ID   DB126_GORGO             Reviewed;         111 AA.
AC   A4H243;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Beta-defensin 126;
DE   AltName: Full=Defensin, beta 126;
DE   Flags: Precursor;
GN   Name=DEFB126;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hollox E.J., Armour J.A.L.;
RT   "Evolution and sequence variation of human beta-defensin genes.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Highly glycosylated atypical beta-defensin involved in
CC       several aspects of sperm function. Facilitates sperm transport in the
CC       female reproductive tract and contributes to sperm protection against
CC       immunodetection; both functions are probably implicating the negative
CC       surface charge provided by its O-linked oligosaccharides in the sperm
CC       glycocalyx. Involved in binding of sperm to oviductal epithelial cells
CC       to form a sperm reservoir until ovulation. Release from the sperm
CC       surface during capacitation and ovaluation by an elevation of oviductal
CC       fluid pH is unmasking other surface components and allows sperm to
CC       penetrate the cumulus matrix and bind to the zona pellucida of the
CC       oocyte. In vitro has antimicrobial activity and may inhibit LPS-
CC       mediated inflammation (By similarity). {ECO:0000250|UniProtKB:Q9BEE3,
CC       ECO:0000250|UniProtKB:Q9BYW3}.
CC   -!- SUBUNIT: Homodimer or homooligomer; disulfide-linked.
CC       {ECO:0000250|UniProtKB:Q9BEE3}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9BEE3}.
CC       Note=Secreted by epididymal cells and is absorbed to the surface of
CC       sperm during transit through the epididymis.
CC       {ECO:0000250|UniProtKB:Q9BEE3}.
CC   -!- PTM: O-glycosylated; glycans contain alpha(2,3)-linked sialic acids (By
CC       similarity). {ECO:0000250|UniProtKB:Q9BEE3,
CC       ECO:0000250|UniProtKB:Q9BYW3}.
CC   -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR   EMBL; AM410148; CAL68958.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4H243; -.
DR   InParanoid; A4H243; -.
DR   Proteomes; UP000001519; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:InterPro.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   InterPro; IPR025933; Beta_defensin.
DR   Pfam; PF13841; Defensin_beta_2; 1.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Defensin;
KW   Disulfide bond; Fertilization; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..111
FT                   /note="Beta-defensin 126"
FT                   /id="PRO_0000436298"
FT   REGION          21..63
FT                   /note="In vitro binds to LPS, mediates antimicrobial
FT                   activity and inhibits LPS-mediated inflammation"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYW3"
FT   DISULFID        27..58
FT                   /evidence="ECO:0000250|UniProtKB:P59665"
FT   DISULFID        34..52
FT                   /evidence="ECO:0000250|UniProtKB:P59665"
FT   DISULFID        38..59
FT                   /evidence="ECO:0000250|UniProtKB:P59665"
FT   DISULFID        72
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BEE3"
SQ   SEQUENCE   111 AA;  12160 MW;  3B733DE25312A331 CRC64;
     MKSLLFTLAV FMLLAQLVSG NWYVKKCLND VGICKKKCKP EEMHVKNGWA MCGKQRDCCV
     PADRRANYPA FCVQTKTTRT STVTATTATT TLMMTTASMS LMAPTPVSPT G