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P59665

- DEF1_HUMAN

UniProt

P59665 - DEF1_HUMAN

Protein

Neutrophil defensin 1

Gene

DEFA1

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

    Defensin 1 and defensin 2 have antibacterial, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane.2 Publications

    GO - Biological processi

    1. antibacterial humoral response Source: UniProt
    2. chemotaxis Source: ProtInc
    3. defense response to fungus Source: UniProtKB-KW
    4. defense response to Gram-positive bacterium Source: UniProt
    5. defense response to virus Source: UniProtKB-KW
    6. immune response Source: ProtInc
    7. innate immune response Source: UniProt
    8. innate immune response in mucosa Source: UniProt
    9. intracellular estrogen receptor signaling pathway Source: UniProt
    10. killing of cells of other organism Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Defensin, Fungicide

    Keywords - Biological processi

    Antiviral defense

    Enzyme and pathway databases

    ReactomeiREACT_115574. Alpha-defensins.
    REACT_115846. Defensins.

    Protein family/group databases

    TCDBi1.C.19.1.1. the defensin (defensin) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neutrophil defensin 1
    Alternative name(s):
    Defensin, alpha 1
    HNP-1
    Short name:
    HP-1
    Short name:
    HP1
    Cleaved into the following 2 chains:
    Alternative name(s):
    HNP-2
    Short name:
    HP-2
    Short name:
    HP2
    Gene namesi
    Name:DEFA1
    Synonyms:DEF1, DEFA2, MRS
    AND
    Name:DEFA1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:2761. DEFA1.
    HGNC:33596. DEFA1B.

    Subcellular locationi

    GO - Cellular componenti

    1. azurophil granule lumen Source: Reactome
    2. extracellular region Source: Reactome
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt
    5. Golgi lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA165585475.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Propeptidei20 – 3819PRO_0000006771Add
    BLAST
    Chaini39 – 9456HP 1-56PRO_0000006772Add
    BLAST
    Peptidei65 – 9430Neutrophil defensin 1PRO_0000006773Add
    BLAST
    Peptidei66 – 9429Neutrophil defensin 2PRO_0000006774Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi66 ↔ 941 Publication
    Disulfide bondi68 ↔ 831 Publication
    Disulfide bondi73 ↔ 931 Publication
    Modified residuei78 – 781ADP-ribosylarginine; by ART11 Publication
    Modified residuei85 – 851Phosphotyrosine1 Publication
    Modified residuei88 – 881ADP-ribosylarginine; by ART11 Publication

    Post-translational modificationi

    ADP-ribosylation drastically reduces cytotoxic and antibacterial activities, and enhances IL8 production.
    Phosphorylation at Tyr-85 has been found in some cancer cell lines, and interferes with ADP-ribosylation.1 Publication

    Keywords - PTMi

    ADP-ribosylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    PaxDbiP59665.
    PeptideAtlasiP59665.
    PRIDEiP59665.

    PTM databases

    PhosphoSiteiP59665.

    Miscellaneous databases

    PMAP-CutDBP59665.

    Expressioni

    Gene expression databases

    BgeeiP59665.
    CleanExiHS_DEFA1.
    GenevestigatoriP59665.

    Organism-specific databases

    HPAiCAB032548.
    HPA052517.

    Interactioni

    Subunit structurei

    Dimer.1 Publication

    Protein-protein interaction databases

    BioGridi108031. 3 interactions.
    IntActiP59665. 5 interactions.
    MINTiMINT-6631351.
    STRINGi9606.ENSP00000372126.

