PGPLF_DROME
ID PGPLF_DROME Reviewed; 369 AA.
AC Q8SXQ7; Q9VSW0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Peptidoglycan-recognition protein LF;
DE AltName: Full=PGRP-like protein;
GN Name=PGRP-LF; ORFNames=CG4437;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [4]
RP IDENTIFICATION.
RX PubMed=12777387; DOI=10.1074/jbc.c300184200;
RA Werner T., Borge-Renberg K., Mellroth P., Steiner H., Hultmark D.;
RT "Functional diversity of the Drosophila PGRP-LC gene cluster in the
RT response to lipopolysaccharide and peptidoglycan.";
RL J. Biol. Chem. 278:26319-26322(2003).
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: Peptidoglycan-recognition protein probably involved in innate
CC immunity by binding to peptidoglycans (PGN) of bacteria and activating
CC the immune response.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Regulated by the imd/Relish pathway.
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; AE014296; AAF50301.2; -; Genomic_DNA.
DR EMBL; AY084190; AAL89928.1; -; mRNA.
DR RefSeq; NP_648299.3; NM_140042.3.
DR PDB; 2F2L; X-ray; 2.10 A; A=85-195.
DR PDB; 2XZ4; X-ray; 1.72 A; A/B=52-226.
DR PDB; 2XZ8; X-ray; 1.94 A; A/B=230-369.
DR PDBsum; 2F2L; -.
DR PDBsum; 2XZ4; -.
DR PDBsum; 2XZ8; -.
DR AlphaFoldDB; Q8SXQ7; -.
DR SMR; Q8SXQ7; -.
DR BioGRID; 64461; 8.
DR IntAct; Q8SXQ7; 6.
DR MINT; Q8SXQ7; -.
DR STRING; 7227.FBpp0076167; -.
DR GlyGen; Q8SXQ7; 2 sites.
DR PaxDb; Q8SXQ7; -.
DR PRIDE; Q8SXQ7; -.
DR EnsemblMetazoa; FBtr0076439; FBpp0076167; FBgn0035977.
DR GeneID; 39064; -.
DR KEGG; dme:Dmel_CG4437; -.
DR CTD; 39064; -.
DR FlyBase; FBgn0035977; PGRP-LF.
DR VEuPathDB; VectorBase:FBgn0035977; -.
DR eggNOG; ENOG502S2KY; Eukaryota.
DR GeneTree; ENSGT00940000166535; -.
DR HOGENOM; CLU_037559_1_2_1; -.
DR InParanoid; Q8SXQ7; -.
DR OMA; WHIQGSH; -.
DR OrthoDB; 1110472at2759; -.
DR PhylomeDB; Q8SXQ7; -.
DR BioGRID-ORCS; 39064; 0 hits in 3 CRISPR screens.
DR ChiTaRS; PGRP-LF; fly.
DR EvolutionaryTrace; Q8SXQ7; -.
DR GenomeRNAi; 39064; -.
DR PRO; PR:Q8SXQ7; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035977; Expressed in seminal fluid secreting gland and 19 other tissues.
DR Genevisible; Q8SXQ7; DM.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005102; F:signaling receptor binding; IPI:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019731; P:antibacterial humoral response; IMP:FlyBase.
DR GO; GO:0098542; P:defense response to other organism; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0050777; P:negative regulation of immune response; IMP:FlyBase.
DR GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR GO; GO:0009617; P:response to bacterium; IDA:FlyBase.
DR CDD; cd06583; PGRP; 2.
DR Gene3D; 3.40.80.10; -; 2.
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; 3.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 2.
DR SUPFAM; SSF55846; SSF55846; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Immunity; Innate immunity;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..369
FT /note="Peptidoglycan-recognition protein LF"
FT /id="PRO_0000220627"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 80..206
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..100
FT /evidence="ECO:0000250"
FT TURN 62..66
FT /evidence="ECO:0007829|PDB:2XZ4"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:2XZ4"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:2XZ4"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:2XZ4"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2XZ4"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2XZ4"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:2XZ4"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2XZ4"
FT HELIX 168..183
FT /evidence="ECO:0007829|PDB:2XZ4"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:2XZ4"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:2XZ4"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2XZ4"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:2XZ4"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:2XZ8"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:2XZ8"
FT HELIX 274..290
FT /evidence="ECO:0007829|PDB:2XZ8"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:2XZ8"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:2XZ8"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:2XZ8"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:2XZ8"
FT HELIX 337..352
FT /evidence="ECO:0007829|PDB:2XZ8"
FT STRAND 355..364
FT /evidence="ECO:0007829|PDB:2XZ8"
SQ SEQUENCE 369 AA; 41966 MW; 01465701EE5DD289 CRC64;
MPKTVVVTHP GKPINNEKRF RFELLYFCVI LLMVVGLAAG YFMWMMSFST HSPNKGLHIL
DRSEWLGEPP SGKYPHLKLP VSNIIIHHTA TEGCEQEDVC IYRMKTIQAF HMKSFGWVDI
GYNFLVGGDG QIYVGRGWHI QGQHVNGYGA ISVSIAFIGT FVNMEPPARQ IEAAKRLMDE
GVRLHRLQPD YHIYAHRQLS PTESPGQKLF ELMQNWPRFT QDPTSLRLLS NETVKIVTRP
YWLAQPPIVP LTPLKLPIES VRFVATNTPS CFTQAECTFR VRLLQNWHIE SNGYKDINYN
FVAAGDENIY EARGWDHSCE PPKDADELVV AFIGPSSSNK KIALELIKQG IKLGHISKNY
SLIDDLEKS
