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Reviewed, UniProtKB/Swiss-Prot Q9V4X2 (PGSC2_DROME)

Last modified November 3, 2009. Version 55. 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

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.

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

Inferred from electronic annotation. Source: UniProtKB-KW

peptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from electronic annotation. Source: EC

protein binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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
Q9V4X2-1 [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: 14738318] [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: 10731132] [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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[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: 11106397] [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: 12032070] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
UniGeneDm.23629

3D structure databases

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

Protein-protein interaction databases

STRINGQ9V4X2.

Proteomic databases

PRIDEQ9V4X2.

Genome annotation databases

EnsemblFBtr0088709; FBpp0087788; FBgn0043575; Drosophila melanogaster. [Genome view]
GeneID35862.
KEGGdme:Dmel_CG14745.
NMPDRfig|7227.3.peg.3923.

Organism-specific databases

CTD35862.
FlyBaseFBgn0043575. PGRP-SC2.

Phylogenomic databases

HOGENOMQ9V4X2.
OMAWNEIRTW.

Enzyme and pathway databases

BRENDA3.5.1.28. 48.

Gene expression databases

GermOnlineCG14745. 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

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: November 3, 2009
This is version 55 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents