ID   CTHL3_BOVIN             Reviewed;         190 AA.
AC   P19661; A5PJ95;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Cathelicidin-3;
DE   AltName: Full=Bactenecin-7;
DE            Short=Bac7;
DE   AltName: Full=PR-59;
DE   Flags: Precursor;
GN   Name=CATHL3; Synonyms=BAC7;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=7925973; DOI=10.1016/0014-5793(94)00954-6;
RA   Scocchi M., Romeo D., Zanetti M.;
RT   "Molecular cloning of Bac7, a proline- and arginine-rich antimicrobial
RT   peptide from bovine neutrophils.";
RL   FEBS Lett. 352:197-200(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RA   Scocchi M., Wang S., Zanetti M.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 131-189, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Neutrophil;
RX   PubMed=2229048; DOI=10.1016/s0021-9258(17)30595-1;
RA   Frank R.W., Gennaro R., Schneider K., Przybylski M., Romeo D.;
RT   "Amino acid sequences of two proline-rich bactenecins. Antimicrobial
RT   peptides of bovine neutrophils.";
RL   J. Biol. Chem. 265:18871-18874(1990).
RN   [5]
RP   CHARACTERIZATION, AND PYROGLUTAMATE FORMATION AT GLN-30.
RX   PubMed=8706679; DOI=10.1111/j.1432-1033.1996.0769w.x;
RA   Storici P., Tossi A., Lenarcic B., Romeo D.;
RT   "Purification and structural characterization of bovine cathelicidins,
RT   precursors of antimicrobial peptides.";
RL   Eur. J. Biochem. 238:769-776(1996).
CC   -!- FUNCTION: Exerts, in vitro, a potent antimicrobial activity. Probably
CC       due to an impairment of the function of the respiratory chain and of
CC       energy-dependent activities in the inner membrane of susceptible
CC       microorganisms.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Large granules of neutrophils.
CC   -!- PTM: Elastase is responsible for its maturation.
CC   -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR   EMBL; L42977; AAA87359.1; -; mRNA.
DR   EMBL; Y09471; CAA70616.1; -; Genomic_DNA.
DR   EMBL; BC134776; AAI34777.1; -; mRNA.
DR   EMBL; BC142014; AAI42015.1; -; mRNA.
DR   PIR; A36589; A36589.
DR   RefSeq; NP_776426.1; NM_174001.2.
DR   PDB; 4JWC; X-ray; 1.80 A; C/D=131-146.
DR   PDB; 4JWD; X-ray; 1.95 A; C/D=173-186.
DR   PDB; 5F8K; X-ray; 2.80 A; 1y/2y=131-146.
DR   PDB; 5HAU; X-ray; 3.00 A; 1x/2x=131-165.
DR   PDBsum; 4JWC; -.
DR   PDBsum; 4JWD; -.
DR   PDBsum; 5F8K; -.
DR   PDBsum; 5HAU; -.
DR   AlphaFoldDB; P19661; -.
DR   SMR; P19661; -.
DR   STRING; 9913.ENSBTAP00000034498; -.
DR   PaxDb; P19661; -.
DR   PeptideAtlas; P19661; -.
DR   PRIDE; P19661; -.
DR   Ensembl; ENSBTAT00000034610; ENSBTAP00000034498; ENSBTAG00000013356.
DR   GeneID; 281037; -.
DR   KEGG; bta:281037; -.
DR   CTD; 281037; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013356; -.
DR   eggNOG; ENOG502SAES; Eukaryota.
DR   GeneTree; ENSGT00390000000410; -.
DR   HOGENOM; CLU_121724_0_0_1; -.
DR   InParanoid; P19661; -.
DR   OrthoDB; 1534863at2759; -.
DR   TreeFam; TF338457; -.
DR   Proteomes; UP000009136; Chromosome 22.
DR   Bgee; ENSBTAG00000013356; Expressed in thymus and 51 other tissues.
DR   ExpressionAtlas; P19661; differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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; Antibiotic; Antimicrobial; Direct protein sequencing;
KW   Disulfide bond; Pyrrolidone carboxylic acid; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..130
FT                   /evidence="ECO:0000269|PubMed:2229048"
FT                   /id="PRO_0000004709"
FT   PEPTIDE         131..189
FT                   /note="Cathelicidin-3"
FT                   /id="PRO_0000004710"
FT   PROPEP          190
FT                   /note="Removed; partial"
FT                   /id="PRO_0000004711"
FT   REGION          133..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..190
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         30
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:8706679"
FT   DISULFID        85..96
FT   DISULFID        107..124
SQ   SEQUENCE   190 AA;  21567 MW;  8CD07D7AA30A731C CRC64;
     METQRASLSL GRWSLWLLLL GLVLPSASAQ ALSYREAVLR AVDRINERSS EANLYRLLEL
     DPPPKDVEDR GARKPTSFTV KETVCPRTSP QPPEQCDFKE NGLVKQCVGT ITLDQSDDLF
     DLNCNELQSV RRIRPRPPRL PRPRPRPLPF PRPGPRPIPR PLPFPRPGPR PIPRPLPFPR
     PGPRPIPRPL