:AAT76806.1};
RN   [1] {ECO:0000312|EMBL:AAT76806.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16386790; DOI=10.1016/j.dci.2005.09.003;
RA   Ma G., Hay D., Li D., Asgari S., Schmidt O.;
RT   "Recognition and inactivation of LPS by lipophorin particles.";
RL   Dev. Comp. Immunol. 30:619-626(2006).
RN   [2] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=34443685; DOI=10.3390/molecules26165097;
RA   Staczek S., Zdybicka-Barabas A., Wojda I., Wiater A., Mak P., Suder P.,
RA   Skrzypiec K., Cytrynska M.;
RT   "Fungal alpha-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in
RT   the Insect Model Host Galleria mellonella.";
RL   Molecules 26:5097-5097(2021).
CC   -!- FUNCTION: Mediates transport for various types of lipids in hemolymph
CC       (Probable). Acts by forming lipoprotein particles that bind
CC       lipoproteins and lipids (Probable). Binds the A.niger cell wall
CC       component alpha-1,3-glucan, a fungal pathogen-associated molecular
CC       pattern (PAMP) that activates the host immune response
CC       (PubMed:34443685). {ECO:0000269|PubMed:34443685, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34443685}.
CC       Note=Secreted in the hemolymph. {ECO:0000269|PubMed:34443685}.
CC   -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|PubMed:34443685}.
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DR   EMBL; AY661711; AAT76806.1; -; mRNA.
DR   Proteomes; UP000504614; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001846; VWF_type-D.
DR   Pfam; PF00094; VWD; 1.
DR   SMART; SM00216; VWD; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS51233; VWFD; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Disulfide bond; Glycoprotein; Lipid transport; Lipid-binding;
KW   Reference proteome; Secreted; Transport.
FT   CHAIN           <1..>1515
FT                   /note="Apolipophorin"
FT                   /id="PRO_0000455042"
FT   DOMAIN          952..1118
FT                   /note="VWFD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   CARBOHYD        988
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        976..1117
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:AAT76806.1"
FT   NON_TER         1515
FT                   /evidence="ECO:0000312|EMBL:AAT76806.1"
SQ   SEQUENCE   1515 AA;  167273 MW;  137D980549C5D045 CRC64;
     EGEKHVGNVE VKAQYGKGKS VNLVVNGAAX PQEYDLDIKA NAPQAENLKK LDLSLKTKNP
     SPDTYVVLVA IDADGRVYKS QSTVVYSEAN PLIDVSYTAP NTPTSRLYVK GVKLSENQAK
     VEVKIVNIRD LSLDAVSEAT LQKDNIILKV VANSEKLGLK NYKVDVATKD ANNNGKRLEF
     QATNDNKNVL SGSTTFISKQ ENKKTIIEGS GTLKVKEEQK SANFKYIRTI LTEGNEQGVE
     TFLNLAVGES SYVAESRITN LEYKNSYVYC EEKKQCAHVE LNSKVNIQKP GVVQHTVNVN
     FDLVKLGISP EFGLQITNEI SEKKLPQYTL DLHAIKNDKK YHLNIYSHPE LGKFPAGITV
     TLPHRVLALE TRVEYPTNKG LPFPIKGEIT IHPDKRKAQY KTAARFLVDV TGSDKQHALI
     ADFGFSHPKL GKEALFKVRG NLKNSDNIIE IATSASVSCH PIFGADRESK FVLQVSPSSF
     KLLLDTPIVK VIELEGTAVV KENLQQGDLK FCLLQGKPVA VRALIKDYQY YEFTTDESDR
     KLSVIGHLDP EKRVDISADL VLSGEKKNIA HGALFLKDNL VKSEYGASKD NFDYFVTALK
     NDLTNLEARV KQLGEEINSD FKDILKRAQP KIQELEKAYK EDLEKIYQEV ANDETLKNSQ
     VINEVAQFLA KIIDDIVHAF KPLVDKVYNV IVETTKKIEE IYEKEIAPQI KSLYETVASI
     VKEFFDGLLD IVAHYAALIT DFYEKHKPEL EELTNTITEI FKDLTRIIVI QLKELKATVG
     QALEAIITTI KETQNSVVTA LQAKYEELGV PESVLNAILE AHNAIRALLP TEETKNFADA
     VYTYVSKKLR SEKFDEQAQL RVVYEKFTVA LQSLIQFLRG QFNQFGIPSL FNIESIPFIT
     GPGQLSYTPT GVGASLSLVN QILRGDIPDP LSLIQAYRPR SLDPFDEIPA KLRGVVVNGQ
     HIFTFDGRHL TFPGNCRYVL AHDYVDRNFT LVLQLQNGKP KSLILEDKSG TTVELKNNGQ
     VAVNGASHGY PVEEKDVYAF RRPDGVLGIG SQYGALAYCS AKLEVCYFEI NGFYLGKLRG
     LLGDGNNEAY DDFRLPNGKI STSESEFGNS YRLASSCPQA KCPEHSHHQQ HAALPPACEQ
     VFGGTSTLRP LSLVLDVAPF RQACIHAVAG NAENALREAC SLGAGYVALG LGTLLPAVLP
     PACVRCTDAG GSKNIGDTYE VKLPNKQADI LVVIETTKSN EKKDKDLVVP LVSQVVDTTR
     NLVVPWNLKS KHIAGIKVYL IGVTSRFPYP IVYDTDLKLK SAKVAFNDEH RYQYTPTIKT
     NCEKADSIQK TIANVIDEIR IVLGLSNINA GYLSAFETPL RPGALKHVIT VNGDACKLEI
     GTPLQAISNI ITYNQLGITH SLVASIPGLE VDGKSAPNVI GYTNDYALEF DGKKHAKEVQ
     GAKVTLTEDN YCAELTEVTD GLVLSATNYN ALGAGERKQF LLAAANAITQ RILQESIVEE
     CVCNYANPFV GRSAC