DEFB1_SHEEP
ID DEFB1_SHEEP Reviewed; 64 AA.
AC O19038;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Beta-defensin 1;
DE Short=BD-1;
DE AltName: Full=sBD1;
DE Flags: Precursor;
GN Name=DEFB1;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9478010; DOI=10.1093/jn/128.2.297s;
RA Huttner K.M., Brezinski-Caliguri D.J., Mahoney M.M., Diamond G.;
RT "Antimicrobial peptide expression is developmentally regulated in the ovine
RT gastrointestinal tract.";
RL J. Nutr. 128:297S-299S(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Trachea;
RX PubMed=9461419; DOI=10.1016/s0378-1119(97)00569-6;
RA Huttner K.M., Lambeth M.R., Burkin H.R., Broad T.E.;
RT "Localization and genomic organization of sheep antimicrobial peptides
RT genes.";
RL Gene 206:85-91(1998).
CC -!- FUNCTION: Has bactericidal activity. 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. {ECO:0000250|UniProtKB:P60022}.
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 -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR EMBL; U75250; AAB61995.1; -; Genomic_DNA.
DR AlphaFoldDB; O19038; -.
DR SMR; O19038; -.
DR STRING; 9940.ENSOARP00000006815; -.
DR Ensembl; ENSOART00000006919; ENSOARP00000006815; ENSOARG00000006364.
DR eggNOG; ENOG502SYUI; Eukaryota.
DR HOGENOM; CLU_189296_4_1_1; -.
DR OMA; SCHRNKG; -.
DR Proteomes; UP000002356; Chromosome 26.
DR Bgee; ENSOARG00000006364; Expressed in rectum and 48 other tissues.
DR ExpressionAtlas; O19038; baseline and differential.
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: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: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 3: Inferred from homology;
KW Antibiotic; Antimicrobial; Defensin; Disulfide bond; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT PEPTIDE 23..64
FT /note="Beta-defensin 1"
FT /id="PRO_0000006963"
FT DISULFID 31..60
FT /evidence="ECO:0000250"
FT DISULFID 38..53
FT /evidence="ECO:0000250"
FT DISULFID 43..61
FT /evidence="ECO:0000250"
SQ SEQUENCE 64 AA; 7244 MW; 3529A9B76ABD023A CRC64;
MRLHHLLLVL FFVVLSAGSG FTQGVRNRLS CHRNKGVCVP SRCPRHMRQI GTCRGPPVKC
CRKK
