ID   PE48_CHRBE              Reviewed;         379 AA.
AC   O17450; Q9XZF7;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Peritrophin-48;
DE   Flags: Precursor;
OS   Chrysomya bezziana (Old world screw-worm fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Chrysomyinae; Chrysomya.
OX   NCBI_TaxID=69364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Larval peritrophic membrane;
RX   PubMed=11439251; DOI=10.1016/s0965-1748(01)00039-x;
RA   Vuocolo T., Eisemann C.H., Pearson R.D., Willadsen P., Tellam R.L.;
RT   "Identification and molecular characterisation of a peritrophin gene,
RT   peritrophin-48, from the myiasis fly Chrysomya bezziana.";
RL   Insect Biochem. Mol. Biol. 31:919-932(2001).
CC   -!- FUNCTION: Binds chitin and may bind related oligosaccharide structures.
CC   -!- TISSUE SPECIFICITY: Larval peritrophic membrane.
CC   -!- PTM: Glycosylated.
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DR   EMBL; AF030557; AAB86623.1; -; mRNA.
DR   EMBL; AF139718; AAD25103.1; -; Genomic_DNA.
DR   AlphaFoldDB; O17450; -.
DR   SMR; O17450; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.170.140.10; Chitin binding domain; 1.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
DR   PANTHER; PTHR23301; CHITIN BINDING PERITROPHIN-A; 1.
DR   PANTHER; PTHR23301:SF110; FI03257P-RELATED; 1.
DR   Pfam; PF01607; CBM_14; 4.
DR   SMART; SM00494; ChtBD2; 5.
DR   SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 4.
DR   PROSITE; PS50940; CHIT_BIND_II; 5.
PE   2: Evidence at transcript level;
KW   Chitin-binding; Disulfide bond; Glycoprotein; Repeat; Signal.
FT   SIGNAL          1..20
FT   CHAIN           21..379
FT                   /note="Peritrophin-48"
FT                   /id="PRO_0000023614"
FT   DOMAIN          25..83
FT                   /note="Chitin-binding type-2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DOMAIN          86..143
FT                   /note="Chitin-binding type-2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DOMAIN          151..208
FT                   /note="Chitin-binding type-2 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DOMAIN          224..283
FT                   /note="Chitin-binding type-2 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DOMAIN          285..356
FT                   /note="Chitin-binding type-2 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        356
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        373
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        60..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        120..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        185..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        324..337
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   CONFLICT        159
FT                   /note="N -> H (in Ref. 1; AAD25103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="K -> T (in Ref. 1; AAD25103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        236
FT                   /note="L -> I (in Ref. 1; AAD25103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        263
FT                   /note="G -> S (in Ref. 1; AAD25103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        278
FT                   /note="Q -> P (in Ref. 1; AAD25103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        282
FT                   /note="L -> F (in Ref. 1; AAD25103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        286
FT                   /note="N -> I (in Ref. 1; AAD25103)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   379 AA;  40829 MW;  FCDCC6AAE7976479 CRC64;
     MKAKTLTATL ALILLAFAQA DYDVASYCQL VQSGTKLPSL DSCQNYYTCV SNGLPTLSSC
     SSGYVFNKDS QQCVPTGSFN CFFGVANPCQ NQDKKFVPSA KQCNEWHYCL AGAIAGTGTC
     KEGQIFNFAK QSCVYGECSN TGNNILDSPN LSVCQIMPNG IYFGDNKNCS TWHKCSGMEE
     KKGTCPNGDN FDPTYASCVP SNMPACSRIQ NPPSTGVVSG PPSTSPCSLG TVVGDLTSCS
     VYYKCENATR SNSTIWNTYT CSGQFFDVIS KQCTSTNQAR TLKGCNRCQF TTGSMYWVNA
     VDPQCSEYFT CSNGLETKST ASTCGAGNFF NEDLQYCMIG NSTVGQYAQT HGACENYTCN
     PNTRLCNLVT ATNTTSSHR
//