Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptidoglycan-recognition protein LC

Gene

PGRP-LC

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. Isoform a and isoform x mediate the induction by LPS and Gram-negative bacteria, while isoform x mediates the induction by peptidoglycan.3 Publications

GO - Molecular functioni

  • lipopolysaccharide receptor activity Source: FlyBase
  • peptidoglycan binding Source: FlyBase
  • peptidoglycan receptor activity Source: FlyBase
  • protein dimerization activity Source: FlyBase
  • signaling pattern recognition receptor activity Source: FlyBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • antibacterial humoral response Source: FlyBase
  • antimicrobial humoral response Source: FlyBase
  • defense response Source: FlyBase
  • defense response to Gram-negative bacterium Source: FlyBase
  • defense response to virus Source: FlyBase
  • detection of bacterium Source: FlyBase
  • immune response Source: FlyBase
  • innate immune response Source: FlyBase
  • peptidoglycan recognition protein signaling pathway Source: FlyBase
  • phagocytosis Source: FlyBase
  • positive regulation of antibacterial peptide biosynthetic process Source: FlyBase
  • positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria Source: FlyBase
  • regulation of humoral immune response Source: FlyBase
  • regulation of melanization defense response Source: FlyBase
  • response to bacterium Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Immunity, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidoglycan-recognition protein LC
Alternative name(s):
Immune response deficient 7 protein
Gene namesi
Name:PGRP-LC
Synonyms:ird7, PGRPLC
ORF Names:CG4432
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0035976. PGRP-LC.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 291291CytoplasmicSequence analysisAdd
BLAST
Transmembranei292 – 31221Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini313 – 520208ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • apicolateral plasma membrane Source: FlyBase
  • cytoplasm Source: FlyBase
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: FlyBase
  • plasma membrane Source: FlyBase
  • spanning component of plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 520520Peptidoglycan-recognition protein LCPRO_0000220624Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi389 – 3891N-linked (GlcNAc...)1 Publication
Disulfide bondi390 ↔ 3962 Publications
Glycosylationi515 – 5151N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9GNK5.
PRIDEiQ9GNK5.

Expressioni

Tissue specificityi

Expressed in the fat body and hemocytes.1 Publication

Developmental stagei

Expressed during larval and pupal stages.1 Publication

Gene expression databases

BgeeiQ9GNK5.
ExpressionAtlasiQ9GNK5. differential.
GenevisibleiQ9GNK5. DM.

Interactioni

GO - Molecular functioni

  • protein dimerization activity Source: FlyBase

Protein-protein interaction databases

BioGridi64460. 76 interactions.
IntActiQ9GNK5. 3 interactions.
MINTiMINT-948537.
STRINGi7227.FBpp0088492.

Structurei

Secondary structure

1
520
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi358 – 3614Combined sources
Beta strandi375 – 38410Combined sources
Helixi393 – 40917Combined sources
Beta strandi419 – 4224Combined sources
Beta strandi428 – 4325Combined sources
Turni433 – 4353Combined sources
Beta strandi440 – 4423Combined sources
Helixi444 – 4474Combined sources
Beta strandi451 – 4577Combined sources
Beta strandi460 – 4623Combined sources
Helixi466 – 48116Combined sources
Beta strandi484 – 49310Combined sources
Helixi494 – 4974Combined sources
Helixi502 – 5043Combined sources
Helixi507 – 5115Combined sources
Turni512 – 5154Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z6IX-ray2.50A355-520[»]
2F2LX-ray2.10A355-520[»]
X418-434[»]
ProteinModelPortaliQ9GNK5.
SMRiQ9GNK5. Positions 355-520.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9GNK5.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IXCZ. Eukaryota.
ENOG410ZJPX. LUCA.
GeneTreeiENSGT00390000016833.
InParanoidiQ9GNK5.
KOiK01446.
OMAiTEMSQCP.
OrthoDBiEOG757CZ5.
PhylomeDBiQ9GNK5.

