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Q01523

- DEF5_HUMAN

UniProt

Q01523 - DEF5_HUMAN

Protein

Defensin-5

Gene

DEFA5

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

    Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. All DEFA5 peptides exert antimicrobial activities, but their potency is affected by peptide processing.3 Publications

    GO - Biological processi

    1. antibacterial humoral response Source: UniProt
    2. defense response to fungus Source: UniProtKB-KW
    3. innate immune response Source: UniProt
    4. killing of cells of other organism Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Defensin, Fungicide

    Enzyme and pathway databases

    ReactomeiREACT_115574. Alpha-defensins.
    REACT_115846. Defensins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Defensin-5
    Alternative name(s):
    Defensin, alpha 5
    HD5(20-94)
    Cleaved into the following 4 chains:
    Gene namesi
    Name:DEFA5
    Synonyms:DEF5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:2764. DEFA5.

    Subcellular locationi

    Secreted 1 Publication. Cytoplasmic vesiclesecretory vesicle 1 Publication
    Note: Peptides HD5(20-94), HD5(23-94) and HD5(29-94) are found within tissues, HD5(20-94) being the predominant intracellular form. Peptides HD5(56-94) and HD5(63-94) are found in the extracellular milieu, HD5(63-94) being the most abundant form.

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: InterPro
    3. Golgi lumen Source: Reactome
    4. secretory granule lumen Source: Reactome
    5. transport vesicle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27241.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Add
    BLAST
    Peptidei20 – 9475Defensin-5PRO_0000006787Add
    BLAST
    Peptidei23 – 9472HD5(23-94)PRO_0000417387Add
    BLAST
    Peptidei29 – 9466HD5(29-94)PRO_0000417388Add
    BLAST
    Peptidei56 – 9439HD5(56-94)PRO_0000417389Add
    BLAST
    Peptidei63 – 9432HD5(63-94)PRO_0000417390Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi65 ↔ 931 Publication
    Disulfide bondi67 ↔ 821 Publication
    Disulfide bondi72 ↔ 921 Publication

    Post-translational modificationi

    Glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ01523.
    PeptideAtlasiQ01523.
    PRIDEiQ01523.

    Miscellaneous databases

    PMAP-CutDBQ01523.

    Expressioni

    Tissue specificityi

    Paneth cells of the small intestine (at protein level).1 Publication

    Gene expression databases

    BgeeiQ01523.
    CleanExiHS_DEFA5.
    GenevestigatoriQ01523.

    Organism-specific databases

    HPAiHPA015775.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi108034. 1 interaction.
    IntActiQ01523. 1 interaction.
    STRINGi9606.ENSP00000329890.

    Structurei

    Secondary structure

    1
    94
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi65 – 706
    Beta strandi76 – 827
    Beta strandi89 – 935

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZMPX-ray1.65A/B/C/D63-94[»]
    2LXZNMR-A63-94[»]
    3I5WX-ray1.63A/B63-94[»]
    4E82X-ray1.70A/B63-94[»]
    4E83X-ray1.90A/B63-94[»]
    4E86X-ray2.75A/B/C/D/E/F/G/H/L63-94[»]
    ProteinModelPortaliQ01523.
    SMRiQ01523. Positions 63-94.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ01523.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alpha-defensin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG69207.
    HOGENOMiHOG000233351.
    HOVERGENiHBG011703.
    InParanoidiQ01523.
    KOiK05230.
    OMAiQSGEDNQ.
    OrthoDBiEOG75TMFQ.
    PhylomeDBiQ01523.
    TreeFamiTF338414.

    Family and domain databases

    InterProiIPR016327. Alpha-defensin.
    IPR006080. Defensin_beta/neutrophil.
    IPR002366. Defensin_propep.
    IPR006081. Mammalian_defensins.
    [Graphical view]
    PANTHERiPTHR11876. PTHR11876. 1 hit.
    PfamiPF00323. Defensin_1. 1 hit.
    PF00879. Defensin_propep. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001875. Alpha-defensin. 1 hit.
    SMARTiSM00048. DEFSN. 1 hit.
    [Graphical view]
    PROSITEiPS00269. DEFENSIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q01523-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRTIAILAAI LLVALQAQAE SLQERADEAT TQKQSGEDNQ DLAISFAGNG   50
    LSALRTSGSQ ARATCYCRTG RCATRESLSG VCEISGRLYR LCCR 94
    Length:94
    Mass (Da):10,071
    Last modified:July 1, 1993 - v1
    Checksum:i19B5B00B6BAF90DA
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711R → H.
    Corresponds to variant rs7839771 [ dbSNP | Ensembl ].
    VAR_059245

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97925 Genomic DNA. Translation: AAA35754.1.
    AF238378 Genomic DNA. Translation: AAT68886.1.
    CH471153 Genomic DNA. Translation: EAW80489.1.
    BC069690 mRNA. Translation: AAH69690.1.
    BC107079 mRNA. Translation: AAI07080.1.
    CCDSiCCDS5963.1.
    PIRiA44454.
    RefSeqiNP_066290.1. NM_021010.1.
    UniGeneiHs.655233.

