ID   PF11_PIG                Reviewed;         212 AA.
AC   P51524;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Prophenin and tritrpticin precursor;
DE   AltName: Full=C6;
DE   Contains:
DE     RecName: Full=Prophenin-1;
DE              Short=PF-1;
DE   Contains:
DE     RecName: Full=Tritrpticin;
DE   Flags: Precursor; Fragment;
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=7576250; DOI=10.1515/bchm3.1995.376.8.507;
RA   Strukelj B., Pungercar J., Kopitar G., Renko M., Lenarcic B., Berbic S.,
RA   Turk V.;
RT   "Molecular cloning and identification of a novel porcine cathelin-like
RT   antibacterial peptide precursor.";
RL   Biol. Chem. Hoppe-Seyler 376:507-510(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 131-209.
RC   TISSUE=Blood;
RX   PubMed=7698355; DOI=10.1016/0014-5793(95)00210-z;
RA   Harwig S.S.L., Kokryakov V.N., Swiderek K.M., Aleshina G.M., Zhao C.,
RA   Lehrer R.I.;
RT   "Prophenin-1, an exceptionally proline-rich antimicrobial peptide from
RT   porcine leukocytes.";
RL   FEBS Lett. 362:65-69(1995).
RN   [3]
RP   STRUCTURE BY NMR OF 112-124, AND FUNCTION (TRITRPTICIN).
RX   PubMed=16997878; DOI=10.1529/biophysj.106.085837;
RA   Schibli D.J., Nguyen L.T., Kernaghan S.D., Rekdal O., Vogel H.J.;
RT   "Structure-function analysis of tritrpticin analogs: potential
RT   relationships between antimicrobial activities, model membrane
RT   interactions, and their micelle-bound NMR structures.";
RL   Biophys. J. 91:4413-4426(2006).
CC   -!- FUNCTION: [Prophenin-1]: Exerts antimicrobial activity. It is more
CC       effective against Gram-negative bacteria than Gram-positive bacteria.
CC       {ECO:0000269|PubMed:16997878}.
CC   -!- FUNCTION: [Tritrpticin]: Cathelicidin-like peptide with antimicrobial
CC       and hemolytic activities. {ECO:0000269|PubMed:16997878}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR   EMBL; X86031; CAA60023.1; -; mRNA.
DR   PIR; S57330; S57330.
DR   PDB; 2I1D; NMR; -; A=112-124.
DR   PDB; 2I1F; NMR; -; A=112-124.
DR   PDB; 2I1H; NMR; -; A=112-124.
DR   PDB; 2I1I; NMR; -; A=112-119.
DR   PDBsum; 2I1D; -.
DR   PDBsum; 2I1F; -.
DR   PDBsum; 2I1H; -.
DR   PDBsum; 2I1I; -.
DR   AlphaFoldDB; P51524; -.
DR   BMRB; P51524; -.
DR   SMR; P51524; -.
DR   PeptideAtlas; P51524; -.
DR   PRIDE; P51524; -.
DR   EvolutionaryTrace; P51524; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
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; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          <1..13
FT                   /evidence="ECO:0000255"
FT   PROPEP          14..130
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000004738"
FT   PEPTIDE         112..124
FT                   /note="Tritrpticin"
FT                   /id="PRO_0000422646"
FT   PEPTIDE         131..209
FT                   /note="Prophenin-1"
FT                   /id="PRO_0000004739"
FT   PROPEP          210..212
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000004740"
FT   REPEAT          132..141
FT                   /note="1"
FT   REPEAT          142..151
FT                   /note="2"
FT   REPEAT          152..161
FT                   /note="3"
FT   REPEAT          162..171
FT                   /note="4"
FT   REPEAT          172..181
FT                   /note="5"
FT   REPEAT          182..191
FT                   /note="6"
FT   REPEAT          192..201
FT                   /note="7"
FT   REGION          132..201
FT                   /note="7 X 10 AA tandem repeats"
FT   REGION          151..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         209
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000255"
FT   DISULFID        69..80
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..108
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   HELIX           119..122
FT                   /evidence="ECO:0007829|PDB:2I1D"
SQ   SEQUENCE   212 AA;  23956 MW;  A315414C90DBF423 CRC64;
     LLLLALVVPS ASAQALSYRE AVLRAVDRLN EQSSEANLYR LLELDQPPKA DEDPGTPKPV
     SFTVKETVCP RPTRQPPELC DFKENGRVKQ CVGTVTLDQI KDPLDITCNE GVRRFPWWWP
     FLRRPRLRRQ AFPPPNVPGP RFPPPNFPGP RFPPPNFPGP RFPPPNFPGP RFPPPNFPGP
     PFPPPIFPGP WFPPPPPFRP PPFGPPRFPG RR