PG4_PIG
ID PG4_PIG Reviewed; 149 AA.
AC P49933;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Protegrin-4;
DE Short=PG-4;
DE Flags: Precursor;
GN Name=NPG4;
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 STRUCTURE BY NMR OF 30-130, AND DISULFIDE BONDS.
RX PubMed=12705830; DOI=10.1021/bi027133c;
RA Yang Y., Sanchez J.F., Strub M.-P., Brutscher B., Aumelas A.;
RT "NMR structure of the cathelin-like domain of the protegrin-3 precursor.";
RL Biochemistry 42:4669-4680(2003).
CC -!- FUNCTION: Microbicidal activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR EMBL; X83268; CAA58241.1; -; mRNA.
DR PIR; B53895; B53895.
DR PDB; 1N5H; NMR; -; A=30-130.
DR PDB; 1N5P; NMR; -; A=30-130.
DR PDB; 6QKF; NMR; -; A=131-148.
DR PDBsum; 1N5H; -.
DR PDBsum; 1N5P; -.
DR PDBsum; 6QKF; -.
DR AlphaFoldDB; P49933; -.
DR BMRB; P49933; -.
DR SMR; P49933; -.
DR InParanoid; P49933; -.
DR ChiTaRS; NPG4; pig.
DR EvolutionaryTrace; P49933; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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; Disulfide bond;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..130
FT /evidence="ECO:0000255"
FT /id="PRO_0000004750"
FT PEPTIDE 131..148
FT /note="Protegrin-4"
FT /id="PRO_0000004751"
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 /evidence="ECO:0000269|PubMed:12705830"
FT DISULFID 107..124
FT /evidence="ECO:0000269|PubMed:12705830"
FT DISULFID 136..145
FT /evidence="ECO:0000250"
FT DISULFID 138..143
FT /evidence="ECO:0000250"
FT HELIX 34..48
FT /evidence="ECO:0007829|PDB:1N5H"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:1N5H"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:1N5H"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1N5H"
FT STRAND 74..88
FT /evidence="ECO:0007829|PDB:1N5H"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1N5H"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:1N5H"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1N5H"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:1N5H"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:6QKF"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:6QKF"
SQ SEQUENCE 149 AA; 16622 MW; A9BAA88429D66ECD CRC64;
METQRASLCL GRWSLWLLLL ALVVPSASAQ ALSYREAVLR AVDRLNEQSS EANLYRLLEL
DQPPKADEDP GTPKPVSFTV KETVCPRPTR QPPELCDFKE NGRVKQCVGT VTLDQIKDPL
DITCNEVQGV RGGRLCYCRG WICFCVGRG
