DEFB1_BOVIN
ID DEFB1_BOVIN Reviewed; 38 AA.
AC P46159;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Beta-defensin 1;
DE AltName: Full=BNBD-1;
DE AltName: Full=BNDB-1;
GN Name=DEFB1;
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, AND FUNCTION.
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).
CC -!- FUNCTION: Has bactericidal activity. Active against E.coli ML35 but not
CC against S.aureus 502A (PubMed:8454635). May act as a ligand for C-C
CC chemokine receptor CCR6. Positively regulates the sperm motility and
CC bactericidal activity in a CCR6-dependent manner. Binds to CCR6 and
CC triggers Ca2+ mobilization in the sperm which is important for its
CC motility (By similarity). {ECO:0000250|UniProtKB:P60022,
CC ECO:0000269|PubMed:8454635}.
CC -!- SUBUNIT: Monomer. Homodimer. {ECO:0000250|UniProtKB:P60022}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P60022}. Membrane
CC {ECO:0000250|UniProtKB:P60022}. Note=Associates with tumor cell
CC membrane-derived microvesicles. {ECO:0000250|UniProtKB:P60022}.
CC -!- TISSUE SPECIFICITY: Neutrophilic granules.
CC -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR PIR; A45495; A45495.
DR AlphaFoldDB; P46159; -.
DR SMR; P46159; -.
DR STRING; 9913.ENSBTAP00000049375; -.
DR PaxDb; P46159; -.
DR HOGENOM; CLU_189296_4_1_1; -.
DR InParanoid; P46159; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:1990742; C:microvesicle; ISS:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR GO; GO:0031731; F:CCR6 chemokine receptor binding; ISS:UniProtKB.
DR GO; GO:0042056; F:chemoattractant activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS:UniProtKB.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0060474; P:positive regulation of flagellated sperm motility involved in capacitation; ISS:UniProtKB.
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 Antibiotic; Antimicrobial; Defensin; Direct protein sequencing;
KW Disulfide bond; Membrane; Reference proteome; Secreted.
FT PEPTIDE 1..38
FT /note="Beta-defensin 1"
FT /id="PRO_0000044721"
FT DISULFID 5..34
FT /evidence="ECO:0000250"
FT DISULFID 12..27
FT /evidence="ECO:0000250"
FT DISULFID 17..35
FT /evidence="ECO:0000250"
SQ SEQUENCE 38 AA; 4278 MW; 48B872D1025E1A68 CRC64;
DFASCHTNGG ICLPNRCPGH MIQIGICFRP RVKCCRSW
