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P81534

- D103A_HUMAN

UniProt

P81534 - D103A_HUMAN

Protein

Beta-defensin 103

Gene

DEFB103A

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

    Exhibits antimicrobial activity against Gram-positive bacteria S.aureus and S.pyogenes, Gram-negative bacteria P.aeruginosa and E.coli and the yeast C.albicans. Kills multiresistant S.aureus and vancomycin-resistant E.faecium. No significant hemolytic activity was observed.1 Publication

    GO - Biological processi

    1. defense response to bacterium Source: UniProtKB-KW
    2. innate immune response Source: Reactome
    3. positive regulation of biosynthetic process of antibacterial peptides active against Gram-positive bacteria Source: UniProtKB

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Defensin

    Enzyme and pathway databases

    ReactomeiREACT_115846. Defensins.
    REACT_115897. Beta defensins.

    Protein family/group databases

    TCDBi1.C.85.1.3. the pore-forming -defensin (-defensin) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-defensin 103
    Alternative name(s):
    Beta-defensin 3
    Short name:
    BD-3
    Short name:
    DEFB-3
    Short name:
    HBD3
    Short name:
    hBD-3
    Defensin, beta 103
    Defensin-like protein
    Gene namesi
    Name:DEFB103A
    Synonyms:BD3, DEFB103, DEFB3
    AND
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:15967. DEFB103A.
    HGNC:31702. DEFB103B.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. Golgi lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134933952.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Peptidei23 – 6745Beta-defensin 103PRO_0000006971Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi33 ↔ 62
    Disulfide bondi40 ↔ 55
    Disulfide bondi45 ↔ 63

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP81534.
    PRIDEiP81534.

    Expressioni

    Tissue specificityi

    Highly expressed in skin and tonsils, and to a lesser extent in trachea, uterus, kidney, thymus, adenoid, pharynx and tongue. Low expression in salivary gland, bone marrow, colon, stomach, polyp and larynx. No expression in small intestine.1 Publication

    Inductioni

    By bacterial infection and by IFNG/IFN-gamma.1 Publication

    Gene expression databases

    BgeeiP81534.
    CleanExiHS_DEFB103A.
    HS_DEFB103B.
    GenevestigatoriP81534.

    Interactioni

    Protein-protein interaction databases

    BioGridi120984. 1 interaction.
    STRINGi9606.ENSP00000320951.

    Structurei

    Secondary structure

    1
    67
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni29 – 313
    Helixi32 – 365
    Beta strandi39 – 446
    Beta strandi49 – 535
    Beta strandi55 – 595
    Beta strandi61 – 655

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KJ6NMR-A23-67[»]
    ProteinModelPortaliP81534.
    SMRiP81534. Positions 23-67.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81534.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the beta-defensin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG40430.
    HOGENOMiHOG000015465.
    HOVERGENiHBG004834.
    InParanoidiP81534.
    OMAiSCLPREE.
    OrthoDBiEOG7SJD7S.
    PhylomeDBiP81534.

    Family and domain databases

    InterProiIPR001855. Defensin_beta-typ.
    [Graphical view]
    PfamiPF00711. Defensin_beta. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P81534-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRIHYLLFAL LFLFLVPVPG HGGIINTLQK YYCRVRGGRC AVLSCLPKEE   50
    QIGKCSTRGR KCCRRKK 67
    Length:67
    Mass (Da):7,697
    Last modified:June 1, 2001 - v2
    Checksum:i54266DE1C90D4B65
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451C → R in AAM62424. 1 PublicationCurated

    Mass spectrometryi

    Molecular mass is 5154.59 Da from positions 23 - 67. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ237673 mRNA. Translation: CAC03097.1.
    AF295370 mRNA. Translation: AAG02237.1.
    AF217245 mRNA. Translation: AAF73853.1.
    AB037972 mRNA. Translation: BAB40572.1.
    AF301470 mRNA. Translation: AAG22030.1.
    AF516673 mRNA. Translation: AAM62424.1.
    CCDSiCCDS34810.1.
    CCDS43701.1.
    RefSeqiNP_001075020.1. NM_001081551.3.
    NP_061131.1. NM_018661.4.
    UniGeneiHs.283082.
    Hs.637221.

    Genome annotation databases

    EnsembliENST00000314357; ENSP00000320951; ENSG00000176797.
    ENST00000318124; ENSP00000324633; ENSG00000177243.
    GeneIDi414325.
    55894.
    KEGGihsa:414325.
    hsa:55894.
    UCSCiuc003wrf.3. human.

