SC1A_DROME
ID SC1A_DROME Reviewed; 185 AA.
AC C0HK98; B5RJ78; Q2XY86; Q70PU9; Q70PV0; Q95SQ9; Q9V3B7;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Peptidoglycan-recognition protein SC1a {ECO:0000303|PubMed:14738318};
DE EC=3.5.1.28 {ECO:0000250|UniProtKB:C0HK99};
DE Flags: Precursor;
GN Name=PGRP-SC1a {ECO:0000303|PubMed:14738318,
GN ECO:0000312|FlyBase:FBgn0043576};
GN ORFNames=CG14746 {ECO:0000312|FlyBase:FBgn0043576};
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] {ECO:0000312|EMBL:ABA86382.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-179.
RC STRAIN=Ral1 {ECO:0000312|EMBL:ABA86382.1};
RX PubMed=16120803; DOI=10.1093/molbev/msi246;
RA Comeron J.M., Guthrie T.B.;
RT "Intragenic Hill-Robertson interference influences selection intensity on
RT synonymous mutations in Drosophila.";
RL Mol. Biol. Evol. 22:2519-2530(2005).
CC -!- FUNCTION: N-acetylmuramyl-L-alanine amidase involved in innate immunity
CC by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by
CC digesting biologically active PGN into biologically inactive fragments.
CC Has no direct bacteriolytic activity. {ECO:0000250|UniProtKB:C0HK99}.
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 Evidence={ECO:0000250|UniProtKB:C0HK99};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q8INK6};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
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DR EMBL; AE013599; AAF59054.1; -; Genomic_DNA.
DR EMBL; AJ556588; CAD89153.1; -; Genomic_DNA.
DR EMBL; AJ556589; CAD89154.1; -; Genomic_DNA.
DR EMBL; AJ556590; CAD89155.1; -; Genomic_DNA.
DR EMBL; AJ556591; CAD89156.1; -; Genomic_DNA.
DR EMBL; AJ556592; CAD89157.1; -; Genomic_DNA.
DR EMBL; AJ556593; CAD89158.1; -; Genomic_DNA.
DR EMBL; AJ556594; CAD89159.1; -; Genomic_DNA.
DR EMBL; AJ556595; CAD89160.1; -; Genomic_DNA.
DR EMBL; AJ556596; CAD89161.1; -; Genomic_DNA.
DR EMBL; AJ556597; CAD89162.1; -; Genomic_DNA.
DR EMBL; AJ556598; CAD89163.1; -; Genomic_DNA.
DR EMBL; AJ556601; CAD89166.1; -; Genomic_DNA.
DR EMBL; AJ556603; CAD89168.1; -; Genomic_DNA.
DR EMBL; AJ556609; CAD89174.1; -; Genomic_DNA.
DR EMBL; DQ138758; ABA86364.1; -; Genomic_DNA.
DR EMBL; DQ138776; ABA86382.1; -; Genomic_DNA.
DR RefSeq; NP_001286209.1; NM_001299280.1.
DR RefSeq; NP_610407.1; NM_136563.2.
DR RefSeq; NP_610409.1; NM_136565.2.
DR AlphaFoldDB; C0HK98; -.
DR SMR; C0HK98; -.
DR STRING; 7227.FBpp0087786; -.
DR DNASU; 35861; -.
DR EnsemblMetazoa; FBtr0088707; FBpp0087786; FBgn0043576.
DR EnsemblMetazoa; FBtr0088708; FBpp0087787; FBgn0033327.
DR EnsemblMetazoa; FBtr0339336; FBpp0308436; FBgn0033327.
DR GeneID; 35859; -.
DR GeneID; 35861; -.
DR KEGG; dme:Dmel_CG14746; -.
DR KEGG; dme:Dmel_CG8577; -.
DR UCSC; CG14746-RA; d. melanogaster.
DR CTD; 35859; -.
DR CTD; 35861; -.
DR FlyBase; FBgn0043576; PGRP-SC1a.
DR VEuPathDB; VectorBase:FBgn0033327; -.
DR VEuPathDB; VectorBase:FBgn0043576; -.
DR eggNOG; ENOG502QR3D; Eukaryota.
DR OMA; FMKQFAI; -.
DR OrthoDB; 1110472at2759; -.
DR BioGRID-ORCS; 35859; 0 hits in 3 CRISPR screens.
DR BioGRID-ORCS; 35861; 0 hits in 3 CRISPR screens.
DR PRO; PR:C0HK98; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033327; Expressed in midgut and 7 other tissues.
DR ExpressionAtlas; C0HK98; baseline and differential.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
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:0050830; P:defense response to Gram-positive bacterium; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
DR GO; GO:0002814; P:negative regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IGI:FlyBase.
DR GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IGI:FlyBase.
DR GO; GO:0009253; P:peptidoglycan catabolic process; ISS:FlyBase.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP: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 3: Inferred from homology;
KW Disulfide bond; Hydrolase; Immunity; Innate immunity; Metal-binding;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..185
FT /note="Peptidoglycan-recognition protein SC1a"
FT /id="PRO_0000023910"
FT DOMAIN 46..170
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT SITE 86
FT /note="Essential for zinc hydrate coordination"
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT DISULFID 58..64
FT /evidence="ECO:0000250|UniProtKB:Q8INK6"
FT VARIANT 6
FT /note="A -> T (in strain: KY024 and KY038)"
FT VARIANT 13
FT /note="V -> I (in strain: KY024)"
SQ SEQUENCE 185 AA; 20395 MW; F23F8D80A33541AC CRC64;
MVSKVALLLA VLVCSQYMAQ GVYVVSKAEW GGRGAKWTVG LGNYLSYAII HHTAGSYCET
RAQCNAVLQS VQNYHMDSLG WPDIGYNFLI GGDGNVYEGR GWNNMGAHAA EWNPYSIGIS
FLGNYNWDTL EPNMISAAQQ LLNDAVNRGQ LSSGYILYGH RQVSATECPG THIWNEIRGW
SHWSG
