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Protein

Peptidoglycan recognition protein 3

Gene

PGLYRP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei231 – 2311Murein
Binding sitei235 – 2351Murein
Binding sitei242 – 2421Murein

GO - Molecular functioni

  • N-acetylmuramoyl-L-alanine amidase activity Source: InterPro
  • peptidoglycan binding Source: UniProtKB
  • peptidoglycan receptor activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

Keywords - Biological processi

Immunity, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PGLYRP3
Synonyms:PGRPIA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:30014. PGLYRP3.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • intracellular Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134861692.

Polymorphism and mutation databases

BioMutaiPGLYRP3.
DMDMi38604974.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 341324Peptidoglycan recognition protein 3PRO_0000023923Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi178 ↔ 300
Disulfide bondi194 ↔ 238
Disulfide bondi214 ↔ 220

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ96LB9.
PRIDEiQ96LB9.

PTM databases

PhosphoSiteiQ96LB9.

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

Up-regulated by exposure to Gram-positive and Gram-negative bacteria.1 Publication

Gene expression databases

BgeeiQ96LB9.
CleanExiHS_PGLYRP3.
GenevisibleiQ96LB9. HS.

Organism-specific databases

HPAiHPA030369.

Interactioni

Subunit structurei

Monomer. Homodimer; disulfide-linked. Heterodimer with PGLYRP4; disulfide-linked.4 Publications

Protein-protein interaction databases

BioGridi125341. 2 interactions.
STRINGi9606.ENSP00000290722.

Structurei

Secondary structure

1
341
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi184 – 1874Combined sources
Beta strandi199 – 20810Combined sources
Helixi217 – 23317Combined sources
Beta strandi243 – 2464Combined sources
Beta strandi252 – 2565Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi263 – 2653Combined sources
Turni269 – 2713Combined sources
Beta strandi272 – 2798Combined sources
Beta strandi282 – 2843Combined sources
Helixi288 – 30316Combined sources
Beta strandi306 – 31510Combined sources
Helixi316 – 3183Combined sources
Beta strandi320 – 3223Combined sources
Helixi328 – 3336Combined sources
Turni337 – 3404Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SK3X-ray2.80A177-341[»]
1SK4X-ray1.65A179-341[»]
1TWQX-ray2.30A177-341[»]
2APHX-ray2.10A/B177-341[»]
ProteinModelPortaliQ96LB9.
SMRiQ96LB9. Positions 21-341.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96LB9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni264 – 2696Interaction with murein

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5479.
GeneTreeiENSGT00390000016833.
HOGENOMiHOG000267017.
HOVERGENiHBG053579.
InParanoidiQ96LB9.
KOiK01446.
OMAiVEKPPNA.
OrthoDBiEOG757CZ5.
PhylomeDBiQ96LB9.
TreeFamiTF323898.

Family and domain databases

Gene3Di3.40.80.10. 2 hits.
InterProiIPR002502. Amidase_domain.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
PANTHERiPTHR11022. PTHR11022. 1 hit.
PfamiPF01510. Amidase_2. 2 hits.
[Graphical view]
SMARTiSM00644. Ami_2. 2 hits.
SM00701. PGRP. 2 hits.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96LB9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTLPWLLAF FILGLQAWDT PTIVSRKEWG ARPLACRALL TLPVAYIITD
60 70 80 90 100
QLPGMQCQQQ SVCSQMLRGL QSHSVYTIGW CDVAYNFLVG DDGRVYEGVG
110 120 130 140 150
WNIQGLHTQG YNNISLGIAF FGNKIGSSPS PAALSAAEGL ISYAIQKGHL
160 170 180 190 200
SPRYIQPLLL KEETCLDPQH PVMPRKVCPN IIKRSAWEAR ETHCPKMNLP
210 220 230 240 250
AKYVIIIHTA GTSCTVSTDC QTVVRNIQSF HMDTRNFCDI GYHFLVGQDG
260 270 280 290 300
GVYEGVGWHI QGSHTYGFND IALGIAFIGY FVEKPPNAAA LEAAQDLIQC
310 320 330 340
AVVEGYLTPN YLLMGHSDVV NILSPGQALY NIISTWPHFK H
Length:341
Mass (Da):37,611
Last modified:December 1, 2001 - v1
Checksum:i8ADD5AA97B632076
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351A → T.
Corresponds to variant rs55991125 [ dbSNP | Ensembl ].
VAR_061515
Natural varianti126 – 1261G → S.1 Publication
Corresponds to variant rs843971 [ dbSNP | Ensembl ].
VAR_024561

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1035.1.
RefSeqiNP_443123.1. NM_052891.2.
UniGeneiHs.348266.

Genome annotation databases

EnsembliENST00000290722; ENSP00000290722; ENSG00000159527.
GeneIDi114771.
KEGGihsa:114771.
UCSCiuc001fbn.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1035.1.
RefSeqiNP_443123.1. NM_052891.2.
UniGeneiHs.348266.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SK3X-ray2.80A177-341[»]
1SK4X-ray1.65A179-341[»]
1TWQX-ray2.30A177-341[»]
2APHX-ray2.10A/B177-341[»]
ProteinModelPortaliQ96LB9.
SMRiQ96LB9. Positions 21-341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125341. 2 interactions.
STRINGi9606.ENSP00000290722.

PTM databases

PhosphoSiteiQ96LB9.

Polymorphism and mutation databases

BioMutaiPGLYRP3.
DMDMi38604974.

Proteomic databases

PaxDbiQ96LB9.
PRIDEiQ96LB9.

Protocols and materials databases

DNASUi114771.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000290722; ENSP00000290722; ENSG00000159527.
GeneIDi114771.
KEGGihsa:114771.
UCSCiuc001fbn.1. human.

Organism-specific databases

CTDi114771.
GeneCardsiGC01M153270.
HGNCiHGNC:30014. PGLYRP3.
HPAiHPA030369.
MIMi608197. gene.
neXtProtiNX_Q96LB9.
PharmGKBiPA134861692.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5479.
GeneTreeiENSGT00390000016833.
HOGENOMiHOG000267017.
HOVERGENiHBG053579.
InParanoidiQ96LB9.
KOiK01446.
OMAiVEKPPNA.
OrthoDBiEOG757CZ5.
PhylomeDBiQ96LB9.
TreeFamiTF323898.

Miscellaneous databases

EvolutionaryTraceiQ96LB9.
GenomeRNAii114771.
NextBioi79145.
PROiQ96LB9.
SOURCEiSearch...

Gene expression databases

BgeeiQ96LB9.
CleanExiHS_PGLYRP3.
GenevisibleiQ96LB9. HS.

Family and domain databases

Gene3Di3.40.80.10. 2 hits.
InterProiIPR002502. Amidase_domain.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
PANTHERiPTHR11022. PTHR11022. 1 hit.
PfamiPF01510. Amidase_2. 2 hits.
[Graphical view]
SMARTiSM00644. Ami_2. 2 hits.
SM00701. PGRP. 2 hits.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPGRP3_HUMAN
AccessioniPrimary (citable) accession number: Q96LB9
Secondary accession number(s): A1A4U8, Q5SY65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.