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PG5_PIG
ID   PG5_PIG                 Reviewed;         149 AA.
AC   P49934;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Protegrin-5;
DE            Short=PG-5;
DE   Flags: Precursor;
GN   Name=NPG5;
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 [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).
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; X84096; CAA58892.1; -; Genomic_DNA.
DR   PIR; S66283; S57609.
DR   PDB; 2NC7; NMR; -; A=131-148.
DR   PDBsum; 2NC7; -.
DR   AlphaFoldDB; P49934; -.
DR   BMRB; P49934; -.
DR   SMR; P49934; -.
DR   STRING; 9823.ENSSSCP00000027630; -.
DR   PeptideAtlas; P49934; -.
DR   InParanoid; P49934; -.
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_0000004752"
FT   PEPTIDE         131..148
FT                   /note="Protegrin-5"
FT                   /id="PRO_0000004753"
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:0000250"
FT   DISULFID        107..124
FT                   /evidence="ECO:0000250"
FT   DISULFID        136..145
FT                   /evidence="ECO:0000250"
FT   DISULFID        138..143
FT                   /evidence="ECO:0000250"
FT   STRAND          135..139
FT                   /evidence="ECO:0007829|PDB:2NC7"
FT   STRAND          142..146
FT                   /evidence="ECO:0007829|PDB:2NC7"
SQ   SEQUENCE   149 AA;  16604 MW;  6CC7262429CD6B64 CRC64;
     METQRASLCL GRWSLWLLLL GLVVPSASAQ ALSYREAVLR AVDRLNEQSS EANLYRLLEL
     DQPPKADEDP GTPKPVSFTV KETVCPRPTR QPPELCDFKE NGRVKQCVGT VTLDQIKDPL
     DITCNEVQGV RGGRLCYCRP RFCVCVGRG
 
 
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