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Reviewed, UniProtKB/Swiss-Prot Q9V3B7 (PGSC1_DROME)

Last modified November 3, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidoglycan-recognition protein SC1a/b
    EC=3.5.1.28
Gene names
Name: PGRP-SC1a
ORF Names: CG14746
AND
Name: PGRP-SC1b
ORF Names: CG8577
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processImmune response
Innate immunity
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processinnate immune response Ref.1

Non-traceable author statement. Source: UniProtKB

peptidoglycan catabolic process Ref.1

Non-traceable author statement. Source: UniProtKB

   Cellular componentextracellular region Ref.1

Non-traceable author statement. Source: UniProtKB

   Molecular functionN-acetylmuramoyl-L-alanine amidase activity Ref.7

Inferred from direct assay. Source: FlyBase

peptidoglycan binding Ref.1

Non-traceable author statement. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9W0H11EBI-109541,EBI-143367

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 185164Peptidoglycan-recognition protein SC1a/b
PRO_0000023910

Sites

Metal binding521Zinc By similarity
Metal binding861Zinc By similarity
Metal binding1601Zinc By similarity
Metal binding1681Zinc By similarity

Amino acid modifications

Disulfide bond58 ↔ 64 By similarity

Natural variations

Natural variant61A → T in PGRP-SC1a; strain: KY038 and in PGRP-SC1b; strain: KY024 and KY038.
Natural variant131V → I in PGRP-SC1b; strain: KY024.

Experimental info

Mutagenesis1681C → A: Abolishes enzyme activity but retains PGN-binding. Ref.7
Sequence conflict1781R → P in AAL28193. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9V3B7-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: F23F8D80A33541AC

FASTA18520,395
        10         20         30         40         50         60 
MVSKVALLLA VLVCSQYMAQ GVYVVSKAEW GGRGAKWTVG LGNYLSYAII HHTAGSYCET 

        70         80         90        100        110        120 
RAQCNAVLQS VQNYHMDSLG WPDIGYNFLI GGDGNVYEGR GWNNMGAHAA EWNPYSIGIS 

       130        140        150        160        170        180 
FLGNYNWDTL EPNMISAAQQ LLNDAVNRGQ LSSGYILYGH RQVSATECPG THIWNEIRGW 


SHWSG 

« Hide

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. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., 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.
RefSeqNP_610407.1.
NP_610409.1.
UniGeneDm.3372
Dm.36623

3D structure databases

HSSPHSSP built from PDB template 1OHT based on UniProtKB Q9VGN3.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9V3B7. 1 interaction.

Proteomic databases

PRIDEQ9V3B7.

Genome annotation databases

EnsemblFBtr0088707; FBpp0087786; FBgn0043576; Drosophila melanogaster. [Genome view]
FBtr0088708; FBpp0087787; FBgn0033327; Drosophila melanogaster. [Genome view]
GeneID35859.
35861.
KEGGdme:Dmel_CG14746.
dme:Dmel_CG8577.
UCSCCG14746-RA. d. melanogaster.

Organism-specific databases

CTD35859.
35861.
FlyBaseFBgn0043576. PGRP-SC1a.
FBgn0033327. PGRP-SC1b.

Phylogenomic databases

HOGENOMQ9V3B7.
OMATHIWNEI.

Enzyme and pathway databases

BRENDA3.5.1.28. 48.

Gene expression databases

GermOnlineCG14746. Drosophila melanogaster.
CG8577. Drosophila melanogaster.

Family and domain databases

InterProIPR002502. Amidase_2.
IPR017331. Peptidoglycan_recognition.
IPR015510. PGRP.
IPR006619. PGRP_met/bac.
[Graphical view]
Gene3DG3DSA:3.40.80.10. Amidase_2. 1 hit.
PANTHERPTHR11022. PGRPs. 1 hit.
PfamPF01510. Amidase_2. 1 hit.
[Graphical view]
PIRSFPIRSF037945. PGRPs. 1 hit.
SMARTSM00644. Ami_2. 1 hit.
SM00701. PGRP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio795548.

Entry information

Entry namePGSC1_DROME
AccessionPrimary (citable) accession number: Q9V3B7
Secondary accession number(s): B5RJ78 expand/collapse secondary AC list , Q70PU9, Q70PV0, Q95SQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 1, 2000
Last modified: November 3, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents