DFB12_BOVIN
ID DFB12_BOVIN Reviewed; 38 AA.
AC P46170;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Beta-defensin 12;
DE AltName: Full=BNBD-12;
DE AltName: Full=BNDB-12;
GN Name=DEFB12;
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 PROTEIN SEQUENCE.
RC STRAIN=Hereford; TISSUE=Neutrophil;
RX PubMed=8454635; DOI=10.1016/s0021-9258(18)53298-1;
RA Selsted M.E., Tang Y.-Q., Morris W.L., McGuire P.A., Novotny M.J.,
RA Smith W., Henschen A.H., Cullor J.S.;
RT "Purification, primary structures, and antibacterial activities of beta-
RT defensins, a new family of antimicrobial peptides from bovine
RT neutrophils.";
RL J. Biol. Chem. 268:6641-6648(1993).
RN [2]
RP DISULFIDE BONDS.
RX PubMed=8454636; DOI=10.1016/s0021-9258(18)53299-3;
RA Tang Y.-Q., Selsted M.E.;
RT "Characterization of the disulfide motif in BNBD-12, an antimicrobial beta-
RT defensin peptide from bovine neutrophils.";
RL J. Biol. Chem. 268:6649-6653(1993).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=7577957; DOI=10.1021/bi00041a048;
RA Zimmermann G.R., Legault P., Selsted M.E., Pardi A.;
RT "Solution structure of bovine neutrophil beta-defensin-12: the peptide fold
RT of the beta-defensins is identical to that of the classical defensins.";
RL Biochemistry 34:13663-13671(1995).
CC -!- FUNCTION: Has bactericidal activity. Active against E.coli ML35 and
CC S.aureus 502A.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Neutrophilic granules.
CC -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR PDB; 1BNB; NMR; -; A=2-38.
DR PDBsum; 1BNB; -.
DR AlphaFoldDB; P46170; -.
DR SMR; P46170; -.
DR PRIDE; P46170; -.
DR InParanoid; P46170; -.
DR EvolutionaryTrace; P46170; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042581; C:specific granule; IDA:CAFA.
DR GO; GO:0031731; F:CCR6 chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0042056; F:chemoattractant activity; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR InterPro; IPR001855; Defensin_beta-typ.
DR InterPro; IPR006080; Defensin_beta/alpha.
DR Pfam; PF00711; Defensin_beta; 1.
DR SMART; SM00048; DEFSN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Defensin;
KW Direct protein sequencing; Disulfide bond; Reference proteome; Secreted.
FT PEPTIDE 1..38
FT /note="Beta-defensin 12"
FT /id="PRO_0000044727"
FT DISULFID 5..34
FT /evidence="ECO:0000269|PubMed:8454636"
FT DISULFID 12..27
FT /evidence="ECO:0000269|PubMed:8454636"
FT DISULFID 17..35
FT /evidence="ECO:0000269|PubMed:8454636"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:1BNB"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:1BNB"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:1BNB"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:1BNB"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1BNB"
SQ SEQUENCE 38 AA; 4106 MW; FD0710704504E3E7 CRC64;
GPLSCGRNGG VCIPIRCPVP MRQIGTCFGR PVKCCRSW
