Reviewed,
UniProtKB/Swiss-Prot Q9V3B7 (PGSC1_DROME)
Last modified
November 3, 2009.
Version 65.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Peptidoglycan-recognition protein SC1a/b EC=3.5.1.28 | |||||||||
| Gene names |
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| Organism | Drosophila melanogaster (Fruit fly) [Complete proteome] | |||||||||
| Taxonomic identifier | 7227 [NCBI] | |||||||||
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora |
Protein attributes
| Sequence length | 185 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity. |
| Catalytic activity | Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. Ref.7 |
| Cofactor | Zinc By similarity. |
| Subcellular location | Secreted Potential. |
| Tissue specificity | Constitutively expressed at high level in gut, in addition to the induced expression in fat body. Ref.1 |
| Induction | Up-regulated by PGN from B.subtilis. Ref.1 |
| Sequence similarities | Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Immune response Innate immunity |
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | innate immune response Ref.1 Non-traceable author statement. Source: UniProtKB peptidoglycan catabolic process Ref.1Non-traceable author statement. Source: UniProtKB |
| Cellular component | extracellular region Ref.1 Non-traceable author statement. Source: UniProtKB |
| Molecular function | N-acetylmuramoyl-L-alanine amidase activity Ref.7 Inferred from direct assay. Source: FlyBase peptidoglycan binding Ref.1Non-traceable author statement. Source: UniProtKB protein bindingInferred from physical interaction. Source: IntAct zinc ion bindingInferred 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 – 21 | 21 | Potential | ||||||||
| Chain | 22 – 185 | 164 | Peptidoglycan-recognition protein SC1a/b | PRO_0000023910 | |||||||
Sites | |||||||||||
| Metal binding | 52 | 1 | Zinc By similarity | ||||||||
| Metal binding | 86 | 1 | Zinc By similarity | ||||||||
| Metal binding | 160 | 1 | Zinc By similarity | ||||||||
| Metal binding | 168 | 1 | Zinc By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 58 ↔ 64 | By similarity | |||||||||
Natural variations | |||||||||||
| Natural variant | 6 | 1 | A → T in PGRP-SC1a; strain: KY038 and in PGRP-SC1b; strain: KY024 and KY038. | ||||||||
| Natural variant | 13 | 1 | V → I in PGRP-SC1b; strain: KY024. | ||||||||
Experimental info | |||||||||||
| Mutagenesis | 168 | 1 | C → A: Abolishes enzyme activity but retains PGN-binding. Ref.7 | ||||||||
| Sequence conflict | 178 | 1 | R → P in AAL28193. Ref.5 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster." Werner T., Liu G., Kang D., Ekengren S., Steiner H., Hultmark D. Proc. Natl. Acad. Sci. U.S.A. 97:13772-13777(2000) [PubMed: 11106397] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (PGRP-SC1B), PGN-BINDING, TISSUE SPECIFICITY, INDUCTION. |
| [2] | "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] (PGRP-SC1A AND PGRP-SC1B). Strain: DI7, Draveil, KY024, KY038, Loua, Monty5, P.bourg, S30, Tahiti, Texas and ZW141. |
| [3] | "The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. Venter J.C.Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (PGRP-SC1A AND PGRP-SC1B). Strain: Berkeley. |
| [4] | "Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. Lewis S.E.Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. |
| [5] | "A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (PGRP-SC1B). Strain: Berkeley. Tissue: Head. |
| [6] | Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (PGRP-SC1B). Strain: Berkeley. |
| [7] | "A scavenger function for a Drosophila peptidoglycan recognition protein." Mellroth P., Karlsson J., Steiner H. J. Biol. Chem. 278:7059-7064(2003) [PubMed: 12496260] [Abstract] Cited for: ENZYME ACTIVITY (PGRP-SC1B), PGN-BINDING, MUTAGENESIS OF CYS-168. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AF207542 mRNA. Translation: AAG23736.1. AJ556588 Genomic DNA. Translation: CAD89153.1. AJ556589 Genomic DNA. Translation: CAD89154.1. AJ556590 Genomic DNA. Translation: CAD89155.1. AJ556591 Genomic DNA. Translation: CAD89156.1. AJ556592 Genomic DNA. Translation: CAD89157.1. AJ556593 Genomic DNA. Translation: CAD89158.1. AJ556594 Genomic DNA. Translation: CAD89159.1. AJ556595 Genomic DNA. Translation: CAD89160.1. AJ556596 Genomic DNA. Translation: CAD89161.1. AJ556597 Genomic DNA. Translation: CAD89162.1. AJ556598 Genomic DNA. Translation: CAD89163.1. AJ556599 Genomic DNA. Translation: CAD89164.1. AJ556600 Genomic DNA. Translation: CAD89165.1. AJ556601 Genomic DNA. Translation: CAD89166.1. AJ556602 Genomic DNA. Translation: CAD89167.1. AJ556603 Genomic DNA. Translation: CAD89168.1. AJ556604 Genomic DNA. Translation: CAD89169.1. AJ556605 Genomic DNA. Translation: CAD89170.1. AJ556606 Genomic DNA. Translation: CAD89171.1. AJ556607 Genomic DNA. Translation: CAD89172.1. AJ556608 Genomic DNA. Translation: CAD89173.1. AJ556609 Genomic DNA. Translation: CAD89174.1. AE013599 Genomic DNA. Translation: AAF59052.1. AE013599 Genomic DNA. Translation: AAF59054.1. AY060645 mRNA. Translation: AAL28193.2. Different initiation. BT044352 mRNA. Translation: ACH92417.1. Different initiation. | |
| RefSeq | NP_610407.1. NP_610409.1. |
| UniGene | Dm.3372 Dm.36623 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1OHT based on UniProtKB Q9VGN3. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9V3B7. 1 interaction. |
Proteomic databases | |
| PRIDE | Q9V3B7. |
Genome annotation databases | |
| Ensembl | FBtr0088707; FBpp0087786; FBgn0043576; Drosophila melanogaster. [Genome view] FBtr0088708; FBpp0087787; FBgn0033327; Drosophila melanogaster. [Genome view] |
| GeneID | 35859. 35861. |
| KEGG | dme:Dmel_CG14746. dme:Dmel_CG8577. |
| UCSC | CG14746-RA. d. melanogaster. |
Organism-specific databases | |
| CTD | 35859. 35861. |
| FlyBase | FBgn0043576. PGRP-SC1a. FBgn0033327. PGRP-SC1b. |
Phylogenomic databases | |
| HOGENOM | Q9V3B7. |
| OMA | THIWNEI. |
Enzyme and pathway databases | |
| BRENDA | 3.5.1.28. 48. |
Gene expression databases | |
| GermOnline | CG14746. Drosophila melanogaster. CG8577. Drosophila melanogaster. |
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... |
Other Resources | |
| NextBio | 795548. |
Entry information
| Entry name | PGSC1_DROME | ||||||||
| Accession | Primary (citable) accession number: Q9V3B7 Secondary accession number(s): B5RJ78 Q95SQ9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Drosophila annotation project | ||||||||
Relevant documents
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with


