D106A_HUMAN
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 03-AUG-2022, entry version 137.
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}.
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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 AlphaFoldDB; Q8N104; -.
DR SMR; Q8N104; -.
DR BioGRID; 128834; 18.
DR STRING; 9606.ENSP00000334364; -.
DR BioMuta; DEFB106A; -.
DR DMDM; 26392715; -.
DR MassIVE; Q8N104; -.
DR PaxDb; Q8N104; -.
DR PeptideAtlas; Q8N104; -.
DR PRIDE; Q8N104; -.
DR ProteomicsDB; 71503; -.
DR Antibodypedia; 56702; 7 antibodies from 6 providers.
DR Antibodypedia; 69006; 27 antibodies from 7 providers.
DR DNASU; 245909; -.
DR Ensembl; ENST00000335186.3; ENSP00000335307.2; ENSG00000186579.3.
DR Ensembl; ENST00000335479.2; ENSP00000334364.2; ENSG00000187082.2.
DR Ensembl; ENST00000621252.2; ENSP00000477883.1; ENSG00000275794.2.
DR Ensembl; ENST00000650001.1; ENSP00000497538.1; ENSG00000285617.1.
DR Ensembl; ENST00000650390.1; ENSP00000498101.1; ENSG00000285617.1.
DR GeneID; 245909; -.
DR GeneID; 503841; -.
DR KEGG; hsa:245909; -.
DR KEGG; hsa:503841; -.
DR MANE-Select; ENST00000335186.3; ENSP00000335307.2; NM_152251.4; NP_689464.1.
DR MANE-Select; ENST00000335479.2; ENSP00000334364.2; NM_001040704.2; NP_001035794.1.
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; -.
DR VEuPathDB; HostDB:ENSG00000187082; -.
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 SignaLink; Q8N104; -.
DR BioGRID-ORCS; 245909; 8 hits in 543 CRISPR screens.
DR BioGRID-ORCS; 503841; 27 hits in 604 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 liver and 31 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:0000269|PubMed:23938203,
FT ECO:0007744|PDB:2LWL"
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:0007829|PDB:2LWL"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:2LWL"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:2LWL"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:2LWL"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2LWL"
SQ SEQUENCE 65 AA; 7369 MW; 9D1C89BB0041E02D CRC64;
MRTFLFLFAV LFFLTPAKNA FFDEKCNKLK GTCKNNCGKN EELIALCQKS LKCCRTIQPC
GSIID