Family and domain databases

Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
PANTHERiPTHR11022. PTHR11022. 1 hit.
SMARTiSM00701. PGRP. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform a1 Publication (identifier: Q9GNK5-1) [UniParc]FASTAAdd to basket

Also known as: B1 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPFSNETEMS QCSNAKRRVN DPLTGPKNCS TSSTDSGVIL NDNVAAFRPE
60 70 80 90 100
KETKDRGTGE GQFQSKSEEK TESKRISVEH TVNITTENVG KTSSPAVSIR
110 120 130 140 150
STTISVVSID DNAIDSSSID SDSEAEAEDY TVQKLGHQVT YPPNSSHLRD
160 170 180 190 200
LNQGLTVISR HVAPGEAAVP PPNPLEAGIV AKQILNGNLA VATPTSPAGG
210 220 230 240 250
ATQGIGSIAL TNSTDVTFGD KHFYEGPVTI QQFLIDNRDK WKPGEGPAGG
260 270 280 290 300
QDNPAFNGGP STNGSAPGSK HEDPAQTPPI CPFLPNTVGR KAVTVTVVFV
310 320 330 340 350
TLTFLLGIVL ATTTNLFGKT LNQSKIRDDD DYRQNIPINS TIDLDNIGGG
360 370 380 390 400
LILRFVERQQ WLAQPPQKEI PDLELPVGLV IALPTNSENC STQAICVLRV
410 420 430 440 450
RLLQTYDIES SQKCDIAYNF LIGGDGNVYV GRGWNKMGAH MNNINYDSQS
460 470 480 490 500
LSFAYIGSFK TIQPSAKQLS VTRLLLERGV KLGKIAPSYR FTASSKLMPS
510 520
VTDFKADALY ASFANWTHWS
Length:520
Mass (Da):56,046
Last modified:March 1, 2001 - v1
Checksum:i3215F8380857DFC1
GO
Isoform x1 Publication (identifier: Q9GNK5-2) [UniParc]FASTAAdd to basket

Also known as: A1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     324-520: SKIRDDDDYR...ASFANWTHWS → TDLDVIDNST...KKWPHWSHEI

Show »
Length:500
Mass (Da):54,094
Checksum:iA0459DE723A8C720
GO
Isoform y1 Publication (identifier: Q9GNK5-3) [UniParc]FASTAAdd to basket

Also known as: C1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     324-520: SKIRDDDDYR...ASFANWTHWS → TNDPEIHVDG...KTWPDLHMTQ

Show »
Length:511
Mass (Da):55,545
Checksum:i0969EE0AF556F549
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform y1 Publication (identifier: Q9GNK5-3)
Sequence conflicti338 – 3381I → V in AAS65052 (PubMed:10731132).Curated
Sequence conflicti355 – 3551L → F in AAS65052 (PubMed:10731132).Curated
Sequence conflicti373 – 3731T → K in AAQ16306 (PubMed:12777387).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei324 – 520197SKIRD…WTHWS → TDLDVIDNSTLVILKVAEWG GRPAKRMLDAQQLPINRVVI SHTAAEGCESREVCSARVNV VQSFHMDSWGWDHIGYNFLV GGDGRVYEGRGWDYVGAHTK GYNRGSIGISFIGTFTTRKP NERQLEACQLLLQEGVRLKK LTTNYRLYGHRQLSATESPG EELYKIIKKWPHWSHEI in isoform x. 4 PublicationsVSP_050759Add
BLAST
Alternative sequencei324 – 520197SKIRD…WTHWS → TNDPEIHVDGKLVVISIKGW GGMPTRGNLKPLKLPVSKVI ISETPPEICTTQDSCSYWTR VTQSRHMDTFNWSQVGYNFL VGGDGRIYEGRGWNYMGDHT RDNNNNSIGITFLGTFRRQE PTPKSLEACQLLIAQGVRLK KLKPDYQLLGHRQITGTLMP GEELYRIIQTWNNWYNLTKT WPDLHMTQ in isoform y. 2 PublicationsVSP_050760Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF207539 mRNA. Translation: AAG23733.1.
AF500096 mRNA. Translation: AAM18530.1.
AY327466 mRNA. Translation: AAQ16306.1.
AE014296 Genomic DNA. Translation: AAF50302.3.
AE014296 Genomic DNA. Translation: AAN11957.1.
AE014296 Genomic DNA. Translation: AAS65052.1.
AY119048 mRNA. Translation: AAM50908.1.
BT025958 mRNA. Translation: ABG02202.1.
RefSeqiNP_001163396.1. NM_001169925.1. [Q9GNK5-2]
NP_001246693.1. NM_001259764.1. [Q9GNK5-1]
NP_648298.1. NM_140041.4. [Q9GNK5-1]
NP_729468.2. NM_168324.4. [Q9GNK5-2]
NP_996030.1. NM_206308.4.
UniGeneiDm.1437.

