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Q9V4X2 (PGSC2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidoglycan-recognition protein SC2

EC=3.5.1.28
Gene names
Name:PGRP-SC2
ORF Names:CG14745
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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.

Tissue specificity

Constitutively expressed at high level in gut, in addition to the induced expression in fat body. Ref.4

Induction

Strongly up-regulated by PGN from B.subtilis. Regulated by both imd/Relish and Toll pathways. Ref.4 Ref.5

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 184164Peptidoglycan-recognition protein SC2
PRO_0000023912

Sites

Metal binding511Zinc By similarity
Metal binding851Zinc By similarity
Metal binding1591Zinc By similarity
Metal binding1671Zinc By similarity

Amino acid modifications

Disulfide bond57 ↔ 63 By similarity

Natural variations

Natural variant71I → V in strain: DI7, Draveil, KY024, KY038, Loua, Monty5, Tahiti and ZW141.
Natural variant241I → V in strain: DI7, Draveil, KY024, KY038, Loua, Monty5 and ZW141.
Natural variant721A → T in strain: KY024, KY038 and ZW141.
Natural variant1711N → H in strain: ZW141.

Sequences

Sequence LengthMass (Da)Tools
Q9V4X2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 0F99D04914B07238

FASTA18419,829
        10         20         30         40         50         60 
MANKALILLA VLFCAQAVLG VTIISKSEWG GRSATSKTSL ANYLSYAVIH HTAGNYCSTK 

        70         80         90        100        110        120 
AACITQLQNI QAYHMDSLGW ADIGYNFLIG GDGNVYEGRG WNVMGAHATN WNSKSIGISF 

       130        140        150        160        170        180 
LGNYNTNTLT SAQITAAKGL LSDAVSRGQI VSGYILYGHR QVGSTECPGT NIWNEIRTWS 


NWKA 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DI7, Draveil, KY024, KY038, Loua, Monty5, P.bourg, S30, Tahiti, Texas and ZW141.
[2]"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].
Strain: Berkeley.
[3]"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.
[4]"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: TISSUE SPECIFICITY, INDUCTION.
[5]"The Toll and Imd pathways are the major regulators of the immune response in Drosophila."
De Gregorio E., Spellman P.T., Tzou P., Rubin G.M., Lemaitre B.
EMBO J. 21:2568-2579(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ556612 Genomic DNA. Translation: CAD89177.1.
AJ556613 Genomic DNA. Translation: CAD89178.1.
AJ556614 Genomic DNA. Translation: CAD89179.1.
AJ556615 Genomic DNA. Translation: CAD89180.1.
AJ556616 Genomic DNA. Translation: CAD89181.1.
AJ556617 Genomic DNA. Translation: CAD89182.1.
AJ556618 Genomic DNA. Translation: CAD89183.1.
AJ556619 Genomic DNA. Translation: CAD89184.1.
AJ556620 Genomic DNA. Translation: CAD89185.1.
AJ556621 Genomic DNA. Translation: CAD89186.1.
AJ556622 Genomic DNA. Translation: CAD89187.1.
AE013599 Genomic DNA. Translation: AAF59051.1.
RefSeqNP_610410.1. NM_136566.1.
UniGeneDm.23629.

3D structure databases

ProteinModelPortalQ9V4X2.
SMRQ9V4X2. Positions 23-184.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9V4X2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088709; FBpp0087788; FBgn0043575.
GeneID35862.
KEGGdme:Dmel_CG14745.

Organism-specific databases

CTD35862.
FlyBaseFBgn0043575. PGRP-SC2.

Phylogenomic databases

eggNOGCOG5479.
GeneTreeENSGT00390000016833.
InParanoidQ9V4X2.
KOK01446.
OMANSESACK.
OrthoDBEOG757CZ5.
PhylomeDBQ9V4X2.

Gene expression databases

BgeeQ9V4X2.

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

GenomeRNAi35862.
NextBio795563.

Entry information

Entry namePGSC2_DROME
AccessionPrimary (citable) accession number: Q9V4X2
Secondary accession number(s): Q70PT2 expand/collapse secondary AC list , Q70PT3, Q70PT5, Q70PT6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 90 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