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Q70PU1 (PGSC2_DROSI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidoglycan-recognition protein SC2

EC=3.5.1.28
Gene names
Name:PGRP-SC2
ORF Names:GD10595
OrganismDrosophila simulans (Fruit fly) [Complete proteome]
Taxonomic identifier7240 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Probably plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity By similarity.

Catalytic activity

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

Cofactor

Zinc By similarity.

Subcellular location

Secreted Potential.

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Ontologies

Keywords
   Biological processImmunity
Innate immunity
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processinnate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

peptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 184164Peptidoglycan-recognition protein SC2
PRO_0000023913

Sites

Metal binding511Zinc By similarity
Metal binding851Zinc By similarity
Metal binding1591Zinc By similarity
Metal binding1671Zinc By similarity

Amino acid modifications

Disulfide bond57 ↔ 63 By similarity

Natural variations

Natural variant121L → V in strain: 08FG. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q70PU1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: BF4070F2313D53C5

FASTA18419,788
        10         20         30         40         50         60 
MANKALILLA VLFCAQAVLG VTIVSKSEWG GRSATSKTSL ASYLSYAVIH HTAGNYCSTK 

        70         80         90        100        110        120 
AACITQLKNI QAYHMDSLGW ADIGYNFLIG GDGNVYEGRG WNVMGAHATN WNSKSIGISF 

       130        140        150        160        170        180 
LGNYNTNTLT SAQITAAKGL LSDAVSRGQI VSGYILYGHR QVGSTECPGT NIWNEIRTWS 


NWKA 

« Hide

References

« Hide 'large scale' references
[1]"The evolution of parasite recognition genes in the innate immune system: purifying selection on Drosophila melanogaster peptidoglycan recognition proteins."
Jiggins F.M., Hurst G.D.D.
J. Mol. Evol. 57:598-605(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C167.4.
[2]"Evolution of genes and genomes on the Drosophila phylogeny."
Drosophila 12 genomes consortium
Nature 450:203-218(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Intragenic Hill-Robertson interference influences selection intensity on synonymous mutations in Drosophila."
Comeron J.M., Guthrie T.B.
Mol. Biol. Evol. 22:2519-2530(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-178.
Strain: Ky-a and Ky-b.
[4]"A new test for selection applied to codon usage in Drosophila simulans and D. mauritiana."
Llopart A., Mabille A., Peters-Hall J.R., Comeron J.M., Kliman R.M.
J. Mol. Evol. 66:224-231(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-178, VARIANT VAL-12.
Strain: 01FG, 02FG, 03FG, 04FG, 05FG, 06FG, 07FG, 08FG, 09FG, 10FG, 11FG, 12FG, 13FG, 14FG, 15FG and 16FG.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ556611 Genomic DNA. Translation: CAD89176.1.
CM000362 Genomic DNA. Translation: EDX06229.1.
DQ138765 Genomic DNA. Translation: ABA86371.1.
DQ138766 Genomic DNA. Translation: ABA86372.1.
EU313688 Genomic DNA. Translation: ABY56488.1.
EU313689 Genomic DNA. Translation: ABY56489.1.
EU313690 Genomic DNA. Translation: ABY56490.1.
EU313691 Genomic DNA. Translation: ABY56491.1.
EU313692 Genomic DNA. Translation: ABY56492.1.
EU313693 Genomic DNA. Translation: ABY56493.1.
EU313694 Genomic DNA. Translation: ABY56494.1.
EU313695 Genomic DNA. Translation: ABY56495.1.
EU313696 Genomic DNA. Translation: ABY56496.1.
EU313697 Genomic DNA. Translation: ABY56497.1.
EU313698 Genomic DNA. Translation: ABY56498.1.
EU313699 Genomic DNA. Translation: ABY56499.1.
EU313700 Genomic DNA. Translation: ABY56500.1.
EU313701 Genomic DNA. Translation: ABY56501.1.
EU313702 Genomic DNA. Translation: ABY56502.1.
EU313703 Genomic DNA. Translation: ABY56503.1.
RefSeqXP_002080644.1. XM_002080608.1.
UniGeneDsi.3330.

3D structure databases

ProteinModelPortalQ70PU1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0210505; FBpp0208997; FBgn0068645.
GeneID6733590.
KEGGdsi:Dsim_GD10595.

Organism-specific databases

FlyBaseFBgn0068645. Dsim\PGRP-SC2.

Phylogenomic databases

KOK01446.
OrthoDBEOG757CZ5.
PhylomeDBQ70PU1.

Family and domain databases

Gene3D3.40.80.10. 1 hit.
InterProIPR002502. Amidase_domain.
IPR017331. Peptidoglycan_recognition.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
PANTHERPTHR11022. PTHR11022. 1 hit.
PfamPF01510. Amidase_2. 1 hit.
[Graphical view]
PIRSFPIRSF037945. PGRPs. 1 hit.
SMARTSM00644. Ami_2. 1 hit.
SM00701. PGRP. 1 hit.
[Graphical view]
SUPFAMSSF55846. SSF55846. 1 hit.
ProtoNetSearch...

Entry information

Entry namePGSC2_DROSI
AccessionPrimary (citable) accession number: Q70PU1
Secondary accession number(s): B2XZX6, B4QG79, Q2XY96
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase