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DEFB1_CHILA
ID   DEFB1_CHILA             Reviewed;          67 AA.
AC   P83943;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Beta-defensin 1;
DE            Short=BD-1;
DE   AltName: Full=Defensin, beta 1;
DE   AltName: Full=cBD-1;
DE   Flags: Precursor;
GN   Name=DEFB1;
OS   Chinchilla lanigera (Long-tailed chinchilla) (Chinchilla villidera).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha;
OC   Chinchillidae; Chinchilla.
OX   NCBI_TaxID=34839 {ECO:0000312|EMBL:AAM97293.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Tongue {ECO:0000269|PubMed:14996845}, and
RC   Trachea {ECO:0000269|PubMed:14996845};
RX   PubMed=14996845; DOI=10.1074/jbc.m400499200;
RA   Harris R.H., Wilk D., Bevins C.L., Munson R.S. Jr., Bakaletz L.O.;
RT   "Identification and characterization of mucosal antimicrobial peptides
RT   expressed by the chinchilla (Chinchilla lanigera) airway.";
RL   J. Biol. Chem. 279:20250-20256(2004).
CC   -!- FUNCTION: Has antibacterial activity against Gram-positive bacterium
CC       S.pneumoniae Serotype 14. Is also active against Gram-negative bacteria
CC       M.catarrhalis 1857, and non-typeable H.influenzae strains 86-028NP and
CC       1128. Has antifungal activity against C.albicans. May have a role in
CC       maintaining sterility in the middle ear (PubMed:14996845). May act as a
CC       ligand for C-C chemokine receptor CCR6. Positively regulates the sperm
CC       motility and bactericidal activity in a CCR6-dependent manner. Binds to
CC       CCR6 and triggers Ca2+ mobilization in the sperm which is important for
CC       its motility (By similarity). {ECO:0000250|UniProtKB:P60022,
CC       ECO:0000269|PubMed:14996845}.
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: Highly expressed in tongue, nasopharyngeal mucosa
CC       and skin, and to a lower extent in the Eustachian tube, lung and
CC       trachea. {ECO:0000269|PubMed:14996845}.
CC   -!- MASS SPECTROMETRY: Mass=5123; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:14996845};
CC   -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR   EMBL; AY128668; AAM97293.1; -; mRNA.
DR   RefSeq; XP_005373890.1; XM_005373833.2.
DR   AlphaFoldDB; P83943; -.
DR   SMR; P83943; -.
DR   Ensembl; ENSCLAT00000023558; ENSCLAP00000023337; ENSCLAG00000016003.
DR   GeneID; 102004444; -.
DR   GeneTree; ENSGT00530000064280; -.
DR   OMA; EQIGHCS; -.
DR   OrthoDB; 1630404at2759; -.
DR   Proteomes; UP000694398; Unassembled WGS sequence.
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; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
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:0051873; P:killing by host of symbiont cells; IDA:CACAO.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Defensin; Disulfide bond; Fungicide; Membrane;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         23..67
FT                   /note="Beta-defensin 1"
FT                   /id="PRO_0000006896"
FT   DISULFID        33..62
FT                   /evidence="ECO:0000250|UniProtKB:P81534"
FT   DISULFID        40..55
FT                   /evidence="ECO:0000250|UniProtKB:P81534"
FT   DISULFID        45..63
FT                   /evidence="ECO:0000250|UniProtKB:P81534"
SQ   SEQUENCE   67 AA;  7676 MW;  30A611CDCCD5BA8D CRC64;
     MRIHYLLFAV LFLFLMPVPG EGGIINTIQR YFCRVRGGRC AALTCLPRET QIGRCSVKGR
     KCCRTRK
 
 
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