    Structurei

    Secondary structure

    1
    94
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi66 – 727
    Beta strandi79 – 857
    Beta strandi88 – 936

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KHTNMR-A65-94[»]
    2PM1X-ray1.60A65-94[»]
    3GNYX-ray1.56A/B65-94[»]
    3H6CX-ray1.63A/B65-94[»]
    3HJ2X-ray1.40A/B65-94[»]
    3HJDX-ray1.65A/B65-94[»]
    3LO1X-ray1.60A65-94[»]
    3LO2X-ray1.56A/B65-94[»]
    3LO4X-ray1.75A/B65-94[»]
    3LO6X-ray1.56A/B65-94[»]
    3LO9X-ray1.56A/B65-94[»]
    3LOEX-ray1.56A65-94[»]
    3LVXX-ray1.63A/B65-94[»]
    4DU0X-ray1.90A/B/C/D65-94[»]
    4LB1X-ray2.00A/B/D/E65-94[»]
    4LB7X-ray1.90A/B/D/E65-94[»]
    4LBBX-ray1.72A/B65-94[»]
    4LBFX-ray1.70A/B/C/D/E/F/G/H65-94[»]
    ProteinModelPortaliP59665.
    SMRiP59665. Positions 65-94.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP59665.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alpha-defensin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG86943.
    HOGENOMiHOG000233351.
    HOVERGENiHBG011703.
    InParanoidiP59665.
    KOiK05230.
    OMAiRVWAFCC.
    OrthoDBiEOG75TMFQ.
    PhylomeDBiP59665.
    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.

    P59665-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRTLAILAAI LLVALQAQAE PLQARADEVA AAPEQIAADI PEVVVSLAWD   50
    ESLAPKHPGS RKNMACYCRI PACIAGERRY GTCIYQGRLW AFCC 94
    Length:94
    Mass (Da):10,201
    Last modified:April 30, 2003 - v1
    Checksum:i0E0F8E95737396FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21130 mRNA. Translation: AAA52302.1.
    M26602 mRNA. Translation: AAA52303.1.
    L12690 Genomic DNA. Translation: AAA36382.1.
    X52053 mRNA. Translation: CAA36280.1.
    AF200455 Genomic DNA. Translation: AAT68875.1.
    AF200455 Genomic DNA. Translation: AAT68878.1.
    AF200455 Genomic DNA. Translation: AAT68879.1.
    AF200455 Genomic DNA. Translation: AAT68880.1.
    AF238378 Genomic DNA. Translation: AAT68883.1.
    AF238378 Genomic DNA. Translation: AAT68884.1.
    BC069423 mRNA. Translation: AAH69423.1.
    BC093791 mRNA. Translation: AAH93791.1.
    BC112188 mRNA. Translation: AAI12189.1.
    CCDSiCCDS34797.1.
    CCDS43691.1.
    PIRiS32499. A40499.
    RefSeqiNP_001035965.1. NM_001042500.1.
    NP_004075.1. NM_004084.3.
    UniGeneiHs.380781.

    Genome annotation databases

    EnsembliENST00000382679; ENSP00000372126; ENSG00000206047.
    ENST00000382689; ENSP00000372136; ENSG00000240247.
    ENST00000382692; ENSP00000372139; ENSG00000206047.
    ENST00000535841; ENSP00000443526; ENSG00000240247.
    GeneIDi1667.
    728358.
    KEGGihsa:1667.
    hsa:728358.
    UCSCiuc003wqv.1. human.

