ID D106A_HUMAN Reviewed; 65 AA. AC Q8N104; Q2NKR0; Q496I8; DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 10-FEB-2021, entry version 131. DE RecName: Full=Beta-defensin 106; DE AltName: Full=Beta-defensin 6; DE Short=BD-6; DE Short=DEFB-6; DE AltName: Full=Defensin, beta 106; DE Flags: Precursor; GN Name=DEFB106A; Synonyms=BD6, DEFB106, DEFB6; GN and GN Name=DEFB106B; 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=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 [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Epididymis; RX PubMed=12193721; DOI=10.4049/jimmunol.169.5.2516; RA Yamaguchi Y., Nagase T., Makita R., Fukuhara S., Tomita T., Tominaga T., RA Kurihara H., Ouchi Y.; RT "Identification of multiple novel epididymis-specific beta-defensin RT isoforms in humans and mice."; RL J. Immunol. 169:2516-2523(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 1-57. RX PubMed=12734011; DOI=10.1186/gb-2003-4-5-r31; RA Semple C.A.M., Rolfe M., Dorin J.R.; RT "Duplication and selection in the evolution of primate beta-defensin RT genes."; RL Genome Biol. 4:R31.1-R31.11(2003). RN [6] RP STRUCTURE BY NMR OF 21-65, DISULFIDE BONDS, FUNCTION, SUBUNIT, INTERACTION RP WITH CCR2, AND SUBCELLULAR LOCATION. RX PubMed=23938203; DOI=10.1016/j.jmb.2013.08.001; RA De Paula V.S., Gomes N.S., Lima L.G., Miyamoto C.A., Monteiro R.Q., RA Almeida F.C., Valente A.P.; RT "Structural basis for the interaction of human beta-defensin 6 and its RT putative chemokine receptor CCR2 and breast cancer microvesicles."; RL J. Mol. Biol. 425:4479-4495(2013). CC -!- FUNCTION: Has antibacterial activity (PubMed:12600824). Acts as a CC ligand for C-C chemokine receptor CCR2 (PubMed:23938203). CC {ECO:0000269|PubMed:12600824, ECO:0000269|PubMed:23938203}. CC -!- SUBUNIT: Monomer (PubMed:23938203). Interacts with CCR2 (via CC extracellular N-terminal region); this interaction may preferentially CC require specific tyrosine sulfation on CCR2 (PubMed:23938203). CC {ECO:0000269|PubMed:23938203}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Membrane CC {ECO:0000269|PubMed:23938203}. Note=Associates with tumor cell CC membrane-derived microvesicles (PubMed:23938203). CC {ECO:0000269|PubMed:23938203}. CC -!- TISSUE SPECIFICITY: Expressed specifically in epididymis and lung. CC {ECO:0000269|PubMed:12600824}. 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; AY122466; AAM93908.1; -; mRNA. DR EMBL; AB089181; BAC10631.1; -; mRNA. DR EMBL; AF529417; AAQ09526.1; -; mRNA. DR EMBL; BC100844; AAI00845.1; -; mRNA. DR EMBL; BC100845; AAI00846.1; -; mRNA. DR EMBL; BC100846; AAI00847.1; -; mRNA. DR EMBL; BC100847; AAI00848.1; -; mRNA. DR EMBL; BC110062; AAI10063.1; -; mRNA. DR EMBL; BC111688; AAI11689.1; -; mRNA. DR EMBL; AF540978; AAN33114.1; -; mRNA. DR CCDS; CCDS34813.1; -. DR CCDS; CCDS34833.1; -. DR RefSeq; NP_001035794.1; NM_001040704.1. DR RefSeq; NP_689464.1; NM_152251.3. DR PDB; 2LWL; NMR; -; A=21-65. DR PDBsum; 2LWL; -. DR SMR; Q8N104; -. DR BioGRID; 128834; 19. DR STRING; 9606.ENSP00000335307; -. DR BioMuta; DEFB106A; -. DR DMDM; 26392715; -. DR PaxDb; Q8N104; -. DR PeptideAtlas; Q8N104; -. DR PRIDE; Q8N104; -. DR