Genome annotation databases

EnsemblMetazoaiFBtr0089491; FBpp0088492; FBgn0035976. [Q9GNK5-1]
FBtr0308349; FBpp0300668; FBgn0035976. [Q9GNK5-1]
GeneIDi39063.
KEGGidme:Dmel_CG4432.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF207539 mRNA. Translation: AAG23733.1.
AF500096 mRNA. Translation: AAM18530.1.
AY327466 mRNA. Translation: AAQ16306.1.
AE014296 Genomic DNA. Translation: AAF50302.3.
AE014296 Genomic DNA. Translation: AAN11957.1.
AE014296 Genomic DNA. Translation: AAS65052.1.
AY119048 mRNA. Translation: AAM50908.1.
BT025958 mRNA. Translation: ABG02202.1.
RefSeqiNP_001163396.1. NM_001169925.1. [Q9GNK5-2]
NP_001246693.1. NM_001259764.1. [Q9GNK5-1]
NP_648298.1. NM_140041.4. [Q9GNK5-1]
NP_729468.2. NM_168324.4. [Q9GNK5-2]
NP_996030.1. NM_206308.4.
UniGeneiDm.1437.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z6IX-ray2.50A355-520[»]
2F2LX-ray2.10A355-520[»]
X418-434[»]
ProteinModelPortaliQ9GNK5.
SMRiQ9GNK5. Positions 355-520.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64460. 76 interactions.
IntActiQ9GNK5. 3 interactions.
MINTiMINT-948537.
STRINGi7227.FBpp0088492.

Proteomic databases

PaxDbiQ9GNK5.
PRIDEiQ9GNK5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089491; FBpp0088492; FBgn0035976. [Q9GNK5-1]
FBtr0308349; FBpp0300668; FBgn0035976. [Q9GNK5-1]
GeneIDi39063.
KEGGidme:Dmel_CG4432.

Organism-specific databases

CTDi39063.
FlyBaseiFBgn0035976. PGRP-LC.

Phylogenomic databases

eggNOGiENOG410IXCZ. Eukaryota.
ENOG410ZJPX. LUCA.
GeneTreeiENSGT00390000016833.
InParanoidiQ9GNK5.
KOiK01446.
OMAiTEMSQCP.
OrthoDBiEOG757CZ5.
PhylomeDBiQ9GNK5.

Miscellaneous databases

EvolutionaryTraceiQ9GNK5.
GenomeRNAii39063.
PROiQ9GNK5.

Gene expression databases

BgeeiQ9GNK5.
ExpressionAtlasiQ9GNK5. differential.
GenevisibleiQ9GNK5. DM.

Family and domain databases

Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
PANTHERiPTHR11022. PTHR11022. 1 hit.
SMARTiSM00701. PGRP. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster."
    Werner T., Liu G., Kang D., Ekengren S., Steiner H., Hultmark D.
    Proc. Natl. Acad. Sci. U.S.A. 97:13772-13777(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; X AND Y), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Berkeley1 Publication and Canton-S1 Publication.
    Tissue: Embryo1 Publication, Head1 Publication, Larva1 Publication and Pupae1 Publication.
  2. "Requirement for a peptidoglycan recognition protein (PGRP) in Relish activation and antibacterial immune responses in Drosophila."
    Choe K.-M., Werner T., Stoeven S., Hultmark D., Anderson K.V.
    Science 296:359-362(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM X), FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    Strain: Berkeley1 Publication.
    Tissue: Larva1 Publication and Pupae1 Publication.
  3. "Functional diversity of the Drosophila PGRP-LC gene cluster in the response to lipopolysaccharide and peptidoglycan."
    Werner T., Borge-Renberg K., Mellroth P., Steiner H., Hultmark D.
    J. Biol. Chem. 278:26319-26322(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM Y), FUNCTION.
    Strain: Canton-SImported.
  4. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  5. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM X).
    Strain: Berkeley1 Publication.
    Tissue: Larva1 Publication and Pupae1 Publication.
  7. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM X).
    Strain: Berkeley.
  8. "Structure of the ectodomain of Drosophila peptidoglycan-recognition protein LCa suggests a molecular mechanism for pattern recognition."
    Chang C.-I., Ihara K., Chelliah Y., Mengin-Lecreulx D., Wakatsuki S., Deisenhofer J.
    Proc. Natl. Acad. Sci. U.S.A. 102:10279-10284(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 355-520, DISULFIDE BOND, FUNCTION.
  9. "Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor."
    Chang C.-I., Chelliah Y., Borek D., Mengin-Lecreulx D., Deisenhofer J.
    Science 311:1761-1764(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 355-520 IN COMPLEX WITH PEPTIDOGLYCAN FRAGMENT, DISULFIDE BOND, GLYCOSYLATION AT ASN-389 AND ASN-515.

Entry informationi

Entry nameiPGPLC_DROME
AccessioniPrimary (citable) accession number: Q9GNK5
Secondary accession number(s): Q1EBX6
, Q7YW58, Q8T5Q2, Q9VSV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.