PGPLA_DROME
ID PGPLA_DROME Reviewed; 368 AA.
AC Q95T64; Q9BLX5; Q9GNK6; Q9GNK7; Q9VSV7; Q9VSV8;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Peptidoglycan-recognition protein LA;
GN Name=PGRP-LA; ORFNames=CG32042;
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 [MRNA] (ISOFORMS 2; 3 AND 4), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-320, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
CC -!- FUNCTION: Peptidoglycan-recognition protein probably involved in innate
CC immunity by binding to peptidoglycans (PGN) of bacteria and activating
CC the immune response. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q95T64-1; Sequence=Displayed;
CC Name=2; Synonyms=LAb, B, F;
CC IsoId=Q95T64-2; Sequence=VSP_013590, VSP_013591;
CC Name=3; Synonyms=LAc, C;
CC IsoId=Q95T64-3; Sequence=VSP_013589;
CC Name=4; Synonyms=LAa, a1, D;
CC IsoId=Q95T64-4; Sequence=VSP_013592;
CC -!- TISSUE SPECIFICITY: 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 -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
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DR EMBL; AF207535; AAG23729.1; -; mRNA.
DR EMBL; AF207536; AAG23730.1; -; mRNA.
DR EMBL; AF313393; AAK00295.1; -; mRNA.
DR EMBL; AE014296; AAF50303.2; -; Genomic_DNA.
DR EMBL; AE014296; AAF50304.2; -; Genomic_DNA.
DR EMBL; AE014296; AAS65050.1; -; Genomic_DNA.
DR EMBL; AE014296; AAS65051.1; -; Genomic_DNA.
DR EMBL; AY060314; AAL25353.1; -; mRNA.
DR EMBL; BT001411; AAN71166.1; -; mRNA.
DR RefSeq; NP_001261623.1; NM_001274694.1. [Q95T64-3]
DR RefSeq; NP_996026.1; NM_206304.2. [Q95T64-1]
DR RefSeq; NP_996027.1; NM_206305.2. [Q95T64-4]
DR RefSeq; NP_996028.1; NM_206306.2. [Q95T64-3]
DR RefSeq; NP_996029.1; NM_206307.2. [Q95T64-2]
DR AlphaFoldDB; Q95T64; -.
DR SMR; Q95T64; -.
DR BioGRID; 64459; 6.
DR IntAct; Q95T64; 6.
DR STRING; 7227.FBpp0076164; -.
DR GlyGen; Q95T64; 2 sites.
DR iPTMnet; Q95T64; -.
DR PaxDb; Q95T64; -.
DR DNASU; 39062; -.
DR EnsemblMetazoa; FBtr0076432; FBpp0076161; FBgn0035975. [Q95T64-2]
DR EnsemblMetazoa; FBtr0076433; FBpp0076162; FBgn0035975. [Q95T64-3]
DR EnsemblMetazoa; FBtr0076434; FBpp0076163; FBgn0035975. [Q95T64-4]
DR EnsemblMetazoa; FBtr0076435; FBpp0076164; FBgn0035975. [Q95T64-1]
DR EnsemblMetazoa; FBtr0333882; FBpp0306014; FBgn0035975. [Q95T64-3]
DR GeneID; 39062; -.
DR KEGG; dme:Dmel_CG32042; -.
DR CTD; 39062; -.
DR FlyBase; FBgn0035975; PGRP-LA.
DR VEuPathDB; VectorBase:FBgn0035975; -.
DR eggNOG; ENOG502S2KY; Eukaryota.
DR InParanoid; Q95T64; -.
DR PhylomeDB; Q95T64; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-6803157; Antimicrobial peptides.
DR SignaLink; Q95T64; -.
DR BioGRID-ORCS; 39062; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39062; -.
DR PRO; PR:Q95T64; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035975; Expressed in mouthpart and 21 other tissues.
DR ExpressionAtlas; Q95T64; baseline and differential.
DR Genevisible; Q95T64; DM.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEP:FlyBase.
DR GO; GO:0006955; P:immune response; ISS: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 GO; GO:0009617; P:response to bacterium; IDA: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; IPR015510; PGRP.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR PANTHER; PTHR11022; PTHR11022; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; SSF55846; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunity; Innate immunity; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..368
FT /note="Peptidoglycan-recognition protein LA"
FT /id="PRO_0000220623"
FT TOPO_DOM 1..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..368
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 233..320
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT REGION 21..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT DISULFID 221..227
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..230
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11106397"
FT /id="VSP_013589"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11106397,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_013590"
FT VAR_SEQ 70..100
FT /note="VVIGPMTQYQGPVSIYYMDYMEAHAMQTAAG -> MKLLLKVHSERTARRRR
FT TPEPSLAHSRDSSR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11106397,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_013591"
FT VAR_SEQ 174..368
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11106397,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_013592"
FT CONFLICT 34
FT /note="S -> C (in Ref. 1; AAK00295)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="P -> S (in Ref. 1; AAK00295)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="N -> D (in Ref. 1; AAK00295)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 40821 MW; F55D07816539541C CRC64;
MFEENNSPTT DNSLWTLQGR QRASPAQRLH NLTSAGSSTS SSGLPLPQNI FTNPAIQPSS
VINLNHSTDV VIGPMTQYQG PVSIYYMDYM EAHAMQTAAG INSNNANGNG NANRSRDKSP
SRRVTRNTIL LITLILLVLA TGLIVLYVEL NRPKPELPSN KAIYFGNNYD HQTFPNLGNG
HLVVDREQWG ASKNSHGLTI PLKRPIPYVL ITHIGVQSLP CDNIYKCSIK MRTIQDSAIA
EKGLPDIQSN FYVSEEGNIY VGRGWDWANT YANQTLAITF MGDYGRFKPG PKQLEGVQFL
LAHAVANRNI DVDYKLVAQN QTKVTRSPGA YVYQEIRNWP HFYGCGMDEA PACGIELGMK
TESWDAKQ