    Polymorphism databases

    DMDMi17372441.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ237673 mRNA. Translation: CAC03097.1 .
    AF295370 mRNA. Translation: AAG02237.1 .
    AF217245 mRNA. Translation: AAF73853.1 .
    AB037972 mRNA. Translation: BAB40572.1 .
    AF301470 mRNA. Translation: AAG22030.1 .
    AF516673 mRNA. Translation: AAM62424.1 .
    CCDSi CCDS34810.1.
    CCDS43701.1.
    RefSeqi NP_001075020.1. NM_001081551.3.
    NP_061131.1. NM_018661.4.
    UniGenei Hs.283082.
    Hs.637221.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KJ6 NMR - A 23-67 [» ]
    ProteinModelPortali P81534.
    SMRi P81534. Positions 23-67.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120984. 1 interaction.
    STRINGi 9606.ENSP00000320951.

    Protein family/group databases

    TCDBi 1.C.85.1.3. the pore-forming -defensin (-defensin) family.

    Polymorphism databases

    DMDMi 17372441.

    Proteomic databases

    PaxDbi P81534.
    PRIDEi P81534.

    Protocols and materials databases

    DNASUi 414325.
    55894.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314357 ; ENSP00000320951 ; ENSG00000176797 .
    ENST00000318124 ; ENSP00000324633 ; ENSG00000177243 .
    GeneIDi 414325.
    55894.
    KEGGi hsa:414325.
    hsa:55894.
    UCSCi uc003wrf.3. human.

    Organism-specific databases

    CTDi 414325.
    55894.
    GeneCardsi GC08M007277.
    GC08P007739.
    HGNCi HGNC:15967. DEFB103A.
    HGNC:31702. DEFB103B.
    MIMi 606611. gene.
    neXtProti NX_P81534.
    PharmGKBi PA134933952.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40430.
    HOGENOMi HOG000015465.
    HOVERGENi HBG004834.
    InParanoidi P81534.
    OMAi SCLPREE.
    OrthoDBi EOG7SJD7S.
    PhylomeDBi P81534.

    Enzyme and pathway databases

    Reactomei REACT_115846. Defensins.
    REACT_115897. Beta defensins.

    Miscellaneous databases

    EvolutionaryTracei P81534.
    GeneWikii DEFB103A.
    NextBioi 108587.
    PROi P81534.
    SOURCEi Search...

    Gene expression databases

    Bgeei P81534.
    CleanExi HS_DEFB103A.
    HS_DEFB103B.
    Genevestigatori P81534.

    Family and domain databases

    InterProi IPR001855. Defensin_beta-typ.
    [Graphical view ]
    Pfami PF00711. Defensin_beta. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of human beta-defensin-3, a novel human inducible peptide antibiotic."
      Harder J., Bartels J., Christophers E., Schroeder J.-M.
      J. Biol. Chem. 276:5707-5713(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-67, FUNCTION, TISSUE SPECIFICITY, INDUCTION, MASS SPECTROMETRY.
      Tissue: Keratinocyte, Lung epithelium and Tracheal epithelium.
    2. "Identification of a novel, multifunctional beta-defensin (human beta-defensin 3) with specific antimicrobial activity. Its interaction with plasma membranes of Xenopus oocytes and the induction of macrophage chemoattraction."
      Conejo-Garcia J.-R., Jaumann F., Schulz S., Krause A., Rodriguez-Jimenez F.-J., Forssmann U., Adermann K., Kluever E., Vogelmeier C., Becker D., Hedrich R., Forssmann W.-G., Bals R.
      Cell Tissue Res. 306:257-264(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. Imai Y.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "EST and genomic database mining yield novel human and mouse beta-defensins."
      Adler D.A., Diamond G., Sheppard P., Holloway J., Presnell S., Jaspers S., Whitmore T., Fox B., Gosink J., Rixon M., Gao Z., Haldeman B., O'Hara P.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "Cloning and expression of Chinese human beta defensin-3."
      Chen S., He F., Li R.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Tonsil.
    7. "The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus."
      Schibli D.J., Hunter H.N., Aseyev V., Starner T.D., Wiencek J.M., McCray P.B. Jr., Tack B.F., Vogel H.J.
      J. Biol. Chem. 277:8279-8289(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 23-67.

    Entry informationi

    Entry nameiD103A_HUMAN
    AccessioniPrimary (citable) accession number: P81534
    Secondary accession number(s): Q8NFG6, Q9NPF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 132 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3