ID   DEFB1_NOMCO             Reviewed;          68 AA.
AC   Q7JGM2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Beta-defensin 1;
DE            Short=BD-1;
DE   AltName: Full=Defensin, beta 1;
DE   Flags: Precursor;
GN   Name=DEFB1;
OS   Nomascus concolor (Black crested gibbon) (Hylobates concolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=29089;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11862391; DOI=10.1007/s00251-001-0412-x;
RA   Del Pero M., Boniotto M., Zuccon D., Cervella P., Spano A., Amoroso A.,
RA   Crovella S.;
RT   "Beta-defensin 1 gene variability among non-human primates.";
RL   Immunogenetics 53:907-913(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY033752; AAK61464.1; -; Genomic_DNA.
DR   EMBL; AY033737; AAK61464.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q7JGM2; -.
DR   SMR; Q7JGM2; -.
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   Pfam; PF00711; Defensin_beta; 1.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Defensin; Disulfide bond; Membrane; Secreted;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..32
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000006901"
FT   PEPTIDE         33..68
FT                   /note="Beta-defensin 1"
FT                   /id="PRO_0000006902"
FT   DISULFID        37..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..59
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..67
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   68 AA;  7535 MW;  B47336DEC3B05C74 CRC64;
     MRTSYLLLFT LCLLLSEMAS GDNFLTGLGH RSDHYNCVRS GGQCLYSACP IYTKIQGTCY
     QGKAKCCK