PE44_LUCCU
ID PE44_LUCCU Reviewed; 356 AA.
AC Q25255;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Peritrophin-44;
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 [MRNA], PROTEIN SEQUENCE OF 24-80; 83-88; 215-232;
RP 254-267; 271-300; 303-308 AND 311-356, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
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 have roles in the maintenance of peritrophic membrane
CC structure and in the determination of the porosity of the peritrophic
CC membrane. May bind chitin or related oligosaccharide structures.
CC -!- TISSUE SPECIFICITY: Larval peritrophic membrane.
CC {ECO:0000269|PubMed:8621536}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all 3 larval instars and to a very
CC low extent in adults, but not pupae or eggs.
CC {ECO:0000269|PubMed:8621536}.
CC -!- PTM: Glycosylated.
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DR EMBL; L25106; AAC37261.1; -; mRNA.
DR AlphaFoldDB; Q25255; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR Pfam; PF01607; CBM_14; 2.
DR SMART; SM00494; ChtBD2; 4.
DR SUPFAM; SSF57625; SSF57625; 4.
DR PROSITE; PS50940; CHIT_BIND_II; 4.
PE 1: Evidence at protein level;
KW Chitin-binding; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Repeat; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:8621536"
FT CHAIN 24..356
FT /note="Peritrophin-44"
FT /id="PRO_0000023613"
FT DOMAIN 28..85
FT /note="Chitin-binding type-2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 88..146
FT /note="Chitin-binding type-2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 147..201
FT /note="Chitin-binding type-2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 220..283
FT /note="Chitin-binding type-2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 286..355
FT /note="Chitin-binding type-2 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 122..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 181..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 262..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
SQ SEQUENCE 356 AA; 38711 MW; 47B6774631CDC60F CRC64;
MKELQITTGC LLLMVAAIGK TSAIYSMSET CEYTPDGFIA DPNSCQSYGY CKNNQLVGTG
KCPDGYLYNN KLGICDSPAN VKCISDSKNA CLHATDNSFV ADPTNCNGYC YCSNKTATCT
TCPEFQLFDS KQIKCVYALE KPECTADSIC RLVPNAVYVG NPNECGEYIS CFNGIGTEGR
CASGYFNKQL GGCQTTNPCL ASSPNPDIGL GVIENLADNN FVCQVNGGNP TEEKPVFISD
GQTCMGYYKC TSRNGPGIWG KCPKGLHFNE GKCVTPFTFP CTFDRCGNLN REFVGAIRTE
CKNFLICKNE TSQGMAYNYA KYIGLPCTDK NYPFFNEVSG TCEKTSPKSD TYKLCV
