PGSC2_DROME
ID PGSC2_DROME Reviewed; 184 AA.
AC Q9V4X2; Q70PT2; Q70PT3; Q70PT5; Q70PT6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Peptidoglycan-recognition protein SC2;
DE EC=3.5.1.28;
DE Flags: Precursor;
GN Name=PGRP-SC2; ORFNames=CG14745;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DI7, Draveil, KY024, KY038, Loua, Monty5, P.bourg, S30, Tahiti,
RC Texas, and ZW141;
RX PubMed=14738318; DOI=10.1007/s00239-003-2506-6;
RA Jiggins F.M., Hurst G.D.D.;
RT "The evolution of parasite recognition genes in the innate immune system:
RT purifying selection on Drosophila melanogaster peptidoglycan recognition
RT proteins.";
RL J. Mol. Evol. 57:598-605(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11106397; DOI=10.1073/pnas.97.25.13772;
RA Werner T., Liu G., Kang D., Ekengren S., Steiner H., Hultmark D.;
RT "A family of peptidoglycan recognition proteins in the fruit fly Drosophila
RT melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13772-13777(2000).
RN [5]
RP INDUCTION.
RX PubMed=12032070; DOI=10.1093/emboj/21.11.2568;
RA De Gregorio E., Spellman P.T., Tzou P., Rubin G.M., Lemaitre B.;
RT "The Toll and Imd pathways are the major regulators of the immune response
RT in Drosophila.";
RL EMBO J. 21:2568-2579(2002).
CC -!- FUNCTION: N-acetylmuramyl-L-alanine amidase involved in innate immunity
CC by degrading bacterial peptidoglycans (PGN). Probably plays a scavenger
CC role by digesting biologically active PGN into biologically inactive
CC fragments. Has no direct bacteriolytic activity (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q8INK6};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed at high level in gut, in
CC addition to the induced expression in fat body.
CC {ECO:0000269|PubMed:11106397}.
CC -!- INDUCTION: Strongly up-regulated by PGN from B.subtilis. Regulated by
CC both imd/Relish and Toll pathways. {ECO:0000269|PubMed:11106397,
CC ECO:0000269|PubMed:12032070}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
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DR EMBL; AJ556612; CAD89177.1; -; Genomic_DNA.
DR EMBL; AJ556613; CAD89178.1; -; Genomic_DNA.
DR EMBL; AJ556614; CAD89179.1; -; Genomic_DNA.
DR EMBL; AJ556615; CAD89180.1; -; Genomic_DNA.
DR EMBL; AJ556616; CAD89181.1; -; Genomic_DNA.
DR EMBL; AJ556617; CAD89182.1; -; Genomic_DNA.
DR EMBL; AJ556618; CAD89183.1; -; Genomic_DNA.
DR EMBL; AJ556619; CAD89184.1; -; Genomic_DNA.
DR EMBL; AJ556620; CAD89185.1; -; Genomic_DNA.
DR EMBL; AJ556621; CAD89186.1; -; Genomic_DNA.
DR EMBL; AJ556622; CAD89187.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF59051.1; -; Genomic_DNA.
DR RefSeq; NP_610410.1; NM_136566.2.
DR AlphaFoldDB; Q9V4X2; -.
DR SMR; Q9V4X2; -.
DR STRING; 7227.FBpp0087788; -.
DR PaxDb; Q9V4X2; -.
DR EnsemblMetazoa; FBtr0088709; FBpp0087788; FBgn0043575.
DR GeneID; 35862; -.
DR KEGG; dme:Dmel_CG14745; -.
DR CTD; 35862; -.
DR FlyBase; FBgn0043575; PGRP-SC2.
DR VEuPathDB; VectorBase:FBgn0043575; -.
DR eggNOG; ENOG502S2KY; Eukaryota.
DR GeneTree; ENSGT00940000166535; -.
DR HOGENOM; CLU_037559_3_2_1; -.
DR InParanoid; Q9V4X2; -.
DR OMA; FKGDHSS; -.
DR OrthoDB; 1110472at2759; -.
DR PhylomeDB; Q9V4X2; -.
DR BioGRID-ORCS; 35862; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35862; -.
DR PRO; PR:Q9V4X2; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0043575; Expressed in adult midgut (Drosophila) and 23 other tissues.
DR ExpressionAtlas; Q9V4X2; baseline and differential.
DR Genevisible; Q9V4X2; DM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; ISS:FlyBase.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002814; P:negative regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IMP:FlyBase.
DR GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR GO; GO:0009253; P:peptidoglycan catabolic process; ISS:FlyBase.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IMP:FlyBase.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; -; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR017331; Peptidoglycan_recognition.
DR InterPro; IPR015510; PGRP.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR PANTHER; PTHR11022; PTHR11022; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR PIRSF; PIRSF037945; PGRPs; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; SSF55846; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Hydrolase; Immunity; Innate immunity; Metal-binding;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..184
FT /note="Peptidoglycan-recognition protein SC2"
FT /id="PRO_0000023912"
FT DOMAIN 45..169
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT SITE 85
FT /note="Important for catalytic activity; essential for
FT amidase activity and zinc hydrate coordination"
FT /evidence="ECO:0000250|UniProtKB:P00806"
FT DISULFID 57..63
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT VARIANT 7
FT /note="I -> V (in strain: DI7, Draveil, KY024, KY038, Loua,
FT Monty5, Tahiti and ZW141)"
FT VARIANT 24
FT /note="I -> V (in strain: DI7, Draveil, KY024, KY038, Loua,
FT Monty5 and ZW141)"
FT VARIANT 72
FT /note="A -> T (in strain: KY024, KY038 and ZW141)"
FT VARIANT 171
FT /note="N -> H (in strain: ZW141)"
SQ SEQUENCE 184 AA; 19829 MW; 0F99D04914B07238 CRC64;
MANKALILLA VLFCAQAVLG VTIISKSEWG GRSATSKTSL ANYLSYAVIH HTAGNYCSTK
AACITQLQNI QAYHMDSLGW ADIGYNFLIG GDGNVYEGRG WNVMGAHATN WNSKSIGISF
LGNYNTNTLT SAQITAAKGL LSDAVSRGQI VSGYILYGHR QVGSTECPGT NIWNEIRTWS
NWKA
