DB118_HUMAN
ID DB118_HUMAN Reviewed; 123 AA.
AC Q96PH6; Q17RC4; Q8N691; Q9NUH0;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Defensin beta 118 {ECO:0000312|HGNC:HGNC:16196};
DE AltName: Full=Beta-defensin 18 {ECO:0000303|PubMed:11854508};
DE Short=DEFB-18 {ECO:0000303|PubMed:11854508};
DE AltName: Full=Epididymal secretory protein 13.6;
DE Short=ESP13.6;
DE Flags: Precursor;
GN Name=DEFB118; Synonyms=C20orf63, DEFB18, ESC42;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Epididymis;
RX PubMed=11564719; DOI=10.1210/endo.142.10.8422;
RA Liu Q., Hamil K.G., Sivashanmugam P., Grossman G., Soundararajan R.,
RA Rao A.J., Richardson R.T., Zhang Y.-L., O'Rand M.G., Petrusz P.,
RA French F.S., Hall S.H.;
RT "Primate epididymis-specific proteins: characterization of ESC42, a novel
RT protein containing a trefoil-like motif in monkey and human.";
RL Endocrinology 142:4529-4539(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12600824; DOI=10.1165/rcmb.2002-0205oc;
RA Kao C.Y., Chen Y., Zhao Y.H., Wu R.;
RT "ORFeome-based search of airway epithelial cell-specific novel human beta-
RT defensin genes.";
RL Am. J. Respir. Cell Mol. Biol. 29:71-80(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-123, AND IDENTIFICATION.
RC TISSUE=B-cell, Fetal lung, and Testis;
RX PubMed=11854508; DOI=10.1073/pnas.042692699;
RA Schutte B.C., Mitros J.P., Bartlett J.A., Walters J.D., Jia H.P.,
RA Welsh M.J., Casavant T.L., McCray P.B. Jr.;
RT "Discovery of five conserved beta-defensin gene clusters using a
RT computational search strategy.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2129-2133(2002).
RN [6]
RP FUNCTION, AND DISULFIDE BONDS.
RX PubMed=15033915; DOI=10.1210/en.2003-1698;
RA Yenugu S., Hamil K.G., Radhakrishnan Y., French F.S., Hall S.H.;
RT "The androgen-regulated epididymal sperm-binding protein, human beta-
RT defensin 118 (DEFB118) (formerly ESC42), is an antimicrobial beta-
RT defensin.";
RL Endocrinology 145:3165-3173(2004).
RN [7]
RP FUNCTION.
RX PubMed=33224970; DOI=10.1155/2020/1395304;
RA Lin Q., Xie K., Chen D., Yu B., Mao X., Yu J., Luo J., Zheng P., Luo Y.,
RA Yan H., He J.;
RT "Expression and Functional Characterization of a Novel Antimicrobial
RT Peptide: Human Beta-Defensin 118.";
RL Biomed. Res. Int. 2020:1395304-1395304(2020).
RN [8]
RP FUNCTION.
RX PubMed=33181266; DOI=10.1016/j.peptides.2020.170438;
RA Hou J., Liu H.Y., Diao H., Yu H.;
RT "The truncated human beta-defensin 118 can modulate lipopolysaccharide
RT mediated inflammatory response in RAW264.7 macrophages.";
RL Peptides 136:170438-170438(2021).
CC -!- FUNCTION: Host defense peptide that exhibits antimicrobial activity
CC against both Gram-negative bacteria, such as E.coli and S.typhimurium,
CC and Gram-positive bacteria, such as S.aureus and B.subtilis
CC (PubMed:15033915, PubMed:33224970). Inhibits cell adhesion of E.coli on
CC intestinal epithelial enterocytes (PubMed:33224970). Causes rapid
CC permeabilization of both the outer and inner membrane of E.coli,
CC leading to morphological alterations on the bacterial surface
CC (PubMed:15033915). Binds to bacterial lipopolysaccharides (LPS) with
CC high affinity, and may thereby be involved in immunoregulation through
CC LPS neutralization (PubMed:33181266). May contribute to epididymal
CC innate immunity and protect the sperm against attack by microorganisms
CC (PubMed:15033915). {ECO:0000269|PubMed:15033915,
CC ECO:0000269|PubMed:33181266, ECO:0000269|PubMed:33224970}.
CC -!- INTERACTION:
CC Q96PH6; P43080: GUCA1A; NbExp=3; IntAct=EBI-17250528, EBI-6873005;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12600824}.
CC -!- TISSUE SPECIFICITY: High-level and epididymis-specific expression
CC (PubMed:12600824). Most abundant in the epithelium of the caput and
CC present in the epididymis lumen and bound to sperm (PubMed:12600824).
