DB126_MACFA
ID DB126_MACFA Reviewed; 123 AA.
AC Q9BEE3;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Beta-defensin 126;
DE AltName: Full=Defensin, beta 126;
DE AltName: Full=Epididymal secretory protein 13.2;
DE Short=ESP13.2;
DE Flags: Precursor;
GN Name=DEFB126;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epididymis;
RX PubMed=10491631; DOI=10.1095/biolreprod61.4.965;
RA Perry A.C.F., Jones R., Moisyadi S., Coadwell W.J., Hall L.;
RT "The novel epididymal secretory protein ESP13.2 in Macaca fascicularis.";
RL Biol. Reprod. 61:965-972(1999).
RN [2]
RP PROTEIN SEQUENCE OF 28-35; 45-54 AND 66-76, FUNCTION, SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=12773404; DOI=10.1095/biolreprod.103.016105;
RA Yudin A.I., Tollner T.L., Li M.W., Treece C.A., Overstreet J.W.,
RA Cherr G.N.;
RT "ESP13.2, a member of the beta-defensin family, is a macaque sperm surface-
RT coating protein involved in the capacitation process.";
RL Biol. Reprod. 69:1118-1128(2003).
RN [3]
RP FUNCTION.
RX PubMed=15349845; DOI=10.1002/mrd.20132;
RA Tollner T.L., Yudin A.I., Treece C.A., Overstreet J.W., Cherr G.N.;
RT "Macaque sperm release ESP13.2 and PSP94 during capacitation: the absence
RT of ESP13.2 is linked to sperm-zona recognition and binding.";
RL Mol. Reprod. Dev. 69:325-337(2004).
RN [4]
RP FUNCTION.
RX PubMed=16079310; DOI=10.1095/biolreprod.105.042432;
RA Yudin A.I., Generao S.E., Tollner T.L., Treece C.A., Overstreet J.W.,
RA Cherr G.N.;
RT "Beta-defensin 126 on the cell surface protects sperm from
RT immunorecognition and binding of anti-sperm antibodies.";
RL Biol. Reprod. 73:1243-1252(2005).
RN [5]
RP GLYCOSYLATION.
RX PubMed=16550483; DOI=10.1007/s00232-005-0806-z;
RA Yudin A.I., Treece C.A., Tollner T.L., Overstreet J.W., Cherr G.N.;
RT "The carbohydrate structure of DEFB126, the major component of the
RT cynomolgus Macaque sperm plasma membrane glycocalyx.";
RL J. Membr. Biol. 207:119-129(2005).
RN [6]
RP FUNCTION.
RX PubMed=18003946; DOI=10.1095/biolreprod.107.064071;
RA Tollner T.L., Yudin A.I., Tarantal A.F., Treece C.A., Overstreet J.W.,
RA Cherr G.N.;
RT "Beta-defensin 126 on the surface of macaque sperm mediates attachment of
RT sperm to oviductal epithelia.";
RL Biol. Reprod. 78:400-412(2008).
RN [7]
RP FUNCTION.
RX PubMed=18658160; DOI=10.1093/humrep/den276;
RA Tollner T.L., Yudin A.I., Treece C.A., Overstreet J.W., Cherr G.N.;
RT "Macaque sperm coating protein DEFB126 facilitates sperm penetration of
RT cervical mucus.";
RL Hum. Reprod. 23:2523-2534(2008).
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 (PubMed:16079310, PubMed:18658160). Involved in binding of
CC sperm to oviductal epithelial cells to form a sperm reservoir until
CC ovulation. Release from the sperm surface during capacitation and
CC ovaluation by an elevation of oviductal fluid pH is unmasking other
CC surface components and allows sperm to penetrate the cumulus matrix and
CC bind to the zona pellucida of the oocyte (PubMed:15349845,
CC PubMed:18003946). In vitro has antimicrobial activity and may inhibit
CC LPS-mediated inflammation (By similarity).
CC {ECO:0000250|UniProtKB:Q9BYW3, ECO:0000269|PubMed:15349845,
CC ECO:0000269|PubMed:16079310, ECO:0000269|PubMed:18003946,
CC ECO:0000269|PubMed:18658160, ECO:0000305|PubMed:12773404}.
CC -!- SUBUNIT: Homodimer or homooligomer; disulfide-linked. {ECO:0000305,
CC ECO:0000305|PubMed:12773404}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12773404}.
CC Note=Secreted by epididymal cells and is absorbed to the surface of
CC sperm during transit through the epididymis. Coats the entire surface
CC of ejaculated sperm. {ECO:0000269|PubMed:12773404}.
CC -!- TISSUE SPECIFICITY: High-level and epididymis-specific expression.
CC Detected in epithelial cells lining the efferent ductules, initial
CC segment, and cauda regions of the epididymis, but not on spermatozoa.
CC -!- PTM: O-glycosylated; glycans contain sialic acids alpha(2,3)-linked to
CC galactose and N-acetylgalactosamine. The C-terminal O-glycosylation
CC contributes substantially to the sperm glyocalyx.
CC {ECO:0000269|PubMed:16550483}.
CC -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR EMBL; AJ236909; CAC27133.1; -; mRNA.
DR RefSeq; NP_001274569.1; NM_001287640.1.
DR AlphaFoldDB; Q9BEE3; -.
DR STRING; 9541.XP_005568666.1; -.
DR Ensembl; ENSMFAT00000012405; ENSMFAP00000038151; ENSMFAG00000038448.
DR GeneID; 102132878; -.
DR CTD; 81623; -.
DR VEuPathDB; HostDB:ENSMFAG00000038448; -.
DR eggNOG; ENOG502TDX7; Eukaryota.
DR GeneTree; ENSGT00390000012226; -.
DR OMA; RSEHGWV; -.
DR OrthoDB; 1603425at2759; -.
DR Proteomes; UP000233100; Chromosome 10.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0030414; F:peptidase inhibitor activity; NAS:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IEA:Ensembl.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Defensin;
KW Direct protein sequencing; Disulfide bond; Fertilization;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..123
FT /note="Beta-defensin 126"
FT /id="PRO_0000436301"
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:0000305|PubMed:12773404"
SQ SEQUENCE 123 AA; 13151 MW; 6B0A9408F25700F4 CRC64;
MKSLLFTLAV FMLLAQLVSG NLYVKRCLND IGICKKTCKP EEVRSEHGWV MCGKRKACCV
PADKRSAYPS FCVHSKTTKT STVTARATAT TATTATAATP LMISNGLISL MTTMAATPVS
PTT
