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Protein

Beta-defensin 126

Gene

DEFB126

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Highly glycosylated atypical beta-defensin involved in several aspects of sperm function. Facilitates sperm transport in the female reproductive tract and contributes to sperm protection against immunodetection; both functions are probably implicating the negative surface charge provided by its O-linked oligosaccharides in the sperm glycocalyx. Involved in binding of sperm to oviductal epithelial cells to form a sperm reservoir until ovulation. Release from the sperm surface during capacitation and ovaluation by an elevation of oviductal fluid pH is unmasking other surface components and allows sperm to penetrate the cumulus matrix and bind to the zona pellucida of the oocyte (By similarity). In vitro has antimicrobial activity and may inhibit LPS-mediated inflammation (PubMed:19373462, PubMed:23229569).By similarity2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Defensin

Keywords - Biological processi

Fertilization

Enzyme and pathway databases

ReactomeiR-HSA-1461957. Beta defensins.
R-HSA-1461973. Defensins.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-defensin 126
Alternative name(s):
Beta-defensin 26
Short name:
DEFB-26
Defensin, beta 126
Epididymal secretory protein 13.2
Short name:
ESP13.2
HBD261 Publication
Gene namesi
Name:DEFB126
Synonyms:C20orf8, DEFB26
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15900. DEFB126.

Subcellular locationi

  • Secreted Curated

  • Note: Secreted by epididymal cells and is absorbed to the surface of sperm during transit through the epididymis (By similarity). Mainly located on the sperm acrosome.By similarity1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

May be involved in infertility. Homozygosity for frameshift truncating mutations are associated with reduced sperm O-linked glycan content, impaired sperm mobility and a reduced live birth rate (PubMed:21775668, PubMed:25721098). However, for one common mutation the change in sperm sialic acid levels has been challenged (PubMed:26832966).

Organism-specific databases

PharmGKBiPA27246.

Polymorphism and mutation databases

BioMutaiDEFB126.
DMDMi61252638.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 11191Beta-defensin 126PRO_0000436299Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 58By similarity
Disulfide bondi34 ↔ 52By similarity
Disulfide bondi38 ↔ 59By similarity
Disulfide bondi72 – 72InterchainBy similarity

Post-translational modificationi

O-glycosylated; glycans contain alpha(2,3)-linked sialic acids.1 Publication1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbiQ9BYW3.
PRIDEiQ9BYW3.

Expressioni

Tissue specificityi

High-level and epididymis-specific expression. Expression is down-regulated in infertile men.1 Publication

Gene expression databases

BgeeiQ9BYW3.
CleanExiHS_DEFB126.
GenevisibleiQ9BYW3. HS.

Interactioni

Subunit structurei

Homodimer or homooligomer; disulfide-linked.By similarityCurated

Protein-protein interaction databases

STRINGi9606.ENSP00000371835.

Structurei

3D structure databases

ProteinModelPortaliQ9BYW3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 6343In vitro binds to LPS, mediates antimicrobial activity and inhibits LPS-mediated inflammation1 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the beta-defensin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J7HN. Eukaryota.
ENOG4111ED2. LUCA.
GeneTreeiENSGT00390000012226.
HOGENOMiHOG000112158.
HOVERGENiHBG051309.
InParanoidiQ9BYW3.
OMAiICKKKCK.
OrthoDBiEOG7Z69FT.
PhylomeDBiQ9BYW3.

Family and domain databases

InterProiIPR025933. Beta_defensin.
IPR020329. Beta_defensin_126.
[Graphical view]
PfamiPF13841. Defensin_beta_2. 1 hit.
[Graphical view]
ProDomiPD289049. Beta_defensin_126. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9BYW3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSLLFTLAV FMLLAQLVSG NWYVKKCLND VGICKKKCKP EEMHVKNGWA
60 70 80 90 100
MCGKQRDCCV PADRRANYPV FCVQTKTTRI STVTATTATT TLMMTTASMS
110
SMAPTPVSPT G
Length:111
Mass (Da):12,174
Last modified:March 15, 2005 - v2
Checksum:i956E77CB6812A32D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31S → F in CAC27121 (PubMed:10491631).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ236910 mRNA. Translation: CAC27121.1.
AF525928 mRNA. Translation: AAP47221.1.
AL360078 Genomic DNA. Translation: CAC17684.1.
AY122478 mRNA. Translation: AAM93919.1.
CCDSiCCDS12990.1.
RefSeqiNP_112193.1. NM_030931.3.
UniGeneiHs.124211.

Genome annotation databases

EnsembliENST00000382398; ENSP00000371835; ENSG00000125788.
GeneIDi81623.
KEGGihsa:81623.
UCSCiuc002wcx.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ236910 mRNA. Translation: CAC27121.1.
AF525928 mRNA. Translation: AAP47221.1.
AL360078 Genomic DNA. Translation: CAC17684.1.
AY122478 mRNA. Translation: AAM93919.1.
CCDSiCCDS12990.1.
RefSeqiNP_112193.1. NM_030931.3.
UniGeneiHs.124211.