ProteomicsDB; 71503; -. DR Antibodypedia; 56702; 7 antibodies. DR Antibodypedia; 69006; 27 antibodies. DR DNASU; 245909; -. DR Ensembl; ENST00000335186; ENSP00000335307; ENSG00000186579. DR Ensembl; ENST00000335479; ENSP00000334364; ENSG00000187082. DR Ensembl; ENST00000621252; ENSP00000477883; ENSG00000275794. DR Ensembl; ENST00000650001; ENSP00000497538; ENSG00000285617. DR Ensembl; ENST00000650390; ENSP00000498101; ENSG00000285617. DR GeneID; 245909; -. DR GeneID; 503841; -. DR KEGG; hsa:245909; -. DR KEGG; hsa:503841; -. DR UCSC; uc003wro.2; human. DR CTD; 245909; -. DR CTD; 503841; -. DR DisGeNET; 245909; -. DR DisGeNET; 503841; -. DR GeneCards; DEFB106A; -. DR GeneCards; DEFB106B; -. DR HGNC; HGNC:18088; DEFB106A. DR HGNC; HGNC:28879; DEFB106B. DR HPA; ENSG00000186579; Tissue enriched (epididymis). DR HPA; ENSG00000187082; Tissue enriched (epididymis). DR neXtProt; NX_Q8N104; -. DR OpenTargets; ENSG00000187082; -. DR PharmGKB; PA142671992; -. DR VEuPathDB; HostDB:ENSG00000186579.2; -. DR VEuPathDB; HostDB:ENSG00000187082.2; -. DR eggNOG; ENOG502TF62; Eukaryota. DR GeneTree; ENSGT00390000005938; -. DR HOGENOM; CLU_187814_0_0_1; -. DR InParanoid; Q8N104; -. DR OMA; RGTCKNN; -. DR OrthoDB; 1629258at2759; -. DR PhylomeDB; Q8N104; -. DR PathwayCommons; Q8N104; -. DR Reactome; R-HSA-1461957; Beta defensins. DR Reactome; R-HSA-1461973; Defensins. DR BioGRID-ORCS; 245909; 2 hits in 442 CRISPR screens. DR BioGRID-ORCS; 503841; 23 hits in 481 CRISPR screens. DR GeneWiki; DEFB106A; -. DR Pharos; Q8N104; Tbio. DR PRO; PR:Q8N104; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q8N104; protein. DR Bgee; ENSG00000186579; Expressed in urinary bladder and 33 other tissues. DR Genevisible; Q8N104; HS. DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB. DR GO; GO:1990742; C:microvesicle; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0031727; F:CCR2 chemokine receptor binding; IDA:UniProtKB. DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB. DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB. DR GO; GO:0061760; P:antifungal innate immune response; IDA: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 InterPro; IPR025933; Beta_defensin. DR Pfam; PF13841; Defensin_beta_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic; Antimicrobial; Defensin; Disulfide bond; KW Membrane; Reference proteome; Secreted; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000305|PubMed:23938203" FT PEPTIDE 21..65 FT /note="Beta-defensin 106" FT /id="PRO_0000006977" FT DISULFID 26..53 FT /evidence="ECO:0000244|PDB:2LWL, FT ECO:0000269|PubMed:23938203" FT DISULFID 33..47 FT /evidence="ECO:0000250" FT DISULFID 37..54 FT /evidence="ECO:0000250" FT CONFLICT 50 FT /note="S -> F (in Ref. 3; AAQ09526)" FT /evidence="ECO:0000305" FT HELIX 22..28 FT /evidence="ECO:0000244|PDB:2LWL" FT STRAND 32..36 FT /evidence="ECO:0000244|PDB:2LWL" FT STRAND 41..46 FT /evidence="ECO:0000244|PDB:2LWL" FT STRAND 52..56 FT /evidence="ECO:0000244|PDB:2LWL" FT STRAND 59..61 FT /evidence="ECO:0000244|PDB:2LWL" SQ SEQUENCE 65 AA; 7369 MW; 9D1C89BB0041E02D CRC64; MRTFLFLFAV LFFLTPAKNA FFDEKCNKLK GTCKNNCGKN EELIALCQKS LKCCRTIQPC GSIID //