PGPSD_DROME
ID PGPSD_DROME Reviewed; 186 AA.
AC Q9VS97; Q70PS3; Q70PS6; Q70PS9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Peptidoglycan-recognition protein SD;
DE Flags: Precursor;
GN Name=PGRP-SD; ORFNames=CG7496;
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, DEVELOPMENTAL STAGE, 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).
RN [6]
RP FUNCTION.
RX PubMed=15448690; DOI=10.1038/ni1123;
RA Bischoff V., Vignal C., Boneca I.G., Michel T., Hoffmann J.A., Royet J.;
RT "Function of the Drosophila pattern-recognition receptor PGRP-SD in the
RT detection of Gram-positive bacteria.";
RL Nat. Immunol. 5:1175-1180(2004).
CC -!- FUNCTION: Peptidoglycan-recognition protein that plays a key role in
CC innate immunity by binding to peptidoglycans (PGN) of Gram-positive
CC bacteria and activating the Toll pathway. Has no activity against on
CC Gram-negative bacteria and fungi. Shows some partial redundancy with
CC PRPGP-SA in Gram-positive bacteria recognition. May act by activating
CC the proteolytic cleavage of Spatzle and the subsequent activation of
CC Toll pathway. Recognizes S.aureus PGN. {ECO:0000269|PubMed:15448690}.
CC -!- INTERACTION:
CC Q9VS97; Q9NHB0: GNBP1; NbExp=4; IntAct=EBI-15721196, EBI-15721168;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In larvae, it is mainly expressed in fat body. Also
CC expressed in uninduced hemocytes and mbn-2 cells.
CC {ECO:0000269|PubMed:11106397}.
CC -!- DEVELOPMENTAL STAGE: Expressed from old embryos. Expressed in larvae
CC and adults. {ECO:0000269|PubMed:11106397}.
CC -!- INDUCTION: Strongly up-regulated by PGN from B.subtilis. Weakly or not
CC expressed in normal conditions. Regulated by the imd/Relish pathway.
CC {ECO:0000269|PubMed:11106397, 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; AJ556623; CAD89188.1; -; Genomic_DNA.
DR EMBL; AJ556624; CAD89189.1; -; Genomic_DNA.
DR EMBL; AJ556625; CAD89190.1; -; Genomic_DNA.
DR EMBL; AJ556626; CAD89191.1; -; Genomic_DNA.
DR EMBL; AJ556627; CAD89192.1; -; Genomic_DNA.
DR EMBL; AJ556628; CAD89193.1; -; Genomic_DNA.
DR EMBL; AJ556629; CAD89194.1; -; Genomic_DNA.
DR EMBL; AJ556630; CAD89195.1; -; Genomic_DNA.
DR EMBL; AJ556631; CAD89196.1; -; Genomic_DNA.
DR EMBL; AJ556632; CAD89197.1; -; Genomic_DNA.
DR EMBL; AJ556633; CAD89198.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50530.1; -; Genomic_DNA.
DR RefSeq; NP_648145.1; NM_139888.3.
DR PDB; 2RKQ; X-ray; 1.50 A; A=19-186.
DR PDBsum; 2RKQ; -.
DR AlphaFoldDB; Q9VS97; -.
DR SMR; Q9VS97; -.
DR BioGRID; 64291; 7.
DR DIP; DIP-60774N; -.
DR IntAct; Q9VS97; 1.
DR STRING; 7227.FBpp0076519; -.
DR GlyGen; Q9VS97; 1 site.
DR PaxDb; Q9VS97; -.
DR EnsemblMetazoa; FBtr0076807; FBpp0076519; FBgn0035806.
DR GeneID; 38858; -.
DR KEGG; dme:Dmel_CG7496; -.
DR CTD; 38858; -.
DR FlyBase; FBgn0035806; PGRP-SD.
DR VEuPathDB; VectorBase:FBgn0035806; -.
DR eggNOG; ENOG502S2KY; Eukaryota.
DR GeneTree; ENSGT00940000166535; -.
DR HOGENOM; CLU_037559_3_2_1; -.
DR InParanoid; Q9VS97; -.
DR OMA; DISYHYL; -.
DR OrthoDB; 1110472at2759; -.
DR PhylomeDB; Q9VS97; -.
DR BioGRID-ORCS; 38858; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; Q9VS97; -.
DR GenomeRNAi; 38858; -.
DR PRO; PR:Q9VS97; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035806; Expressed in head capsule and 17 other tissues.
DR ExpressionAtlas; Q9VS97; baseline and differential.
DR Genevisible; Q9VS97; DM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:FlyBase.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0032499; P:detection of peptidoglycan; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
DR GO; GO:0061059; P:positive regulation of peptidoglycan recognition protein 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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Immunity; Innate immunity;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..186
FT /note="Peptidoglycan-recognition protein SD"
FT /id="PRO_0000023914"
FT DOMAIN 47..169
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..63
FT /evidence="ECO:0000250"
FT VARIANT 41
FT /note="E -> V (in strain: DI7, Draveil, Loua, Monty5,
FT Tahiti, Texas, S30 and ZW141)"
FT VARIANT 62
FT /note="T -> A (in strain: DI7, Draveil, Loua, Monty5,
FT Tahiti, Texas, S30 and ZW141)"
FT VARIANT 68
FT /note="Q -> R (in strain: DI7, Draveil, Loua, Monty5,
FT Tahiti, Texas, S30 and ZW141)"
FT VARIANT 183
FT /note="S -> F (in strain: Loua, Monty5, P. bourg, Tahiti,
FT Texas and S30)"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:2RKQ"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:2RKQ"
FT HELIX 60..76
FT /evidence="ECO:0007829|PDB:2RKQ"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:2RKQ"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2RKQ"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2RKQ"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2RKQ"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:2RKQ"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2RKQ"
FT HELIX 131..146
FT /evidence="ECO:0007829|PDB:2RKQ"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:2RKQ"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:2RKQ"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:2RKQ"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:2RKQ"
SQ SEQUENCE 186 AA; 20123 MW; 09B0C5A7CF4BBF85 CRC64;
MTWIGLLIVG LTAIAVQGEV PIVTRAEWNA KPPNGAIDSM ETPLPRAVIA HTAGGACADD
VTCSQHMQNL QNFQMSKQKF SDIGYHYLIG GNGKVYEGRS PSQRGAFAGP NNDGSLGIAF
IGNFEERAPN KEALDAAKEL LEQAVKQAQL VEGYKLLGHR QVSATKSPGE ALYALIQQWP
NWSEEM
