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O75594 (PGRP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptidoglycan recognition protein 1
Alternative name(s):
Peptidoglycan recognition protein short
Short name=PGRP-S
Gene names
Name:PGLYRP1
Synonyms:PGLYRP, PGRP, TNFSF3L
ORF Names:SBBI68, UNQ639/PRO1269
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length196 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.6 Ref.7

Subunit structure

Homodimer; disulfide-linked. Ref.7 Ref.8

Subcellular location

Secreted. Cytoplasmic granule By similarity Ref.7.

Tissue specificity

Highly expressed in bone marrow. Weak expression found in kidney, liver, small intestine, spleen, thymus, peripheral leukocyte, lung, fetal spleen and neutrophils. Ref.1 Ref.6

Post-translational modification

N-glycosylated. N-glycosylation is required for bactericidal activity. Ref.7

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 196175Peptidoglycan recognition protein 1
PRO_0000023901

Amino acid modifications

Glycosylation1121N-linked (GlcNAc...) Potential
Disulfide bond30 ↔ 154 Ref.8
Disulfide bond46 ↔ 91 Ref.8
Disulfide bond67 ↔ 73 Ref.8

Natural variations

Natural variant341V → G.
Corresponds to variant rs34180629 [ dbSNP | Ensembl ].
VAR_050497

Secondary structure

............................. 196
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75594 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: D954C51440DC27DC

FASTA19621,731
        10         20         30         40         50         60 
MSRRSMLLAW ALPSLLRLGA AQETEDPACC SPIVPRNEWK ALASECAQHL SLPLRYVVVS 

        70         80         90        100        110        120 
HTAGSSCNTP ASCQQQARNV QHYHMKTLGW CDVGYNFLIG EDGLVYEGRG WNFTGAHSGH 

       130        140        150        160        170        180 
LWNPMSIGIS FMGNYMDRVP TPQAIRAAQG LLACGVAQGA LRSNYVLKGH RDVQRTLSPG 

       190 
NQLYHLIQNW PHYRSP 

« Hide

References

« Hide 'large scale' references
[1]"A peptidoglycan recognition protein in innate immunity conserved from insects to humans."
Kang D., Liu G., Lundstroem A., Gelius E., Steiner H.
Proc. Natl. Acad. Sci. U.S.A. 95:10078-10082(1998) [PubMed: 9707603] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Bone marrow.
[2]Wan T., Zhang W., Cao X.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed: 15057824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"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: 11461926] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[7]"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: 16354652] [Abstract]
Cited for: FUNCTION, SUBUNIT, GLYCOSYLATION, SUBCELLULAR LOCATION.
[8]"Crystal structure of human peptidoglycan recognition protein S (PGRP-S) at 1.70 A resolution."
Guan R., Wang Q., Sundberg E.J., Mariuzza R.A.
J. Mol. Biol. 347:683-691(2005) [PubMed: 15769462] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-196, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF076483 mRNA. Translation: AAC31822.1.
AF242517 mRNA. Translation: AAF99598.1.
AY358936 mRNA. Translation: AAQ89295.1.
AC007785 Genomic DNA. Translation: AAD38243.1.
BC096154 mRNA. Translation: AAH96154.1.
BC096155 mRNA. Translation: AAH96155.1.
BC096156 mRNA. Translation: AAH96156.1.
BC096157 mRNA. Translation: AAH96157.1.
BC101845 mRNA. Translation: AAI01846.1.
BC101847 mRNA. Translation: AAI01848.1.
IPIIPI00021085.
RefSeqNP_005082.1. NM_005091.2.
UniGeneHs.137583.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YCKX-ray1.70A22-196[»]
ProteinModelPortalO75594.
SMRO75594. Positions 30-196.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-3306405.
STRINGO75594.

PTM databases

PhosphoSiteO75594.

Proteomic databases

PeptideAtlasO75594.
PRIDEO75594.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000008938; ENSP00000008938; ENSG00000008438.
GeneID8993.
KEGGhsa:8993.
UCSCuc002pdx.1. human.

Organism-specific databases

CTD8993.
GeneCardsGC19M046522.
H-InvDBHIX0039958.
HGNCHGNC:8904. PGLYRP1.
HPAHPA045702.
MIM604963. gene.
neXtProtNX_O75594.
PharmGKBPA33241.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG11911.
GeneTreeENSGT00390000016833.
HOGENOMHBG268368.
HOVERGENHBG007406.
InParanoidO75594.
OMARNVQHYH.
OrthoDBEOG4DFPPK.
PhylomeDBO75594.

Gene expression databases

ArrayExpressO75594.
BgeeO75594.
CleanExHS_PGLYRP1.
GenevestigatorO75594.
GermOnlineENSG00000008438. Homo sapiens.

Family and domain databases

InterProIPR002502. Amidase_domain.
IPR017331. Peptidoglycan_recognition.
IPR015510. PGRP.
IPR006619. PGRP_domain_met/bac.
[Graphical view]
Gene3DG3DSA:3.40.80.10. Amidase_2. 1 hit.
KOK01446.
PANTHERPTHR11022. PGRPs. 1 hit.
PfamPF01510. Amidase_2. 1 hit.
[Graphical view]
PIRSFPIRSF037945. PGRPs. 1 hit.
SMARTSM00644. Ami_2. 1 hit.
SM00701. PGRP. 1 hit.
[Graphical view]
SUPFAMSSF55846. Amidase_2. 1 hit.
ProtoNetSearch...

Other

NextBio33723.
SOURCESearch...

Entry information

Entry namePGRP1_HUMAN
AccessionPrimary (citable) accession number: O75594
Secondary accession number(s): Q4VB36
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1998
Last modified: January 25, 2012
This is version 103 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

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families