    Genome annotation databases

    EnsembliENST00000330590; ENSP00000329890; ENSG00000164816.
    GeneIDi1670.
    KEGGihsa:1670.
    UCSCiuc003wra.1. human.

    Polymorphism databases

    DMDMi399353.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97925 Genomic DNA. Translation: AAA35754.1 .
    AF238378 Genomic DNA. Translation: AAT68886.1 .
    CH471153 Genomic DNA. Translation: EAW80489.1 .
    BC069690 mRNA. Translation: AAH69690.1 .
    BC107079 mRNA. Translation: AAI07080.1 .
    CCDSi CCDS5963.1.
    PIRi A44454.
    RefSeqi NP_066290.1. NM_021010.1.
    UniGenei Hs.655233.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZMP X-ray 1.65 A/B/C/D 63-94 [» ]
    2LXZ NMR - A 63-94 [» ]
    3I5W X-ray 1.63 A/B 63-94 [» ]
    4E82 X-ray 1.70 A/B 63-94 [» ]
    4E83 X-ray 1.90 A/B 63-94 [» ]
    4E86 X-ray 2.75 A/B/C/D/E/F/G/H/L 63-94 [» ]
    ProteinModelPortali Q01523.
    SMRi Q01523. Positions 63-94.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108034. 1 interaction.
    IntActi Q01523. 1 interaction.
    STRINGi 9606.ENSP00000329890.

    Polymorphism databases

    DMDMi 399353.

    Proteomic databases

    PaxDbi Q01523.
    PeptideAtlasi Q01523.
    PRIDEi Q01523.

    Protocols and materials databases

    DNASUi 1670.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330590 ; ENSP00000329890 ; ENSG00000164816 .
    GeneIDi 1670.
    KEGGi hsa:1670.
    UCSCi uc003wra.1. human.

    Organism-specific databases

    CTDi 1670.
    GeneCardsi GC08M006900.
    HGNCi HGNC:2764. DEFA5.
    HPAi HPA015775.
    MIMi 600472. gene.
    neXtProti NX_Q01523.
    PharmGKBi PA27241.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG69207.
    HOGENOMi HOG000233351.
    HOVERGENi HBG011703.
    InParanoidi Q01523.
    KOi K05230.
    OMAi QSGEDNQ.
    OrthoDBi EOG75TMFQ.
    PhylomeDBi Q01523.
    TreeFami TF338414.

    Enzyme and pathway databases

    Reactomei REACT_115574. Alpha-defensins.
    REACT_115846. Defensins.

    Miscellaneous databases

    ChiTaRSi DEFA5. human.
    EvolutionaryTracei Q01523.
    GeneWikii DEFA5.
    GenomeRNAii 1670.
    NextBioi 6872.
    PMAP-CutDB Q01523.
    PROi Q01523.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q01523.
    CleanExi HS_DEFA5.
    Genevestigatori Q01523.

    Family and domain databases

    InterProi IPR016327. Alpha-defensin.
    IPR006080. Defensin_beta/neutrophil.
    IPR002366. Defensin_propep.
    IPR006081. Mammalian_defensins.
    [Graphical view ]
    PANTHERi PTHR11876. PTHR11876. 1 hit.
    Pfami PF00323. Defensin_1. 1 hit.
    PF00879. Defensin_propep. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001875. Alpha-defensin. 1 hit.
    SMARTi SM00048. DEFSN. 1 hit.
    [Graphical view ]
    PROSITEi PS00269. DEFENSIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Paneth cells of the human small intestine express an antimicrobial peptide gene."
      Jones D.E., Bevins C.L.
      J. Biol. Chem. 267:23216-23225(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Intestine.
    2. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "Paneth cell trypsin is the processing enzyme for human defensin-5."
      Ghosh D., Porter E., Shen B., Lee S.K., Wilk D., Drazba J., Yadav S.P., Crabb J.W., Ganz T., Bevins C.L.
      Nat. Immunol. 3:583-590(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, PEPTIDE CHARACTERIZATION, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "Antibacterial activity and specificity of the six human alpha-defensins."
      Ericksen B., Wu Z., Lu W., Lehrer R.I.
      Antimicrob. Agents Chemother. 49:269-275(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Crystal structures of human alpha-defensins HNP4, HD5, and HD6."
      Szyk A., Wu Z., Tucker K., Yang D., Lu W., Lubkowski J.
      Protein Sci. 15:2749-2760(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 63-94, FUNCTION, SUBUNIT, DISULFIDE BONDS.

    Entry informationi

    Entry nameiDEF5_HUMAN
    AccessioniPrimary (citable) accession number: Q01523
    Secondary accession number(s): A0JDY6, Q3KNV2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 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. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3