ID   PE55_LUCCU              Reviewed;         220 AA.
AC   Q95UE8; Q8MUP5;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2003, sequence version 2.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Peritrophin-55;
DE   Flags: Precursor;
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 20-57 AND
RP   60-94, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Larva;
RX   PubMed=12535682; DOI=10.1016/s0965-1748(02)00208-4;
RA   Tellam R.L., Vuocolo T., Eisemann C.H., Briscoe S., Riding G.A.,
RA   Elvin C.M., Pearson R.D.;
RT   "Identification of an immuno-protective mucin-like protein, peritrophin-55,
RT   from the peritrophic matrix of Lucilia cuprina larvae.";
RL   Insect Biochem. Mol. Biol. 33:239-252(2003).
CC   -!- FUNCTION: May bind oligosaccharide structures.
CC   -!- TISSUE SPECIFICITY: Larval peritrophic membrane.
CC       {ECO:0000269|PubMed:12535682}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in all 3 larval instars but not adults
CC       or eggs. {ECO:0000269|PubMed:12535682}.
CC   -!- PTM: Glycosylated.
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DR   EMBL; AY055470; AAL15463.1; -; mRNA.
DR   EMBL; AF515826; AAM55223.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q95UE8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
DR   SUPFAM; SSF57625; SSF57625; 1.
DR   PROSITE; PS50940; CHIT_BIND_II; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:12535682"
FT   CHAIN           20..220
FT                   /note="Peritrophin-55"
FT                   /id="PRO_0000023618"
FT   DOMAIN          33..95
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   REGION          116..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..211
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        68..84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   CONFLICT        67
FT                   /note="D -> H (in Ref. 1; AAL15463)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="P -> F (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        142
FT                   /note="I -> P (in Ref. 1; AAM55223)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        164
FT                   /note="V -> G (in Ref. 1; AAM55223)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190
FT                   /note="S -> P (in Ref. 1; AAM55223)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   220 AA;  23535 MW;  88C74ED57F2ED7C7 CRC64;
     MKSVFVCTLV LALAHHAFAG VCDSNVDYNS TLITPCLGND IIVLWPNYLN FNTYYKCVEF
     GKPQLMDCPP NTYFTYYFQQ CTGCDNFIPA PTCEYLKQTT DVECVPLVKP TTAAPTTLKT
     TPSKTTPIVT TAPPSTPVPS TIVTNKPDPT TPKTTKPPKV TTTVNPSPPT GTGPATNAPS
     SDIPLPPIAS TVNTKYPTPP GMPPTPPSFG TPPSIVQLQN