D103A_HUMAN
ID D103A_HUMAN Reviewed; 67 AA.
AC P81534; Q8NFG6; Q9NPF6;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Beta-defensin 103;
DE AltName: Full=Beta-defensin 3;
DE Short=BD-3;
DE Short=DEFB-3;
DE Short=HBD3;
DE Short=hBD-3;
DE AltName: Full=Defensin, beta 103;
DE AltName: Full=Defensin-like protein;
DE Flags: Precursor;
GN Name=DEFB103A; Synonyms=BD3, DEFB103, DEFB3;
GN and
GN Name=DEFB103B;
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], PROTEIN SEQUENCE OF 23-67, FUNCTION, TISSUE
RP SPECIFICITY, INDUCTION, AND MASS SPECTROMETRY.
RC TISSUE=Keratinocyte, Lung epithelium, and Tracheal epithelium;
RX PubMed=11085990; DOI=10.1074/jbc.m008557200;
RA Harder J., Bartels J., Christophers E., Schroeder J.-M.;
RT "Isolation and characterization of human beta-defensin-3, a novel human
RT inducible peptide antibiotic.";
RL J. Biol. Chem. 276:5707-5713(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=11702237; DOI=10.1007/s004410100433;
RA Conejo-Garcia J.-R., Jaumann F., Schulz S., Krause A.,
RA Rodriguez-Jimenez F.-J., Forssmann U., Adermann K., Kluever E.,
RA Vogelmeier C., Becker D., Hedrich R., Forssmann W.-G., Bals R.;
RT "Identification of a novel, multifunctional beta-defensin (human beta-
RT defensin 3) with specific antimicrobial activity. Its interaction with
RT plasma membranes of Xenopus oocytes and the induction of macrophage
RT chemoattraction.";
RL Cell Tissue Res. 306:257-264(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11223260; DOI=10.1016/s0378-1119(00)00569-2;
RA Jia H.P., Schutte B.C., Schudy A., Linzmeier R., Guthmiller J.M.,
RA Johnson G.K., Tack B.F., Mitros J.P., Rosenthal A., Ganz T.,
RA McCray P.B. Jr.;
RT "Discovery of new human beta-defensins using a genomics-based approach.";
RL Gene 263:211-218(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Imai Y.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Adler D.A., Diamond G., Sheppard P., Holloway J., Presnell S., Jaspers S.,
RA Whitmore T., Fox B., Gosink J., Rixon M., Gao Z., Haldeman B., O'Hara P.;
RT "EST and genomic database mining yield novel human and mouse beta-
RT defensins.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tonsil;
RA Chen S., He F., Li R.;
RT "Cloning and expression of Chinese human beta defensin-3.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0007744|PDB:1KJ6}
RP STRUCTURE BY NMR OF 23-67, AND DISULFIDE BONDS.
RX PubMed=11741980; DOI=10.1074/jbc.m108830200;
RA Schibli D.J., Hunter H.N., Aseyev V., Starner T.D., Wiencek J.M.,
RA McCray P.B. Jr., Tack B.F., Vogel H.J.;
RT "The solution structures of the human beta-defensins lead to a better
RT understanding of the potent bactericidal activity of HBD3 against
RT Staphylococcus aureus.";
RL J. Biol. Chem. 277:8279-8289(2002).
CC -!- FUNCTION: Exhibits antimicrobial activity against Gram-positive
CC bacteria S.aureus and S.pyogenes, Gram-negative bacteria P.aeruginosa
CC and E.coli and the yeast C.albicans. Kills multiresistant S.aureus and
CC vancomycin-resistant E.faecium. No significant hemolytic activity was
CC observed. {ECO:0000269|PubMed:11085990}.
CC -!- INTERACTION:
CC P81534; Q13520: AQP6; NbExp=3; IntAct=EBI-12074168, EBI-13059134;
CC P81534; Q9Y2C3: B3GALT5; NbExp=3; IntAct=EBI-12074168, EBI-14141066;
CC P81534; Q15125: EBP; NbExp=3; IntAct=EBI-12074168, EBI-3915253;
CC P81534; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12074168, EBI-781551;
CC P81534; Q2M2E3: ODF4; NbExp=3; IntAct=EBI-12074168, EBI-12382569;
CC P81534; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-12074168, EBI-17247926;
CC P81534; Q8IWB4: SPATA31A7; NbExp=3; IntAct=EBI-12074168, EBI-1222614;
CC P81534; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-12074168, EBI-17280858;
CC P81534; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-12074168, EBI-8638294;
CC P81534; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-12074168, EBI-12345267;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Highly expressed in skin and tonsils, and to a
CC lesser extent in trachea, uterus, kidney, thymus, adenoid, pharynx and
CC tongue. Low expression in salivary gland, bone marrow, colon, stomach,
CC polyp and larynx. No expression in small intestine.
CC {ECO:0000269|PubMed:11085990}.
CC -!- INDUCTION: By bacterial infection and by IFNG/IFN-gamma.
CC {ECO:0000269|PubMed:11085990}.
CC -!- MASS SPECTROMETRY: Mass=5154.59; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11085990};
CC -!- SIMILARITY: Belongs to the beta-defensin family. {ECO:0000305}.
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DR EMBL; AJ237673; CAC03097.1; -; mRNA.
DR EMBL; AF295370; AAG02237.1; -; mRNA.
DR EMBL; AF217245; AAF73853.1; -; mRNA.
DR EMBL; AB037972; BAB40572.1; -; mRNA.
DR EMBL; AF301470; AAG22030.1; -; mRNA.
DR EMBL; AF516673; AAM62424.1; -; mRNA.
DR CCDS; CCDS34810.1; -.
DR CCDS; CCDS43701.1; -.
