PG3_PIG
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 03-AUG-2022, entry version 114.
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}.
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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 Ensembl; ENSSSCT00000012426; ENSSSCP00000012102; ENSSSCG00000011349.
DR Ensembl; ENSSSCT00000030874; ENSSSCP00000027630; ENSSSCG00000011349.
DR Ensembl; ENSSSCT00000040644; ENSSSCP00000031180; ENSSSCG00000011349.
DR Ensembl; ENSSSCT00000062800; ENSSSCP00000042988; ENSSSCG00000011349.
DR GeneID; 100144484; -.
DR CTD; 100144484; -.
DR GeneTree; ENSGT00390000000410; -.
DR InParanoid; P32196; -.
DR EvolutionaryTrace; P32196; -.
DR Proteomes; UP000008227; Chromosome 13.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000011349; Expressed in epididymis and 22 other tissues.
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 InterPro; IPR001894; Cathelicidin-like.
DR InterPro; IPR018216; Cathelicidin_CS.
DR InterPro; IPR046350; Cystatin_sf.
DR PANTHER; PTHR10206; PTHR10206; 1.
DR SUPFAM; SSF54403; SSF54403; 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
