PE48A_LUCCU
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 25-MAY-2022, entry version 78.
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 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; SSF57625; 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