DR RefSeq; NP_001075020.1; NM_001081551.3.
DR RefSeq; NP_061131.1; NM_018661.4.
DR RefSeq; XP_016885681.1; XM_017030192.1.
DR PDB; 1KJ6; NMR; -; A=23-67.
DR PDBsum; 1KJ6; -.
DR AlphaFoldDB; P81534; -.
DR SMR; P81534; -.
DR BioGRID; 120984; 13.
DR BioGRID; 136062; 12.
DR IntAct; P81534; 10.
DR STRING; 9606.ENSP00000320951; -.
DR TCDB; 1.C.85.1.3; the pore-forming Beta-defensin (Beta-defensin) family.
DR BioMuta; DEFB103A; -.
DR DMDM; 17372441; -.
DR MassIVE; P81534; -.
DR PaxDb; P81534; -.
DR PeptideAtlas; P81534; -.
DR PRIDE; P81534; -.
DR ProteomicsDB; 57697; -.
DR Antibodypedia; 22020; 146 antibodies from 20 providers.
DR Antibodypedia; 58735; 53 antibodies from 9 providers.
DR DNASU; 55894; -.
DR Ensembl; ENST00000314357.4; ENSP00000320951.3; ENSG00000176797.4.
DR Ensembl; ENST00000318124.3; ENSP00000324633.3; ENSG00000177243.3.
DR Ensembl; ENST00000613448.2; ENSP00000480773.1; ENSG00000273641.2.
DR Ensembl; ENST00000642635.1; ENSP00000495040.1; ENSG00000285376.1.
DR Ensembl; ENST00000646258.1; ENSP00000493640.1; ENSG00000285376.1.
DR Ensembl; ENST00000646344.2; ENSP00000493616.1; ENSG00000284978.2.
DR GeneID; 414325; -.
DR GeneID; 55894; -.
DR KEGG; hsa:414325; -.
DR KEGG; hsa:55894; -.
DR MANE-Select; ENST00000314357.4; ENSP00000320951.3; NM_001081551.4; NP_001075020.1.
DR MANE-Select; ENST00000318124.3; ENSP00000324633.3; NM_018661.4; NP_061131.1.
DR UCSC; uc003wrf.4; human.
DR CTD; 414325; -.
DR CTD; 55894; -.
DR DisGeNET; 414325; -.
DR DisGeNET; 55894; -.
DR GeneCards; DEFB103A; -.
DR GeneCards; DEFB103B; -.
DR HGNC; HGNC:15967; DEFB103A.
DR HGNC; HGNC:31702; DEFB103B.
DR HPA; ENSG00000176797; Tissue enhanced (lymphoid tissue, salivary gland, vagina).
DR HPA; ENSG00000177243; Not detected.
DR MIM; 606611; gene.
DR neXtProt; NX_P81534; -.
DR OpenTargets; ENSG00000176797; -.
DR PharmGKB; PA134933952; -.
DR VEuPathDB; HostDB:ENSG00000176797; -.
DR VEuPathDB; HostDB:ENSG00000177243; -.
DR eggNOG; ENOG502TF5P; Eukaryota.
DR GeneTree; ENSGT00530000064280; -.
DR HOGENOM; CLU_189296_2_0_1; -.
DR InParanoid; P81534; -.
DR OMA; EQIGHCS; -.
DR OrthoDB; 1630404at2759; -.
DR PhylomeDB; P81534; -.
DR PathwayCommons; P81534; -.
DR Reactome; R-HSA-1461957; Beta defensins.
DR Reactome; R-HSA-1461973; Defensins.
DR SignaLink; P81534; -.
DR BioGRID-ORCS; 414325; 57 hits in 571 CRISPR screens.
DR BioGRID-ORCS; 55894; 99 hits in 870 CRISPR screens.
DR ChiTaRS; DEFB103A; human.
DR ChiTaRS; DEFB103B; human.
DR EvolutionaryTrace; P81534; -.
DR GeneWiki; DEFB103A; -.
DR Pharos; P81534; Tbio.
DR PRO; PR:P81534; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P81534; protein.
DR Bgee; ENSG00000176797; Expressed in skin of leg and 49 other tissues.
DR Genevisible; P81534; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0031731; F:CCR6 chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0042056; F:chemoattractant activity; IBA:GO_Central.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
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:0051873; P:killing by host of symbiont cells; IDA:CACAO.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR InterPro; IPR001855; Defensin_beta-typ.
DR Pfam; PF00711; Defensin_beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Defensin;
KW Direct protein sequencing; Disulfide bond; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:11085990"
FT PEPTIDE 23..67
FT /note="Beta-defensin 103"
FT /id="PRO_0000006971"
FT DISULFID 33..62
FT /evidence="ECO:0000269|PubMed:11741980,
FT ECO:0007744|PDB:1KJ6"
FT DISULFID 40..55
FT /evidence="ECO:0000269|PubMed:11741980,
FT ECO:0007744|PDB:1KJ6"
FT DISULFID 45..63
FT /evidence="ECO:0000269|PubMed:11741980,
FT ECO:0007744|PDB:1KJ6"
FT CONFLICT 45
FT /note="C -> R (in Ref. 6; AAM62424)"
FT /evidence="ECO:0000305"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1KJ6"
FT HELIX 32..36
FT /evidence="ECO:0007829|PDB:1KJ6"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1KJ6"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1KJ6"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1KJ6"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1KJ6"
SQ SEQUENCE 67 AA; 7697 MW; 54266DE1C90D4B65 CRC64;
MRIHYLLFAL LFLFLVPVPG HGGIINTLQK YYCRVRGGRC AVLSCLPKEE QIGKCSTRGR
KCCRRKK
