PG1_PIG
ID PG1_PIG Reviewed; 149 AA.
AC P32194;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Protegrin-1;
DE Short=PG-1;
DE AltName: Full=Neutrophil peptide 1;
DE Flags: Precursor;
GN Name=NPG1;
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], AND AMIDATION AT ARG-148.
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 PROTEIN SEQUENCE OF 131-148.
RC TISSUE=Neutrophil;
RX PubMed=8375505; DOI=10.1016/0014-5793(93)80900-f;
RA Mirgorodskaya O.A., Shevchenko A.A., Abdalla K.O.M.A., Chernushevich I.V.,
RA Egorov T.A., Musoliamov A.X., Kokryakov V.N., Shamova O.V.;
RT "Primary structure of three cationic peptides from porcine neutrophils.
RT Sequence determination by the combined usage of electrospray ionization
RT mass spectrometry and Edman degradation.";
RL FEBS Lett. 330:339-342(1993).
RN [5]
RP STRUCTURE BY NMR OF PROTEGRIN 1.
RX PubMed=8647100; DOI=10.1111/j.1432-1033.1996.0575p.x;
RA Aumelase A., Mangoni M., Roumestand C., Chiche L., Despaux E., Grassy G.,
RA Calas B., Chavanieu A.;
RT "Synthesis and solution structure of the antimicrobial peptide protegrin-
RT 1.";
RL Eur. J. Biochem. 237:575-583(1996).
RN [6]
RP STRUCTURE BY NMR OF PROTEGRIN 1.
RX PubMed=8807886; DOI=10.1016/s1074-5521(96)90145-3;
RA Fahrner R.L., Dieckmann T., Harwig S.S., Lehrer R.I., Eisenberg D.,
RA Feigon J.;
RT "Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide
RT from porcine leukocytes.";
RL Chem. Biol. 3:543-550(1996).
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; X79868; CAA56251.1; -; mRNA.
DR EMBL; X84094; CAA58890.1; -; Genomic_DNA.
DR PIR; S66284; S57607.
DR RefSeq; NP_001116621.1; NM_001123149.1.
DR PDB; 1PG1; NMR; -; A=131-148.
DR PDB; 1ZY6; NMR; -; A/B=131-148.
DR PDBsum; 1PG1; -.
DR PDBsum; 1ZY6; -.
DR AlphaFoldDB; P32194; -.
DR BMRB; P32194; -.
DR SMR; P32194; -.
DR DIP; DIP-61300N; -.
DR TCDB; 1.C.33.1.9; the cathelicidin (cathelicidin) family.
DR PaxDb; P32194; -.
DR PeptideAtlas; P32194; -.
DR Ensembl; ENSSSCT00070010715; ENSSSCP00070008821; ENSSSCG00070005556.
DR GeneID; 100144483; -.
DR KEGG; ssc:100144483; -.
DR CTD; 100144483; -.
DR eggNOG; ENOG502SAES; Eukaryota.
DR InParanoid; P32194; -.
DR OrthoDB; 1534863at2759; -.
DR EvolutionaryTrace; P32194; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unassembled WGS sequence.
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 ECO:0000269|PubMed:8375505"
FT /id="PRO_0000004744"
FT PEPTIDE 131..148
FT /note="Protegrin-1"
FT /id="PRO_0000004745"
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:0000269|PubMed:8013647"
FT DISULFID 85..96
FT /evidence="ECO:0000250"
FT DISULFID 107..124
FT /evidence="ECO:0000250"
FT DISULFID 136..145
FT DISULFID 138..143
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:1PG1"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:1PG1"
SQ SEQUENCE 149 AA; 16677 MW; 6EFBA98429CD6EC4 CRC64;
METQRASLCL GRWSLWLLLL ALVVPSASAQ ALSYREAVLR AVDRLNEQSS EANLYRLLEL
DQPPKADEDP GTPKPVSFTV KETVCPRPTR QPPELCDFKE NGRVKQCVGT VTLDQIKDPL
DITCNEVQGV RGGRLCYCRR RFCVCVGRG
