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Peritrophin-48

 PE48_CHRBE              Reviewed;         379 AA.
O17450; Q9XZF7;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 62.
RecName: Full=Peritrophin-48;
Flags: Precursor;
Chrysomya bezziana (Old world screw-worm fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Oestroidea; Calliphoridae; Chrysomyinae; Chrysomya.
NCBI_TaxID=69364;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Larval peritrophic membrane;
PubMed=11439251; DOI=10.1016/S0965-1748(01)00039-X;
Vuocolo T., Eisemann C.H., Pearson R.D., Willadsen P., Tellam R.L.;
"Identification and molecular characterisation of a peritrophin gene,
peritrophin-48, from the myiasis fly Chrysomya bezziana.";
Insect Biochem. Mol. Biol. 31:919-932(2001).
-!- FUNCTION: Binds chitin and may bind related oligosaccharide
structures.
-!- TISSUE SPECIFICITY: Larval peritrophic membrane.
-!- PTM: Glycosylated.
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EMBL; AF030557; AAB86623.1; -; mRNA.
EMBL; AF139718; AAD25103.1; -; Genomic_DNA.
ProteinModelPortal; O17450; -.
SMR; O17450; -.
GO; GO:0005576; C:extracellular region; IEA:InterPro.
GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
GO; GO:0006030; P:chitin metabolic process; IEA:InterPro.
Gene3D; 2.170.140.10; -; 5.
InterPro; IPR002557; Chitin-bd_dom.
InterPro; IPR036508; Chitin-bd_dom_sf.
Pfam; PF01607; CBM_14; 4.
SMART; SM00494; ChtBD2; 5.
SUPFAM; SSF57625; SSF57625; 4.
PROSITE; PS50940; CHIT_BIND_II; 5.
2: Evidence at transcript level;
Chitin-binding; Disulfide bond; Glycoprotein; Repeat; Signal.
SIGNAL 1 20
CHAIN 21 379 Peritrophin-48.
/FTId=PRO_0000023614.
DOMAIN 25 83 Chitin-binding type-2 1.
{ECO:0000255|PROSITE-ProRule:PRU00144}.
DOMAIN 86 143 Chitin-binding type-2 2.
{ECO:0000255|PROSITE-ProRule:PRU00144}.
DOMAIN 151 208 Chitin-binding type-2 3.
{ECO:0000255|PROSITE-ProRule:PRU00144}.
DOMAIN 224 283 Chitin-binding type-2 4.
{ECO:0000255|PROSITE-ProRule:PRU00144}.
DOMAIN 285 356 Chitin-binding type-2 5.
{ECO:0000255|PROSITE-ProRule:PRU00144}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 168 168 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 247 247 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 252 252 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 356 356 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 373 373 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 60 73 {ECO:0000255|PROSITE-ProRule:PRU00144}.
DISULFID 120 133 {ECO:0000255|PROSITE-ProRule:PRU00144}.
DISULFID 185 198 {ECO:0000255|PROSITE-ProRule:PRU00144}.
DISULFID 324 337 {ECO:0000255|PROSITE-ProRule:PRU00144}.
CONFLICT 159 159 N -> H (in Ref. 1; AAD25103).
{ECO:0000305}.
CONFLICT 167 167 K -> T (in Ref. 1; AAD25103).
{ECO:0000305}.
CONFLICT 236 236 L -> I (in Ref. 1; AAD25103).
{ECO:0000305}.
CONFLICT 263 263 G -> S (in Ref. 1; AAD25103).
{ECO:0000305}.
CONFLICT 278 278 Q -> P (in Ref. 1; AAD25103).
{ECO:0000305}.
CONFLICT 282 282 L -> F (in Ref. 1; AAD25103).
{ECO:0000305}.
CONFLICT 286 286 N -> I (in Ref. 1; AAD25103).
{ECO:0000305}.
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


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