Reviewed, UniProtKB/Swiss-Prot Q70PU1 (PGSC2_DROSI)

Names and origin

Protein names

Recommended name:
    Peptidoglycan-recognition protein SC2
    EC=3.5.1.28

Gene names

Name:	PGRP-SC2
ORF Names:	GD10595

Organism

Drosophila simulans (Fruit fly)

Taxonomic identifier

7240 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	184 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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 process	Immune response Innate immunity
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	innate immune response Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N-acetylmuramoyl-L-alanine amidase activity Inferred from electronic annotation. Source: EC protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 184	164	Peptidoglycan-recognition protein SC2		PRO_0000023913
Sites
	Metal binding	51	1	Zinc By similarity
	Metal binding	85	1	Zinc By similarity
	Metal binding	159	1	Zinc By similarity
	Metal binding	167	1	Zinc By similarity
Amino acid modifications
	Disulfide bond	57 ↔ 63		By similarity
Natural variations
	Natural variant	12	1	L → V in strain: 08FG. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q70PU1-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: BF4070F2313D53C5	FASTA	184	19,788
	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

References

	« Hide 'large scale' referencesShow '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: 14738318] [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: 17994087] [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: 16120803] [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: 18288436] [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
EMBLGenBankDDBJ	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.
RefSeq	XP_002080644.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	6733590.
KEGG	dsi:Dsim_GD10595.
Organism-specific databases
FlyBase	FBgn0068645. Dsim\PGRP-SC2.
Enzyme and pathway databases
BRENDA	3.5.1.28. 189309.
Family and domain databases
InterPro	IPR002502. Amidase_2. IPR017331. Peptidoglycan_recognition. IPR015510. PGRP. IPR006619. PGRP_met/bac. [Graphical view]
Gene3D	G3DSA:3.40.80.10. Amidase_2. 1 hit.
PANTHER	PTHR11022. PGRPs. 1 hit.
Pfam	PF01510. Amidase_2. 1 hit. [Graphical view]
PIRSF	PIRSF037945. PGRPs. 1 hit.
SMART	SM00644. Ami_2. 1 hit. SM00701. PGRP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGSC2_DROSI

Accession

Primary (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:	June 16, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project