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Q96LB9 (PGRP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidoglycan recognition protein 3
Alternative name(s):
Peptidoglycan recognition protein I-alpha
Short name=PGLYRPIalpha
Short name=PGRP-I-alpha
Peptidoglycan recognition protein intermediate alpha
Gene names
Name:PGLYRP3
Synonyms:PGRPIA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram-negative bacteria, and has bacteriostatic activity towards Gram-negative bacteria. Plays a role in innate immunity. Ref.4

Subunit structure

Monomer. Homodimer; disulfide-linked. Heterodimer with PGLYRP4; disulfide-linked. Ref.4 Ref.5

Subcellular location

Secreted Ref.4.

Tissue specificity

Detected in skin epidermis, eccrine sweat glands and ducts, ciliary body epithelial cells of the eye, in small intestine, colon, stomach and in mature epithelial cells of the tongue (at protein level). Highly expressed in skin and esophagus, expressed also in tonsils and thymus and to a much lesser extent in the stomach, descending colon, rectum and brain. Ref.1 Ref.4

Induction

Up-regulated by exposure to Gram-positive and Gram-negative bacteria. Ref.4

Post-translational modification

N-glycosylated. Ref.4

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

Ontologies

Keywords
   Biological processImmunity
Innate immunity
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionAntibiotic
Antimicrobial
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to Gram-positive bacterium

Inferred from direct assay Ref.1. Source: UniProtKB

detection of bacterium

Inferred from direct assay Ref.1. Source: UniProtKB

growth of symbiont in host

Inferred from electronic annotation. Source: Ensembl

innate immune response

Non-traceable author statement Ref.1. Source: UniProtKB

negative regulation of interferon-gamma production

Inferred from electronic annotation. Source: Ensembl

negative regulation of natural killer cell differentiation involved in immune response

Inferred from electronic annotation. Source: Ensembl

pattern recognition receptor signaling pathway

Inferred from direct assay Ref.1. Source: GOC

peptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Non-traceable author statement Ref.1. Source: UniProtKB

membrane

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from electronic annotation. Source: InterPro

peptidoglycan binding

Inferred from direct assay Ref.1PubMed 17502600. Source: UniProtKB

peptidoglycan receptor activity

Inferred from direct assay Ref.1. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 341324Peptidoglycan recognition protein 3
PRO_0000023923

Regions

Region264 – 2696Interaction with murein

Sites

Binding site2311Murein
Binding site2351Murein
Binding site2421Murein

Amino acid modifications

Glycosylation1131N-linked (GlcNAc...) Potential
Disulfide bond178 ↔ 300
Disulfide bond194 ↔ 238
Disulfide bond214 ↔ 220

Natural variations

Natural variant351A → T.
Corresponds to variant rs55991125 [ dbSNP | Ensembl ].
VAR_061515
Natural variant1261G → S. Ref.3
Corresponds to variant rs843971 [ dbSNP | Ensembl ].
VAR_024561

Secondary structure

............................... 341
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96LB9 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 8ADD5AA97B632076

FASTA34137,611
        10         20         30         40         50         60 
MGTLPWLLAF FILGLQAWDT PTIVSRKEWG ARPLACRALL TLPVAYIITD QLPGMQCQQQ 

        70         80         90        100        110        120 
SVCSQMLRGL QSHSVYTIGW CDVAYNFLVG DDGRVYEGVG WNIQGLHTQG YNNISLGIAF 

       130        140        150        160        170        180 
FGNKIGSSPS PAALSAAEGL ISYAIQKGHL SPRYIQPLLL KEETCLDPQH PVMPRKVCPN 

       190        200        210        220        230        240 
IIKRSAWEAR ETHCPKMNLP AKYVIIIHTA GTSCTVSTDC QTVVRNIQSF HMDTRNFCDI 

       250        260        270        280        290        300 
GYHFLVGQDG GVYEGVGWHI QGSHTYGFND IALGIAFIGY FVEKPPNAAA LEAAQDLIQC 

