ID PGRP1_HUMAN Reviewed; 196 AA. AC O75594; Q4VB36; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 13-FEB-2019, entry version 157. DE RecName: Full=Peptidoglycan recognition protein 1; DE AltName: Full=Peptidoglycan recognition protein short; DE Short=PGRP-S; DE Flags: Precursor; GN Name=PGLYRP1; Synonyms=PGLYRP, PGRP, TNFSF3L; GN ORFNames=SBBI68, UNQ639/PRO1269; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Bone marrow; RX PubMed=9707603; DOI=10.1073/pnas.95.17.10078; RA Kang D., Liu G., Lundstroem A., Gelius E., Steiner H.; RT "A peptidoglycan recognition protein in innate immunity conserved from RT insects to humans."; RL Proc. Natl. Acad. Sci. U.S.A. 95:10078-10082(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Wan T., Zhang W., Cao X.; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=11461926; DOI=10.1074/jbc.M105566200; RA Liu C., Xu Z., Gupta D., Dziarski R.; RT "Peptidoglycan recognition proteins: a novel family of four human RT innate immunity pattern recognition molecules."; RL J. Biol. Chem. 276:34686-34694(2001). RN [7] RP FUNCTION, SUBUNIT, GLYCOSYLATION, AND SUBCELLULAR LOCATION. RX PubMed=16354652; DOI=10.1074/jbc.M511631200; RA Lu X., Wang M., Qi J., Wang H., Li X., Gupta D., Dziarski R.; RT "Peptidoglycan recognition proteins are a new class of human RT bactericidal proteins."; RL J. Biol. Chem. 281:5895-5907(2006). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-196, AND DISULFIDE BONDS. RX PubMed=15769462; DOI=10.1016/j.jmb.2005.01.070; RA Guan R., Wang Q., Sundberg E.J., Mariuzza R.A.; RT "Crystal structure of human peptidoglycan recognition protein S (PGRP- RT S) at 1.70 A resolution."; RL J. Mol. Biol. 347:683-691(2005). CC -!- FUNCTION: Pattern receptor that binds to murein peptidoglycans CC (PGN) of Gram-positive bacteria. Has bactericidal activity towards CC Gram-positive bacteria. May kill Gram-positive bacteria by CC interfering with peptidoglycan biosynthesis. Binds also to Gram- CC negative bacteria, and has bacteriostatic activity towards Gram- CC negative bacteria. Plays a role in innate immunity. CC {ECO:0000269|PubMed:11461926, ECO:0000269|PubMed:16354652}. CC -!- SUBUNIT: Homodimer; disulfide-linked. CC {ECO:0000269|PubMed:15769462, ECO:0000269|PubMed:16354652}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16354652}. CC Cytoplasmic granule {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Highly expressed in bone marrow. Weak CC expression found in kidney, liver, small intestine, spleen, CC thymus, peripheral leukocyte, lung, fetal spleen and neutrophils. CC {ECO:0000269|PubMed:11461926, ECO:0000269|PubMed:9707603}. CC -!- PTM: N-glycosylated. N-glycosylation is required for bactericidal CC activity. {ECO:0000269|PubMed:16354652}. CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AF076483; AAC31822.1; -; mRNA. DR EMBL; AF242517; AAF99598.1; -; mRNA. DR EMBL; AY358936; AAQ89295.1; -; mRNA. DR EMBL; AC007785; AAD38243.1; -; Genomic_DNA. DR EMBL; BC096154; AAH96154.1; -; mRNA. DR EMBL; BC096155; AAH96155.1; -; mRNA. DR EMBL; BC096156; AAH96156.1; -; mRNA. DR EMBL; BC096157; AAH96157.1; -; mRNA. DR EMBL; BC101845; AAI01846.1; -; mRNA. DR EMBL; BC101847; AAI01848.1; -; mRNA. DR CCDS; CCDS12680.1; -. DR RefSeq; NP_005082.1; NM_005091.2. DR UniGene; Hs.137583; -. DR PDB; 1YCK; X-ray; 1.70 A; A=22-196. DR PDBsum; 1YCK; -. DR ProteinModelPortal; O75594; -. DR SMR; O75594; -. DR BioGrid; 114474; 3. DR IntAct; O75594; 1. DR MINT; O75594; -. DR STRING; 9606.ENSP00000008938; -. DR iPTMnet; O75594; -. DR PhosphoSitePlus; O75594; -. DR BioMuta; PGLYRP1; -. DR jPOST; O75594; -. DR PaxDb; O75594; -. DR PeptideAtlas; O75594; -. DR PRIDE; O75594; -. DR ProteomicsDB; 50104; -. DR DNASU; 8993; -. DR Ensembl; ENST00000008938; ENSP00000008938; ENSG00000008438. DR GeneID; 8993; -. DR KEGG; hsa:8993; -. DR UCSC; uc002pdx.4; human. DR CTD; 8993; -. DR DisGeNET; 8993; -. DR EuPathDB; HostDB:ENSG00000008438.4; -. DR GeneCards; PGLYRP1; -. DR HGNC; HGNC:8904; PGLYRP1. DR HPA; HPA045702; -. DR MIM; 604963; gene. DR