ID   PE48A_LUCCU             Reviewed;         375 AA.
AC   P91745;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   22-FEB-2023, entry version 80.
DE   RecName: Full=Peritrophin-48;
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 {ECO:0000312|EMBL:AAB38414.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-47; 60-68; 93-101;
RP   185-196 AND 239-256, AND TISSUE SPECIFICITY.
RC   TISSUE=Larval peritrophic membrane;
RX   PubMed=9639876; DOI=10.1016/s0965-1748(97)00103-3;
RA   Schorderet S., Pearson R.D., Vuocolo T., Eisemann C.H., Riding G.A.,
RA   Tellam R.L.;
RT   "cDNA and deduced amino acid sequences of a peritrophic membrane
RT   glycoprotein, 'peritrophin-48', from the larvae of Lucilia cuprina.";
RL   Insect Biochem. Mol. Biol. 28:99-111(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-49.
RC   TISSUE=Larval peritrophic membrane;
RX   PubMed=8621536; DOI=10.1074/jbc.271.15.8925;
RA   Elvin C.M., Vuocolo T., Pearson R.D., East I.J., Riding G.A.,
RA   Eisemann C.H., Tellam R.L.;
RT   "Characterization of a major peritrophic membrane protein, peritrophin-44,
RT   from the larvae of Lucilia cuprina. cDNA and deduced amino acid
RT   sequences.";
RL   J. Biol. Chem. 271:8925-8935(1996).
CC   -!- FUNCTION: May bind chitin or related oligosaccharide structures.
CC       {ECO:0000303|PubMed:9639876}.
CC   -!- TISSUE SPECIFICITY: Cardia and midgut peritrophic membrane.
CC       {ECO:0000269|PubMed:9639876}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in all 3 larval instars and adults, but
CC       not pupae or eggs.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:9639876}.
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DR   EMBL; U79715; AAB38414.1; -; mRNA.
DR   AlphaFoldDB; P91745; -.
DR   SMR; P91745; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR   Gene3D; 2.170.140.10; Chitin binding domain; 1.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
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   1: Evidence at protein level;
KW   Chitin-binding; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Repeat; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:8621536,
FT                   ECO:0000269|PubMed:9639876"
FT   CHAIN           21..375
FT                   /note="Peritrophin-48"
FT                   /id="PRO_0000023615"
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          153..210
FT                   /note="Chitin-binding type-2 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DOMAIN          224..292
FT                   /note="Chitin-binding type-2 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DOMAIN          294..360
FT                   /note="Chitin-binding type-2 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        360
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        187..200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        265..278
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        330..343
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
SQ   SEQUENCE   375 AA;  41318 MW;  459082BF0AF6C7AF CRC64;
     MIIKTLLASV AIMLIATVNA EYNVAKYCEL VKIGTLMPSM ISCQDYYICR LNNQPIPVKC
     GANTVFDKDT QGCVPEAQAN CILSLDNPCE NKDRTFAPSS KACNEWHYCL NGNIVANGSC
     QPGQIFDASK NSCIYGACNS DDDDSNSDFT PVLNICDIMQ NGQFFGDFEN CQNWQKCNNG
     RLQKGICLGN LVYDTKNGMC LQNDGTMCER TNGMVSEDGG APDETLCTSS NDGPLPDKLT
     CSVYYICEQD TTSTPTTYKW IKTSCPNGQY FDVFGDGCLD RAKRRVYTGC NRCEYTTGST
     TYWVNAVSND CTKFSTCRNG RKITNEDGSC NSGYYFNEAD QYCNMGDFTN YAETNGACQN
     YSCNGYDCTT KPSAT
//