DB126_PANTR
ID DB126_PANTR Reviewed; 108 AA.
AC Q30KK2; A4H242;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Beta-defensin 126;
DE AltName: Full=Defensin, beta 126;
DE Flags: Precursor;
GN Name=DEFB126;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16033865; DOI=10.1152/physiolgenomics.00104.2005;
RA Patil A.A., Cai Y., Sang Y., Blecha F., Zhang G.;
RT "Cross-species analysis of the mammalian beta-defensin gene family:
RT presence of syntenic gene clusters and preferential expression in the male
RT reproductive tract.";
RL Physiol. Genomics 23:5-17(2005).
RN [2]
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}.
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; DQ012078; AAY59808.1; -; mRNA.
DR EMBL; AM410147; CAL68957.1; -; Genomic_DNA.
DR RefSeq; NP_001123243.1; NM_001129771.1.
DR AlphaFoldDB; Q30KK2; -.
DR STRING; 9598.ENSPTRP00000022490; -.
DR PaxDb; Q30KK2; -.
DR GeneID; 458023; -.
DR KEGG; ptr:458023; -.
DR CTD; 81623; -.
DR eggNOG; ENOG502TDX7; Eukaryota.
DR InParanoid; Q30KK2; -.
DR OrthoDB; 1608276at2759; -.
DR Proteomes; UP000002277; 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..108
FT /note="Beta-defensin 126"
FT /id="PRO_0000436302"
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"
FT CONFLICT 86
FT /note="K -> R (in Ref. 1; AAY59808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 108 AA; 11768 MW; 765C5D748C1636FD CRC64;
MKSLLFTLAV FMLLAQLVSG NWYVKKCLND VGICKKKCKP GEMHIKNGWA TCGKQRDCCV
PADRRANYPA FCVQTKTTRT STVTAKTTLM VTTASMSSMA PTPVSPTG