neXtProt; NX_O75594; -. DR OpenTargets; ENSG00000008438; -. DR PharmGKB; PA33241; -. DR eggNOG; ENOG410IYTD; Eukaryota. DR eggNOG; ENOG4111PQD; LUCA. DR GeneTree; ENSGT00940000161006; -. DR HOGENOM; HOG000267017; -. DR HOVERGEN; HBG007406; -. DR InParanoid; O75594; -. DR KO; K01446; -. DR OMA; IQNWPHY; -. DR OrthoDB; 1110472at2759; -. DR PhylomeDB; O75594; -. DR TreeFam; TF323898; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-6803157; Antimicrobial peptides. DR EvolutionaryTrace; O75594; -. DR GeneWiki; PGLYRP1; -. DR GenomeRNAi; 8993; -. DR PRO; PR:O75594; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000008438; Expressed in 79 organ(s), highest expression level in bone marrow. DR Genevisible; O75594; HS. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0097013; C:phagocytic vesicle lumen; TAS:Reactome. DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome. DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome. DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IBA:GO_Central. DR GO; GO:0042834; F:peptidoglycan binding; IDA:UniProtKB. DR GO; GO:0016019; F:peptidoglycan receptor activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB. DR GO; GO:0019730; P:antimicrobial humoral response; IBA:GO_Central. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB. DR GO; GO:0016045; P:detection of bacterium; IDA:UniProtKB. DR GO; GO:0044117; P:growth of symbiont in host; IEA:Ensembl. DR GO; GO:0045087; P:innate immune response; NAS:UniProtKB. DR GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB. DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl. DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IBA:GO_Central. DR GO; GO:0032827; P:negative regulation of natural killer cell differentiation involved in immune response; IBA:GO_Central. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR GO; GO:0051714; P:positive regulation of cytolysis in other organism; IDA:UniProtKB. DR CDD; cd06583; PGRP; 1. DR Gene3D; 3.40.80.10; -; 1. DR InterPro; IPR036505; Amidase/PGRP_sf. DR InterPro; IPR002502; Amidase_domain. DR InterPro; IPR017331; Peptidoglycan_recognition. DR InterPro; IPR015510; PGRP. DR InterPro; IPR006619; PGRP_domain_met/bac. DR PANTHER; PTHR11022; PTHR11022; 1. DR Pfam; PF01510; Amidase_2; 1. DR PIRSF; PIRSF037945; PGRPs; 1. DR SMART; SM00644; Ami_2; 1. DR SMART; SM00701; PGRP; 1. DR SUPFAM; SSF55846; SSF55846; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic; Antimicrobial; Complete proteome; KW Disulfide bond; Glycoprotein; Immunity; Innate immunity; Polymorphism; KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 196 Peptidoglycan recognition protein 1. FT /FTId=PRO_0000023901. FT DOMAIN 53 180 N-acetylmuramoyl-L-alanine amidase. FT {ECO:0000255}. FT MOD_RES 22 22 Pyrrolidone carboxylic acid. FT {ECO:0000250|UniProtKB:Q8SPP7}. FT CARBOHYD 112 112 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 30 154 {ECO:0000269|PubMed:15769462}. FT DISULFID 46 91 {ECO:0000269|PubMed:15769462}. FT DISULFID 67 73 {ECO:0000269|PubMed:15769462}. FT VARIANT 34 34 V -> G (in dbSNP:rs34180629). FT /FTId=VAR_050497. FT HELIX 36 39 {ECO:0000244|PDB:1YCK}. FT STRAND 52 61 {ECO:0000244|PDB:1YCK}. FT HELIX 70 86 {ECO:0000244|PDB:1YCK}. FT STRAND 96 99 {ECO:0000244|PDB:1YCK}. FT STRAND 105 109 {ECO:0000244|PDB:1YCK}. FT TURN 110 112 {ECO:0000244|PDB:1YCK}. FT STRAND 116 118 {ECO:0000244|PDB:1YCK}. FT TURN 120 122 {ECO:0000244|PDB:1YCK}. FT HELIX 123 125 {ECO:0000244|PDB:1YCK}. FT STRAND 126 133 {ECO:0000244|PDB:1YCK}. FT STRAND 136 138 {ECO:0000244|PDB:1YCK}. FT HELIX 142 157 {ECO:0000244|PDB:1YCK}. FT STRAND 160 169 {ECO:0000244|PDB:1YCK}. FT HELIX 170 172 {ECO:0000244|PDB:1YCK}. FT STRAND 174 176 {ECO:0000244|PDB:1YCK}. FT HELIX 181 187 {ECO:0000244|PDB:1YCK}. SQ SEQUENCE 196 AA; 21731 MW; D954C51440DC27DC CRC64; MSRRSMLLAW ALPSLLRLGA AQETEDPACC SPIVPRNEWK ALASECAQHL SLPLRYVVVS HTAGSSCNTP ASCQQQARNV QHYHMKTLGW CDVGYNFLIG EDGLVYEGRG WNFTGAHSGH LWNPMSIGIS FMGNYMDRVP TPQAIRAAQG LLACGVAQGA LRSNYVLKGH RDVQRTLSPG NQLYHLIQNW PHYRSP //