PR39_PIG
ID PR39_PIG Reviewed; 172 AA.
AC P80054; Q9TR84;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Antibacterial protein PR-39;
DE Flags: Precursor;
GN Name=PR39;
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], AND AMIDATION AT PRO-169.
RX PubMed=7624374; DOI=10.1073/pnas.92.15.7085;
RA Gudmundsson G.H., Magnusson K.P., Chowdhary B.P., Johansson M.,
RA Andersson L., Boman H.G.;
RT "Structure of the gene for porcine peptide antibiotic PR-39, a cathelin
RT gene family member: comparative mapping of the locus for the human peptide
RT antibiotic FALL-39.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7085-7089(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone marrow;
RX PubMed=8250863; DOI=10.1006/bbrc.1993.2358;
RA Storici P., Zanetti M.;
RT "A cDNA derived from pig bone marrow cells predicts a sequence identical to
RT the intestinal antibacterial peptide PR-39.";
RL Biochem. Biophys. Res. Commun. 196:1058-1065(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=7498526; DOI=10.1016/0014-5793(95)01237-3;
RA Zhao C., Ganz T., Lehrer R.I.;
RT "Structures of genes for two cathelin-associated antimicrobial peptides:
RT prophenin-2 and PR-39.";
RL FEBS Lett. 376:130-134(1995).
RN [4]
RP PROTEIN SEQUENCE OF 131-169.
RC TISSUE=Intestine;
RX PubMed=1765098; DOI=10.1111/j.1432-1033.1991.tb16442.x;
RA Agerberth B., Lee J.-Y., Bergman T., Carlquist M., Boman H.G., Mutt V.,
RA Joernvall H.;
RT "Amino acid sequence of PR-39. Isolation from pig intestine of a new member
RT of the family of proline-arginine-rich antibacterial peptides.";
RL Eur. J. Biochem. 202:849-854(1991).
RN [5]
RP PROTEIN SEQUENCE OF 131-164, AND FUNCTION.
RC TISSUE=Neutrophil;
RX PubMed=7996056; DOI=10.1002/jlb.56.6.807;
RA Shi J., Ross C.R., Chengappa M.M., Blecha F.;
RT "Identification of a proline-arginine-rich antibacterial peptide from
RT neutrophils that is analogous to PR-39, an antibacterial peptide from the
RT small intestine.";
RL J. Leukoc. Biol. 56:807-811(1994).
CC -!- FUNCTION: Exerts a potent antimicrobial activity against both E.coli
CC and B.megaterium. {ECO:0000269|PubMed:7996056}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Small intestine and bone marrow.
CC -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR EMBL; X87236; CAA60682.1; -; Genomic_DNA.
DR EMBL; L23825; AAA31109.1; -; mRNA.
DR EMBL; X89201; CAA61487.1; -; Genomic_DNA.
DR PIR; S68232; S68232.
DR RefSeq; NP_999615.1; NM_214450.1.
DR PDB; 4EZO; X-ray; 1.90 A; C/D=131-145.
DR PDBsum; 4EZO; -.
DR AlphaFoldDB; P80054; -.
DR SMR; P80054; -.
DR BioGRID; 1150284; 3.
DR PeptideAtlas; P80054; -.
DR PRIDE; P80054; -.
DR Ensembl; ENSSSCT00070010353; ENSSSCP00070008501; ENSSSCG00070005376.
DR Ensembl; ENSSSCT00070021946; ENSSSCP00070018179; ENSSSCG00070011269.
DR GeneID; 407610; -.
DR KEGG; ssc:407610; -.
DR CTD; 407610; -.
DR InParanoid; P80054; -.
DR OrthoDB; 1534863at2759; -.
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; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..130
FT /evidence="ECO:0000269|PubMed:1765098,
FT ECO:0000269|PubMed:7996056"
FT /id="PRO_0000004730"
FT CHAIN 131..169
FT /note="Antibacterial protein PR-39"
FT /id="PRO_0000004731"
FT REGION 61..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..172
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P19660"
FT MOD_RES 169
FT /note="Proline amide"
FT /evidence="ECO:0000269|PubMed:7624374"
FT DISULFID 85..96
FT /evidence="ECO:0000250"
FT DISULFID 107..124
FT /evidence="ECO:0000250"
FT CONFLICT 21
FT /note="G -> A (in Ref. 2; AAA31109)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="A -> T (in Ref. 1; CAA60682)"
FT /evidence="ECO:0000305"
FT CONFLICT 90..91
FT /note="RQ -> QR (in Ref. 1; CAA60682)"
FT /evidence="ECO:0000305"
FT CONFLICT 117..119
FT /note="IHS -> NDP (in Ref. 1; CAA60682)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="P -> I (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 19477 MW; 994B792798C0E133 CRC64;
METQRASLCL GRWSLWLLLL GLVVPSASAQ ALSYREAVLR AVDRLNEQSS EANLYRLLEL
DQPPKADEDP GTPKPVSFTV KETVCPRPTR QPPELCDFKE NGRVKQCVGT VTLNPSIHSL
DISCNEIQSV RRRPRPPYLP RPRPPPFFPP RLPPRIPPGF PPRFPPRFPG KR