CC Also expressed in pancreas (PubMed:12600824).
CC {ECO:0000269|PubMed:12600824}.
CC -!- PTM: The three-dimensional structure formed by the three intramolecular
CC disulfide bridges is indispensable for antimicrobial activity.
CC {ECO:0000269|PubMed:15033915}.
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; AF347073; AAL27987.1; -; mRNA.
DR EMBL; AF529415; AAQ09524.1; -; mRNA.
DR EMBL; AL031650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117378; AAI17379.1; -; mRNA.
DR EMBL; AY122471; AAM93913.1; -; mRNA.
DR CCDS; CCDS13177.1; -.
DR RefSeq; NP_473453.1; NM_054112.2.
DR AlphaFoldDB; Q96PH6; -.
DR SMR; Q96PH6; -.
DR BioGRID; 125585; 4.
DR IntAct; Q96PH6; 1.
DR STRING; 9606.ENSP00000253381; -.
DR GlyGen; Q96PH6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96PH6; -.
DR PhosphoSitePlus; Q96PH6; -.
DR BioMuta; DEFB118; -.
DR DMDM; 23813949; -.
DR MassIVE; Q96PH6; -.
DR PaxDb; Q96PH6; -.
DR PeptideAtlas; Q96PH6; -.
DR PRIDE; Q96PH6; -.
DR Antibodypedia; 49713; 13 antibodies from 8 providers.
DR DNASU; 117285; -.
DR Ensembl; ENST00000253381.3; ENSP00000253381.2; ENSG00000131068.4.
DR GeneID; 117285; -.
DR KEGG; hsa:117285; -.
DR MANE-Select; ENST00000253381.3; ENSP00000253381.2; NM_054112.3; NP_473453.1.
DR UCSC; uc002wvr.4; human.
DR CTD; 117285; -.
DR GeneCards; DEFB118; -.
DR HGNC; HGNC:16196; DEFB118.
DR HPA; ENSG00000131068; Tissue enriched (epididymis).
DR MIM; 607650; gene.
DR neXtProt; NX_Q96PH6; -.
DR PharmGKB; PA27245; -.
DR VEuPathDB; HostDB:ENSG00000131068; -.
DR eggNOG; ENOG502TM86; Eukaryota.
DR GeneTree; ENSGT00530000064565; -.
DR HOGENOM; CLU_164142_0_0_1; -.
DR InParanoid; Q96PH6; -.
DR OMA; CWNKSGH; -.
DR OrthoDB; 1618767at2759; -.
DR PhylomeDB; Q96PH6; -.
DR TreeFam; TF336381; -.
DR PathwayCommons; Q96PH6; -.
DR Reactome; R-HSA-1461957; Beta defensins.
DR Reactome; R-HSA-1461973; Defensins.
DR BioGRID-ORCS; 117285; 20 hits in 1054 CRISPR screens.
DR GeneWiki; DEFB118; -.
DR GenomeRNAi; 117285; -.
DR Pharos; Q96PH6; Tbio.
DR PRO; PR:Q96PH6; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q96PH6; protein.
DR Bgee; ENSG00000131068; Expressed in corpus epididymis and 5 other tissues.
DR ExpressionAtlas; Q96PH6; baseline and differential.
DR Genevisible; Q96PH6; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; NAS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; TAS:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0051673; P:membrane disruption in another organism; IDA:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; NAS:UniProtKB.
DR InterPro; IPR025933; Beta_defensin.
DR Pfam; PF13841; Defensin_beta_2; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Defensin;
KW Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PEPTIDE 20..62
FT /note="Defensin beta 118"
FT /id="PRO_0000006983"
FT PROPEP 65..123
FT /evidence="ECO:0000255"
FT /id="PRO_0000006984"
FT REGION 100..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 27..54
FT /evidence="ECO:0000250|UniProtKB:Q91V82"
FT DISULFID 34..48
FT /evidence="ECO:0000250|UniProtKB:Q91V82"
FT DISULFID 38..55
FT /evidence="ECO:0000250|UniProtKB:Q91V82"
FT VARIANT 56
FT /note="I -> V (in dbSNP:rs34173055)"
FT /id="VAR_061133"
SQ SEQUENCE 123 AA; 13614 MW; 0CBAFDB0AE459BA6 CRC64;
MKLLLLALPM LVLLPQVIPA YSGEKKCWNR SGHCRKQCKD GEAVKDTCKN LRACCIPSNE
DHRRVPATSP TPLSDSTPGI IDDILTVRFT TDYFEVSSKK DMVEESEAGR GTETSLPNVH
HSS
