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Q9V3B7 (PGSC1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

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.

Sequence caution

The sequence AAL28193.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CG9184Q9W0H11EBI-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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[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] [Europe PMC] [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 (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (PGRP-SC1B).
Strain: Berkeley.
Tissue: Head.
[7]"A scavenger function for a Drosophila peptidoglycan recognition protein."
Mellroth P., Karlsson J., Steiner H.
J. Biol. Chem. 278:7059-7064(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY (PGRP-SC1B), PGN-BINDING, MUTAGENESIS OF CYS-168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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: ACH92417.2.
RefSeqNP_610407.1. NM_136563.1.
NP_610409.1. NM_136565.1.
UniGeneDm.3372.
Dm.38443.

3D structure databases

ProteinModelPortalQ9V3B7.
SMRQ9V3B7. Positions 24-183.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid61708. 1 interaction.
61710. 1 interaction.
IntActQ9V3B7. 1 interaction.
MINTMINT-1610118.
STRING7227.FBpp0087786.

Proteomic databases

PaxDbQ9V3B7.
PRIDEQ9V3B7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088707; FBpp0087786; FBgn0043576.
FBtr0088708; FBpp0087787; FBgn0033327.
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

eggNOGCOG5479.
GeneTreeENSGT00390000016833.
InParanoidQ9V3B7.
KOK01446.
OMATLEPNMI.
OrthoDBEOG757CZ5.
PhylomeDBQ9V3B7.

Gene expression databases

BgeeQ9V3B7.

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...

Other

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: April 16, 2014
This is version 100 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