3D structure databases

ProteinModelPortaliQ9BYW3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000371835.

Polymorphism and mutation databases

BioMutaiDEFB126.
DMDMi61252638.

Proteomic databases

PaxDbiQ9BYW3.
PRIDEiQ9BYW3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000382398; ENSP00000371835; ENSG00000125788.
GeneIDi81623.
KEGGihsa:81623.
UCSCiuc002wcx.5. human.

Organism-specific databases

CTDi81623.
GeneCardsiDEFB126.
HGNCiHGNC:15900. DEFB126.
neXtProtiNX_Q9BYW3.
PharmGKBiPA27246.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J7HN. Eukaryota.
ENOG4111ED2. LUCA.
GeneTreeiENSGT00390000012226.
HOGENOMiHOG000112158.
HOVERGENiHBG051309.
InParanoidiQ9BYW3.
OMAiICKKKCK.
OrthoDBiEOG7Z69FT.
PhylomeDBiQ9BYW3.

Enzyme and pathway databases

ReactomeiR-HSA-1461957. Beta defensins.
R-HSA-1461973. Defensins.

Miscellaneous databases

GeneWikiiDEFB126.
GenomeRNAii81623.
PROiQ9BYW3.

Gene expression databases

BgeeiQ9BYW3.
CleanExiHS_DEFB126.
GenevisibleiQ9BYW3. HS.

Family and domain databases

InterProiIPR025933. Beta_defensin.
IPR020329. Beta_defensin_126.
[Graphical view]
PfamiPF13841. Defensin_beta_2. 1 hit.
[Graphical view]
ProDomiPD289049. Beta_defensin_126. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The novel epididymal secretory protein ESP13.2 in Macaca fascicularis."
    Perry A.C.F., Jones R., Moisyadi S., Coadwell W.J., Hall L.
    Biol. Reprod. 61:965-972(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Epididymis.
  2. "Distribution of new human beta-defensin genes clustered on chromosome 20 in functionally different segments of epididymis."
    Rodriguez-Jimenez F.-J., Krause A., Schulz S., Forssmann W.-G., Conejo-Garcia J.-R., Schreeb R., Motzkus D.
    Genomics 81:175-183(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Discovery of five conserved beta-defensin gene clusters using a computational search strategy."
    Schutte B.C., Mitros J.P., Bartlett J.A., Walters J.D., Jia H.P., Welsh M.J., Casavant T.L., McCray P.B. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 99:2129-2133(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-96, IDENTIFICATION.
    Tissue: Testis.
  5. "Alterations in gene expression in the caput epididymides of nonobstructive azoospermic men."
    Dube E., Hermo L., Chan P.T., Cyr D.G.
    Biol. Reprod. 78:342-351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Soluble fusion expression and characterization of bioactive human beta-defensin 26 and 27."
    Huang L., Leong S.S., Jiang R.
    Appl. Microbiol. Biotechnol. 84:301-308(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "A common mutation in the defensin DEFB126 causes impaired sperm function and subfertility."
    Tollner T.L., Venners S.A., Hollox E.J., Yudin A.I., Liu X., Tang G., Xing H., Kays R.J., Lau T., Overstreet J.W., Xu X., Bevins C.L., Cherr G.N.
    Sci. Transl. Med. 3:92RA65-92RA65(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN INFERTILITY, GLYCOSYLATION.
  8. "Human beta-defensin DEFB126 is capable of inhibiting LPS-mediated inflammation."
    Liu H., Yu H., Gu Y., Xin A., Zhang Y., Diao H., Lin D.
    Appl. Microbiol. Biotechnol. 97:3395-3408(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Another functional frame-shift polymorphism of DEFB126 (rs11467497) associated with male infertility."
    Duan S., Shi C., Chen G., Zheng J.F., Wu B., Diao H., Ji L., Gu Y., Xin A., Wu Y., Zhou W., Miao M., Xu L., Li Z., Yuan Y., Wang P., Shi H.
    J. Cell. Mol. Med. 19:1077-1084(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN INFERTILITY.
  10. "Lectin binding of human sperm associates with DEFB126 mutation and serves as a potential biomarker for subfertility."
    Xin A., Cheng L., Diao H., Wu Y., Zhou S., Shi C., Sun Y., Wang P., Duan S., Zheng J., Wu B., Yuan Y., Gu Y., Chen G., Sun X., Shi H., Tao S., Zhang Y.
    Sci. Rep. 6:20249-20249(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, POSSIBLE INVOLVEMENT IN INFERTILITY.

Entry informationi

Entry nameiDB126_HUMAN
AccessioniPrimary (citable) accession number: Q9BYW3
Secondary accession number(s): Q562G3, Q9H1M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: March 15, 2005
Last modified: June 8, 2016
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.