ID PG3_PIG Reviewed; 149 AA. AC P32196; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 24-JAN-2024, entry version 119. DE RecName: Full=Protegrin-3; DE Short=PG-3; DE Flags: Precursor; GN Name=NPG3; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Bone marrow; RX PubMed=8013647; DOI=10.1016/0014-5793(94)00493-5; RA Zhao C., Liu L., Lehrer R.I.; RT "Identification of a new member of the protegrin family by cDNA cloning."; RL FEBS Lett. 346:285-288(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Red Duroc; RX PubMed=7628604; DOI=10.1016/0014-5793(95)00633-k; RA Zhao C., Ganz T., Lehrer R.I.; RT "The structure of porcine protegrin genes."; RL FEBS Lett. 368:197-202(1995). RN [3] RP PROTEIN SEQUENCE OF 131-148. RC TISSUE=Leukocyte; RX PubMed=8335113; DOI=10.1016/0014-5793(93)80175-t; RA Kokryakov V.N., Harwig S.S.L., Panyutich E.A., Shevchenko A.A., RA Aleshina G.M., Shamova O.V., Korneva H.A., Lehrer R.I.; RT "Protegrins: leukocyte antimicrobial peptides that combine features of RT corticostatic defensins and tachyplesins."; RL FEBS Lett. 327:231-236(1993). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 30-130, AND DISULFIDE BONDS. RX PubMed=12377122; DOI=10.1016/s0969-2126(02)00859-6; RA Sanchez J.F., Hoh F., Strub M.-P., Aumelas A., Dumas C.; RT "Structure of the cathelicidin motif of protegrin-3 precursor: structural RT insights into the activation mechanism of an antimicrobial protein."; RL Structure 10:1363-1370(2002). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 30-130, AND DISULFIDE BONDS. RX PubMed=14604526; DOI=10.1016/j.str.2003.09.014; RA Strub M.-P., Hoh F., Sanchez J.F., Strub J.-M., Bock A., Aumelas A., RA Dumas C.; RT "Selenomethionine and selenocysteine double labeling strategy for RT crystallographic phasing."; RL Structure 11:1359-1367(2003). CC -!- FUNCTION: Microbicidal activity. Active against E.coli, Listeria CC monocytogenes and C.albicans, in vitro. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the cathelicidin 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; X83267; CAA58240.1; -; mRNA. DR EMBL; X84095; CAA58891.1; -; Genomic_DNA. DR PIR; S66285; A53895. DR RefSeq; NP_001116622.1; NM_001123150.1. DR PDB; 1KWI; X-ray; 2.19 A; A=30-130. DR PDB; 1LXE; X-ray; 2.50 A; A=30-130. DR PDB; 1PFP; X-ray; 2.30 A; A=30-130. DR PDB; 2MZ6; NMR; -; A/B=131-148. DR PDBsum; 1KWI; -. DR PDBsum; 1LXE; -. DR PDBsum; 1PFP; -. DR PDBsum; 2MZ6; -. DR AlphaFoldDB; P32196; -. DR BMRB; P32196; -. DR SMR; P32196; -. DR PeptideAtlas; P32196; -. DR GeneID; 100144484; -. DR CTD; 100144484; -. DR InParanoid; P32196; -. DR EvolutionaryTrace; P32196; -. DR Proteomes; UP000008227; Chromosome 13. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR Bgee; ENSSSCG00000011349; Expressed in epididymis and 22 other cell types or tissues. DR ExpressionAtlas; P32196; differential. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0001530; F:lipopolysaccharide binding; IBA:GO_Central. DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IBA:GO_Central. DR Gene3D; 3.10.450.10; -; 1. DR InterPro; IPR001894; Cathelicidin-like. DR InterPro; IPR018216; Cathelicidin_CS. DR InterPro; IPR046350; Cystatin_sf. DR PANTHER; PTHR10206; CATHELICIDIN; 1. DR PANTHER; PTHR10206:SF2; CATHELICIDIN ANTIMICROBIAL PEPTIDE; 1. DR Pfam; PF00666; Cathelicidins; 1. DR SUPFAM; SSF54403; Cystatin/monellin; 1. DR PROSITE; PS00946; CATHELICIDINS_1; 1. DR PROSITE; PS00947; CATHELICIDINS_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Amidation; Antibiotic; Antimicrobial; KW Direct protein sequencing; Disulfide bond; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT PROPEP 30..130 FT /evidence="ECO:0000269|PubMed:8335113" FT /id="PRO_0000004748" FT PEPTIDE 131..148 FT /note="Protegrin-3" FT /id="PRO_0000004749" FT REGION 61..80 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 148 FT /note="Arginine amide" FT /evidence="ECO:0000250|UniProtKB:P32194" FT DISULFID 85..96 FT DISULFID 107..124 FT DISULFID 136..145 FT /evidence="ECO:0000250" FT DISULFID 138..143 FT /evidence="ECO:0000250" FT HELIX 32..48 FT /evidence="ECO:0007829|PDB:1KWI" FT STRAND 51..60 FT /evidence="ECO:0007829|PDB:1KWI" FT STRAND 74..88 FT /evidence="ECO:0007829|PDB:1KWI" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:1KWI" FT STRAND 104..111 FT /evidence="ECO:0007829|PDB:1KWI" FT STRAND 121..126 FT /evidence="ECO:0007829|PDB:1KWI" FT STRAND 135..139 FT /evidence="ECO:0007829|PDB:2MZ6" FT STRAND 142..147 FT /evidence="ECO:0007829|PDB:2MZ6" SQ SEQUENCE 149 AA; 16578 MW; 6F4BA98429CD6ED4 CRC64; METQRASLCL GRWSLWLLLL ALVVPSASAQ ALSYREAVLR AVDRLNEQSS EANLYRLLEL DQPPKADEDP GTPKPVSFTV KETVCPRPTR QPPELCDFKE NGRVKQCVGT VTLDQIKDPL DITCNEVQGV RGGGLCYCRR RFCVCVGRG //