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}.
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; 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