CTHL4_BOVIN
ID CTHL4_BOVIN Reviewed; 144 AA.
AC P33046; A3KN14;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Cathelicidin-4;
DE AltName: Full=Indolicidin;
DE Flags: Precursor;
GN Name=CATHL4;
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=1520337; DOI=10.1016/s0006-291x(05)81517-7;
RA del Sal G., Storici P., Schneider C., Romeo D., Zanetti M.;
RT "cDNA cloning of the neutrophil bactericidal peptide indolicidin.";
RL Biochem. Biophys. Res. Commun. 187:467-472(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 131-143, AND AMIDATION AT ARG-143.
RC TISSUE=Neutrophil;
RX PubMed=1537821; DOI=10.1016/s0021-9258(18)42830-x;
RA Selsted M.E., Novotny M.J., Morris W.L., Tang Y.-Q., Smith W., Cullor J.S.;
RT "Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils.";
RL J. Biol. Chem. 267:4292-4295(1992).
RN [4]
RP ANTIFUNGAL ACTIVITY.
RX PubMed=12745074; DOI=10.1016/s0006-291x(03)00755-1;
RA Lee D.G., Kim H.K., Kim S.A., Park Y., Park S.C., Jang S.H., Hahm K.S.;
RT "Fungicidal effect of indolicidin and its interaction with phospholipid
RT membranes.";
RL Biochem. Biophys. Res. Commun. 305:305-310(2003).
RN [5]
RP STRUCTURE BY NMR OF 131-144.
RX PubMed=11123901; DOI=10.1021/bi000714m;
RA Rozek A., Friedrich C.L., Hancock R.E.;
RT "Structure of the bovine antimicrobial peptide indolicidin bound to
RT dodecylphosphocholine and sodium dodecyl sulfate micelles.";
RL Biochemistry 39:15765-15774(2000).
CC -!- FUNCTION: Potent microbicidal activity; active against S.aureus and
CC E.coli.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Large granules of neutrophils.
CC -!- PTM: Elastase might be responsible for its maturation.
CC -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR EMBL; X67340; CAA47755.1; -; mRNA.
DR EMBL; BC133480; AAI33481.1; -; mRNA.
DR PIR; JC1222; JC1222.
DR RefSeq; NP_777252.1; NM_174827.2.
DR PDB; 1G89; NMR; -; A=131-143.
DR PDB; 1G8C; NMR; -; A=131-143.
DR PDB; 1HR1; NMR; -; A=131-143.
DR PDB; 1QX9; NMR; -; A=132-144.
DR PDB; 1QXQ; NMR; -; A=134-144.
DR PDB; 5ZVF; NMR; -; A=131-143.
DR PDB; 5ZVN; NMR; -; A=131-143.
DR PDBsum; 1G89; -.
DR PDBsum; 1G8C; -.
DR PDBsum; 1HR1; -.
DR PDBsum; 1QX9; -.
DR PDBsum; 1QXQ; -.
DR PDBsum; 5ZVF; -.
DR PDBsum; 5ZVN; -.
DR AlphaFoldDB; P33046; -.
DR SMR; P33046; -.
DR STRING; 9913.ENSBTAP00000026747; -.
DR TCDB; 1.C.33.1.2; the cathelicidin (cathelicidin) family.
DR PaxDb; P33046; -.
DR PeptideAtlas; P33046; -.
DR PRIDE; P33046; -.
DR Ensembl; ENSBTAT00000026747; ENSBTAP00000026747; ENSBTAG00000052903.
DR Ensembl; ENSBTAT00000044788; ENSBTAP00000042250; ENSBTAG00000053016.
DR GeneID; 282166; -.
DR KEGG; bta:282166; -.
DR CTD; 282166; -.
DR VEuPathDB; HostDB:ENSBTAG00000052903; -.
DR VEuPathDB; HostDB:ENSBTAG00000053016; -.
DR eggNOG; ENOG502SAES; Eukaryota.
DR GeneTree; ENSGT00390000000410; -.
DR HOGENOM; CLU_121724_1_1_1; -.
DR InParanoid; P33046; -.
DR OMA; GNFFRKA; -.
DR OrthoDB; 1534863at2759; -.
DR TreeFam; TF338457; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-6803157; Antimicrobial peptides.
DR EvolutionaryTrace; P33046; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000052903; Expressed in caput epididymis and 23 other tissues.
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; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
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 GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
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; Fungicide; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..130
FT /evidence="ECO:0000269|PubMed:1537821"
FT /id="PRO_0000004720"
FT PEPTIDE 131..143
FT /note="Cathelicidin-4"
FT /id="PRO_0000004721"
FT MOD_RES 143
FT /note="Arginine amide"
FT /evidence="ECO:0000269|PubMed:1537821"
FT DISULFID 85..96
FT /evidence="ECO:0000250"
FT DISULFID 107..124
FT /evidence="ECO:0000250"
FT HELIX 135..142
FT /evidence="ECO:0007829|PDB:1HR1"
SQ SEQUENCE 144 AA; 16479 MW; E3B1CBBE55C09911 CRC64;
MQTQRASLSL GRWSLWLLLL GLVVPSASAQ ALSYREAVLR AVDQLNELSS EANLYRLLEL
DPPPKDNEDL GTRKPVSFTV KETVCPRTIQ QPAEQCDFKE KGRVKQCVGT VTLDPSNDQF
DLNCNELQSV ILPWKWPWWP WRRG
