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Protein

Peptidoglycan-recognition protein SC1a/b

Gene

PGRP-SC1a

more
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.1 Publication

Cofactori

Zn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521ZincBy similarity
Metal bindingi86 – 861ZincBy similarity
Metal bindingi160 – 1601ZincBy similarity
Metal bindingi168 – 1681ZincBy similarity

GO - Molecular functioni

  • N-acetylmuramoyl-L-alanine amidase activity Source: FlyBase
  • peptidoglycan binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • immune response Source: FlyBase
  • innate immune response Source: UniProtKB
  • negative regulation of innate immune response Source: FlyBase
  • peptidoglycan catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Immunity, Innate immunity

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidoglycan-recognition protein SC1a/b (EC:3.5.1.28)
Gene namesi
Name:PGRP-SC1a
ORF Names:CG14746
AND
Name:PGRP-SC1b
ORF Names:CG8577
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0043576. PGRP-SC1a.
FBgn0033327. PGRP-SC1b.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi168 – 1681C → A: Abolishes enzyme activity but retains PGN-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 185164Peptidoglycan-recognition protein SC1a/bPRO_0000023910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 64By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9V3B7.
PRIDEiQ9V3B7.

Expressioni

Tissue specificityi

Constitutively expressed at high level in gut, in addition to the induced expression in fat body.1 Publication

Inductioni

Up-regulated by PGN from B.subtilis.1 Publication

Gene expression databases

BgeeiQ9V3B7.
ExpressionAtlasiQ9V3B7. differential.
GenevisibleiQ9V3B7. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CG9184Q9W0H11EBI-109541,EBI-143367

Protein-protein interaction databases

BioGridi61708. 1 interaction.
61710. 1 interaction.
IntActiQ9V3B7. 1 interaction.
MINTiMINT-1610118.
STRINGi7227.FBpp0087787.

Structurei

3D structure databases

ProteinModelPortaliQ9V3B7.
SMRiQ9V3B7. Positions 24-183.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5479.
GeneTreeiENSGT00390000016833.
InParanoidiQ9V3B7.
KOiK01446.
OMAiQARNVQH.
OrthoDBiEOG757CZ5.
PhylomeDBiQ9V3B7.

Family and domain databases

Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR017331. Peptidoglycan_recognition.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
PANTHERiPTHR11022. PTHR11022. 1 hit.
PfamiPF01510. Amidase_2. 1 hit.
[Graphical view]
PIRSFiPIRSF037945. PGRPs. 1 hit.
SMARTiSM00644. Ami_2. 1 hit.
SM00701. PGRP. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9V3B7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSKVALLLA VLVCSQYMAQ GVYVVSKAEW GGRGAKWTVG LGNYLSYAII
60 70 80 90 100
HHTAGSYCET RAQCNAVLQS VQNYHMDSLG WPDIGYNFLI GGDGNVYEGR
110 120 130 140 150
GWNNMGAHAA EWNPYSIGIS FLGNYNWDTL EPNMISAAQQ LLNDAVNRGQ
160 170 180
LSSGYILYGH RQVSATECPG THIWNEIRGW SHWSG
Length:185
Mass (Da):20,395
Last modified:May 1, 2000 - v1
Checksum:iF23F8D80A33541AC
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti178 – 1781R → P in AAL28193 (PubMed:12537569).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61A → T in PGRP-SC1a; strain: KY038 and in PGRP-SC1b; strain: KY024 and KY038.
Natural varianti13 – 131V → I in PGRP-SC1b; strain: KY024.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_001286209.1. NM_001299280.1.
NP_610407.1. NM_136563.2.
NP_610409.1. NM_136565.2.
UniGeneiDm.3372.

Genome annotation databases

EnsemblMetazoaiFBtr0088707; FBpp0087786; FBgn0043576.
FBtr0088708; FBpp0087787; FBgn0033327.
FBtr0339336; FBpp0308436; FBgn0033327.
GeneIDi35859.
35861.
KEGGidme:Dmel_CG14746.
dme:Dmel_CG8577.
UCSCiCG14746-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_001286209.1. NM_001299280.1.
NP_610407.1. NM_136563.2.
NP_610409.1. NM_136565.2.
UniGeneiDm.3372.

3D structure databases

ProteinModelPortaliQ9V3B7.
SMRiQ9V3B7. Positions 24-183.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61708. 1 interaction.
61710. 1 interaction.
IntActiQ9V3B7. 1 interaction.
MINTiMINT-1610118.
STRINGi7227.FBpp0087787.

Proteomic databases

PaxDbiQ9V3B7.
PRIDEiQ9V3B7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088707; FBpp0087786; FBgn0043576.
FBtr0088708; FBpp0087787; FBgn0033327.
FBtr0339336; FBpp0308436; FBgn0033327.
GeneIDi35859.
35861.
KEGGidme:Dmel_CG14746.
dme:Dmel_CG8577.
UCSCiCG14746-RA. d. melanogaster.

Organism-specific databases

CTDi35859.
35861.
FlyBaseiFBgn0043576. PGRP-SC1a.
FBgn0033327. PGRP-SC1b.

Phylogenomic databases

eggNOGiCOG5479.
GeneTreeiENSGT00390000016833.
InParanoidiQ9V3B7.
KOiK01446.
OMAiQARNVQH.
OrthoDBiEOG757CZ5.
PhylomeDBiQ9V3B7.

Miscellaneous databases

NextBioi795548.
PROiQ9V3B7.

Gene expression databases

BgeeiQ9V3B7.
ExpressionAtlasiQ9V3B7. differential.
GenevisibleiQ9V3B7. DM.

Family and domain databases

Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR017331. Peptidoglycan_recognition.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
PANTHERiPTHR11022. PTHR11022. 1 hit.
PfamiPF01510. Amidase_2. 1 hit.
[Graphical view]
PIRSFiPIRSF037945. PGRPs. 1 hit.
SMARTiSM00644. Ami_2. 1 hit.
SM00701. PGRP. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. 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.

Entry informationi

Entry nameiPGSC1_DROME
AccessioniPrimary (citable) accession number: Q9V3B7
Secondary accession number(s): B5RJ78
, Q70PU9, Q70PV0, Q95SQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.