       310        320        330        340 
AVVEGYLTPN YLLMGHSDVV NILSPGQALY NIISTWPHFK H 

« Hide

References

« Hide 'large scale' references
[1]"Peptidoglycan recognition proteins: a novel family of four human innate immunity pattern recognition molecules."
Liu C., Xu Z., Gupta D., Dziarski R.
J. Biol. Chem. 276:34686-34694(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-126.
[4]"Peptidoglycan recognition proteins are a new class of human bactericidal proteins."
Lu X., Wang M., Qi J., Wang H., Li X., Gupta D., Dziarski R.
J. Biol. Chem. 281:5895-5907(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, GLYCOSYLATION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
[5]"Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein Ialpha."
Guan R., Malchiodi E.L., Wang Q., Schuck P., Mariuzza R.A.
J. Biol. Chem. 279:31873-31882(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 177-341, SUBUNIT.
[6]"Structural basis for peptidoglycan binding by peptidoglycan recognition proteins."
Guan R., Roychowdhury A., Ember B., Kumar S., Boons G.-J., Mariuzza R.A.
Proc. Natl. Acad. Sci. U.S.A. 101:17168-17173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 177-341 IN COMPLEX WITH MUREIN FRAGMENT.
[7]"Crystal structure of human peptidoglycan recognition protein I alpha bound to a muramyl pentapeptide from Gram-positive bacteria."
Guan R., Brown P.H., Swaminathan C.P., Roychowdhury A., Boons G.-J., Mariuzza R.A.
Protein Sci. 15:1199-1206(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 177-341 IN COMPLEX WITH MUREIN FRAGMENT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY035376 mRNA. Translation: AAK72484.1.
AL591704, AL161636 Genomic DNA. Translation: CAI19491.1.
AL161636, AL591704 Genomic DNA. Translation: CAI19556.1.
BC069741 mRNA. Translation: AAH69741.1.
BC069798 mRNA. Translation: AAH69798.1.
BC069801 mRNA. Translation: AAH69801.1.
BC128114 mRNA. Translation: AAI28115.1.
BC128115 mRNA. Translation: AAI28116.1.
CCDSCCDS1035.1.
RefSeqNP_443123.1. NM_052891.1.
UniGeneHs.348266.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SK3X-ray2.80A177-341[»]
1SK4X-ray1.65A179-341[»]
1TWQX-ray2.30A177-341[»]
2APHX-ray2.10A/B177-341[»]
ProteinModelPortalQ96LB9.
SMRQ96LB9. Positions 21-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000290722.

PTM databases

PhosphoSiteQ96LB9.

Polymorphism databases

DMDM38604974.

Proteomic databases

PaxDbQ96LB9.
PRIDEQ96LB9.

Protocols and materials databases

DNASU114771.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290722; ENSP00000290722; ENSG00000159527.
GeneID114771.
KEGGhsa:114771.
UCSCuc001fbn.1. human.

Organism-specific databases

CTD114771.
GeneCardsGC01M153270.
HGNCHGNC:30014. PGLYRP3.
HPAHPA030369.
MIM608197. gene.
neXtProtNX_Q96LB9.
PharmGKBPA134861692.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5479.
HOGENOMHOG000267017.
HOVERGENHBG053579.
InParanoidQ96LB9.
KOK01446.
OMAVEKPPNA.
OrthoDBEOG757CZ5.
PhylomeDBQ96LB9.
TreeFamTF323898.

Gene expression databases

BgeeQ96LB9.
CleanExHS_PGLYRP3.
GenevestigatorQ96LB9.

Family and domain databases

Gene3D3.40.80.10. 2 hits.
InterProIPR002502. Amidase_domain.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
PANTHERPTHR11022. PTHR11022. 1 hit.
PfamPF01510. Amidase_2. 2 hits.
[Graphical view]
SMARTSM00644. Ami_2. 2 hits.
SM00701. PGRP. 2 hits.
[Graphical view]
SUPFAMSSF55846. SSF55846. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceQ96LB9.
GenomeRNAi114771.
NextBio79145.
PROQ96LB9.
SOURCESearch...

Entry information

Entry namePGRP3_HUMAN
AccessionPrimary (citable) accession number: Q96LB9
Secondary accession number(s): A1A4U8, Q5SY65
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM