CTHL2_BOVIN
ID CTHL2_BOVIN Reviewed; 176 AA.
AC P19660; B9TUB9; Q0P560;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cathelicidin-2;
DE AltName: Full=Bactenecin-5;
DE Short=Bac5;
DE AltName: Full=PR-42;
DE Flags: Precursor;
GN Name=CATHL2; Synonyms=BAC5;
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=Neutrophil;
RX PubMed=8416958; DOI=10.1016/s0021-9258(18)54182-x;
RA Zanetti M., del Sal G., Storici P., Schneider C., Romeo D.;
RT "The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence
RT homologous to a cysteine proteinase inhibitor that is common to other
RT neutrophil antibiotics.";
RL J. Biol. Chem. 268:522-526(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-159.
RC STRAIN=Isolate 44N, Isolate 74S, Isolate 80U, and Isolate JEW38;
RX PubMed=19136450; DOI=10.1093/jhered/esn112;
RA Gillenwaters E.N., Seabury C.M., Elliott J.S., Womack J.E.;
RT "Sequence analysis and polymorphism discovery in 4 members of the bovine
RT cathelicidin gene family.";
RL J. Hered. 100:241-245(2009).
RN [4]
RP PROTEIN SEQUENCE OF 131-173, 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 STRUCTURE BY NMR OF 131-173, AND AMIDATION AT PRO-173.
RX PubMed=8605180; DOI=10.1021/bi951681r;
RA Raj P.A., Marcus E., Edgerton M.;
RT "Delineation of an active fragment and poly(L-proline) II conformation for
RT candidacidal activity of bactenecin 5.";
RL Biochemistry 35:4314-4325(1996).
RN [6]
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 -!- DOMAIN: BAC5 sequence consists almost exclusively of X-P-P-Y repeats.
CC -!- PTM: Elastase is responsible for its maturation.
CC -!- SIMILARITY: Belongs to the cathelicidin family. {ECO:0000305}.
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DR EMBL; L02650; AAA30404.1; -; mRNA.
DR EMBL; EU380691; ACC61269.1; -; Genomic_DNA.
DR EMBL; EU380692; ACC61270.1; -; Genomic_DNA.
DR EMBL; EU380693; ACC61271.1; -; Genomic_DNA.
DR EMBL; EU380697; ACC61275.1; -; Genomic_DNA.
DR EMBL; BC120477; AAI20478.1; -; mRNA.
DR PIR; A45328; A45328.
DR RefSeq; NP_777251.1; NM_174826.3.
DR AlphaFoldDB; P19660; -.
DR SMR; P19660; -.
DR STRING; 9913.ENSBTAP00000034497; -.
DR PaxDb; P19660; -.
DR PeptideAtlas; P19660; -.
DR PRIDE; P19660; -.
DR Ensembl; ENSBTAT00000034609; ENSBTAP00000034497; ENSBTAG00000024852.
DR GeneID; 282165; -.
DR KEGG; bta:282165; -.
DR CTD; 282165; -.
DR VEuPathDB; HostDB:ENSBTAG00000024852; -.
DR eggNOG; ENOG502SAES; Eukaryota.
DR GeneTree; ENSGT00390000000410; -.
DR HOGENOM; CLU_121724_0_0_1; -.
DR InParanoid; P19660; -.
DR OrthoDB; 1534863at2759; -.
DR TreeFam; TF338457; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000024852; Expressed in thymus and 35 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; 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 Amidation; 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_0000004700"
FT PEPTIDE 131..173
FT /note="Cathelicidin-2"
FT /id="PRO_0000004701"
FT PROPEP 174..176
FT /note="Removed in mature form"
FT /id="PRO_0000004702"
FT REGION 157..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:8706679"
FT MOD_RES 173
FT /note="Proline amide"
FT /evidence="ECO:0000269|PubMed:8605180"
FT DISULFID 85..96
FT /evidence="ECO:0000250"
FT DISULFID 107..124
FT /evidence="ECO:0000250"
FT CONFLICT 170..171
FT /note="GP -> R (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 20030 MW; D2D1881C05929415 CRC64;
METQRASLSL GRCSLWLLLL GLVLPSASAQ ALSYREAVLR AVDQFNERSS EANLYRLLEL
DPTPNDDLDP GTRKPVSFRV KETDCPRTSQ QPLEQCDFKE NGLVKQCVGT VTLDPSNDQF
DINCNELQSV RFRPPIRRPP IRPPFYPPFR PPIRPPIFPP IRPPFRPPLG PFPGRR
