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Protein

Peritrophin-48

Gene
N/A
Organism
Chrysomya bezziana (Old world screw-worm fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Binds chitin and may bind related oligosaccharide structures.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Chitin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Peritrophin-48
OrganismiChrysomya bezziana (Old world screw-worm fly)
Taxonomic identifieri69364 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaOestroideaCalliphoridaeChrysomyinaeChrysomya

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
ChainiPRO_000002361421 – 379Peritrophin-48Add BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi60 ↔ 73PROSITE-ProRule annotation
Disulfide bondi120 ↔ 133PROSITE-ProRule annotation
Glycosylationi150N-linked (GlcNAc...)Sequence analysis1
Glycosylationi168N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi185 ↔ 198PROSITE-ProRule annotation
Glycosylationi247N-linked (GlcNAc...)Sequence analysis1
Glycosylationi252N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi324 ↔ 337PROSITE-ProRule annotation
Glycosylationi341N-linked (GlcNAc...)Sequence analysis1
Glycosylationi356N-linked (GlcNAc...)Sequence analysis1
Glycosylationi373N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Larval peritrophic membrane.

Structurei

3D structure databases

ProteinModelPortaliO17450.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 83Chitin-binding type-2 1PROSITE-ProRule annotationAdd BLAST59
Domaini86 – 143Chitin-binding type-2 2PROSITE-ProRule annotationAdd BLAST58
Domaini151 – 208Chitin-binding type-2 3PROSITE-ProRule annotationAdd BLAST58
Domaini224 – 283Chitin-binding type-2 4PROSITE-ProRule annotationAdd BLAST60
Domaini285 – 356Chitin-binding type-2 5PROSITE-ProRule annotationAdd BLAST72

Sequence similaritiesi

Contains 5 chitin-binding type-2 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.170.140.10. 5 hits.
InterProiIPR002557. Chitin-bd_dom.
[Graphical view]
PfamiPF01607. CBM_14. 4 hits.
[Graphical view]
SMARTiSM00494. ChtBD2. 5 hits.
[Graphical view]
SUPFAMiSSF57625. SSF57625. 4 hits.
PROSITEiPS50940. CHIT_BIND_II. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O17450-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAKTLTATL ALILLAFAQA DYDVASYCQL VQSGTKLPSL DSCQNYYTCV
60 70 80 90 100
SNGLPTLSSC SSGYVFNKDS QQCVPTGSFN CFFGVANPCQ NQDKKFVPSA
110 120 130 140 150
KQCNEWHYCL AGAIAGTGTC KEGQIFNFAK QSCVYGECSN TGNNILDSPN
160 170 180 190 200
LSVCQIMPNG IYFGDNKNCS TWHKCSGMEE KKGTCPNGDN FDPTYASCVP
210 220 230 240 250
SNMPACSRIQ NPPSTGVVSG PPSTSPCSLG TVVGDLTSCS VYYKCENATR
260 270 280 290 300
SNSTIWNTYT CSGQFFDVIS KQCTSTNQAR TLKGCNRCQF TTGSMYWVNA
310 320 330 340 350
VDPQCSEYFT CSNGLETKST ASTCGAGNFF NEDLQYCMIG NSTVGQYAQT
360 370
HGACENYTCN PNTRLCNLVT ATNTTSSHR
Length:379
Mass (Da):40,829
Last modified:January 1, 1998 - v1
Checksum:iFCDCC6AAE7976479
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti159N → H in AAD25103 (PubMed:11439251).Curated1
Sequence conflicti167K → T in AAD25103 (PubMed:11439251).Curated1
Sequence conflicti236L → I in AAD25103 (PubMed:11439251).Curated1
Sequence conflicti263G → S in AAD25103 (PubMed:11439251).Curated1
Sequence conflicti278Q → P in AAD25103 (PubMed:11439251).Curated1
Sequence conflicti282L → F in AAD25103 (PubMed:11439251).Curated1
Sequence conflicti286N → I in AAD25103 (PubMed:11439251).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030557 mRNA. Translation: AAB86623.1.
AF139718 Genomic DNA. Translation: AAD25103.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030557 mRNA. Translation: AAB86623.1.
AF139718 Genomic DNA. Translation: AAD25103.1.

3D structure databases

ProteinModelPortaliO17450.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.170.140.10. 5 hits.
InterProiIPR002557. Chitin-bd_dom.
[Graphical view]
PfamiPF01607. CBM_14. 4 hits.
[Graphical view]
SMARTiSM00494. ChtBD2. 5 hits.
[Graphical view]
SUPFAMiSSF57625. SSF57625. 4 hits.
PROSITEiPS50940. CHIT_BIND_II. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPE48_CHRBE
AccessioniPrimary (citable) accession number: O17450
Secondary accession number(s): Q9XZF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.