    Polymorphism databases

    DMDMi30316322.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21130 mRNA. Translation: AAA52302.1 .
    M26602 mRNA. Translation: AAA52303.1 .
    L12690 Genomic DNA. Translation: AAA36382.1 .
    X52053 mRNA. Translation: CAA36280.1 .
    AF200455 Genomic DNA. Translation: AAT68875.1 .
    AF200455 Genomic DNA. Translation: AAT68878.1 .
    AF200455 Genomic DNA. Translation: AAT68879.1 .
    AF200455 Genomic DNA. Translation: AAT68880.1 .
    AF238378 Genomic DNA. Translation: AAT68883.1 .
    AF238378 Genomic DNA. Translation: AAT68884.1 .
    BC069423 mRNA. Translation: AAH69423.1 .
    BC093791 mRNA. Translation: AAH93791.1 .
    BC112188 mRNA. Translation: AAI12189.1 .
    CCDSi CCDS34797.1.
    CCDS43691.1.
    PIRi S32499. A40499.
    RefSeqi NP_001035965.1. NM_001042500.1.
    NP_004075.1. NM_004084.3.
    UniGenei Hs.380781.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KHT NMR - A 65-94 [» ]
    2PM1 X-ray 1.60 A 65-94 [» ]
    3GNY X-ray 1.56 A/B 65-94 [» ]
    3H6C X-ray 1.63 A/B 65-94 [» ]
    3HJ2 X-ray 1.40 A/B 65-94 [» ]
    3HJD X-ray 1.65 A/B 65-94 [» ]
    3LO1 X-ray 1.60 A 65-94 [» ]
    3LO2 X-ray 1.56 A/B 65-94 [» ]
    3LO4 X-ray 1.75 A/B 65-94 [» ]
    3LO6 X-ray 1.56 A/B 65-94 [» ]
    3LO9 X-ray 1.56 A/B 65-94 [» ]
    3LOE X-ray 1.56 A 65-94 [» ]
    3LVX X-ray 1.63 A/B 65-94 [» ]
    4DU0 X-ray 1.90 A/B/C/D 65-94 [» ]
    4LB1 X-ray 2.00 A/B/D/E 65-94 [» ]
    4LB7 X-ray 1.90 A/B/D/E 65-94 [» ]
    4LBB X-ray 1.72 A/B 65-94 [» ]
    4LBF X-ray 1.70 A/B/C/D/E/F/G/H 65-94 [» ]
    ProteinModelPortali P59665.
    SMRi P59665. Positions 65-94.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108031. 3 interactions.
    IntActi P59665. 5 interactions.
    MINTi MINT-6631351.
    STRINGi 9606.ENSP00000372126.

    Protein family/group databases

    TCDBi 1.C.19.1.1. the defensin (defensin) family.

    PTM databases

    PhosphoSitei P59665.

    Polymorphism databases

    DMDMi 30316322.

    Proteomic databases

    PaxDbi P59665.
    PeptideAtlasi P59665.
    PRIDEi P59665.

    Protocols and materials databases

    DNASUi 1667.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000382679 ; ENSP00000372126 ; ENSG00000206047 .
    ENST00000382689 ; ENSP00000372136 ; ENSG00000240247 .
    ENST00000382692 ; ENSP00000372139 ; ENSG00000206047 .
    ENST00000535841 ; ENSP00000443526 ; ENSG00000240247 .
    GeneIDi 1667.
    728358.
    KEGGi hsa:1667.
    hsa:728358.
    UCSCi uc003wqv.1. human.

    Organism-specific databases

    CTDi 1667.
    728358.
    GeneCardsi GC08M006822.
    GC08M006843.
    HGNCi HGNC:2761. DEFA1.
    HGNC:33596. DEFA1B.
    HPAi CAB032548.
    HPA052517.
    MIMi 125220. gene.
    neXtProti NX_P59665.
    PharmGKBi PA165585475.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG86943.
    HOGENOMi HOG000233351.
    HOVERGENi HBG011703.
    InParanoidi P59665.
    KOi K05230.
    OMAi RVWAFCC.
    OrthoDBi EOG75TMFQ.
    PhylomeDBi P59665.
    TreeFami TF338414.

    Enzyme and pathway databases

    Reactomei REACT_115574. Alpha-defensins.
    REACT_115846. Defensins.

    Miscellaneous databases

    ChiTaRSi DEFA1. human.
    EvolutionaryTracei P59665.
    GeneWikii DEFA1B.
    Defensin,_alpha_1.
    NextBioi 6860.
    PMAP-CutDB P59665.
    PROi P59665.
    SOURCEi Search...

    Gene expression databases

    Bgeei P59665.
    CleanExi HS_DEFA1.
    Genevestigatori P59665.

    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. "Isolation and characterization of human defensin cDNA clones."
      Daher K.A., Lehrer R.I., Ganz T., Kronenberg M.
      Proc. Natl. Acad. Sci. U.S.A. 85:7327-7331(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "A myeloid-related sequence that localizes to human chromosome 8q21.1-22."
      Mars W.M., vanTuinen P., Drabkin H.A., White J.W., Saunders G.F.
      Blood 71:1713-1719(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Differentiation stage-specific expression of a gene during granulopoiesis."
      Wiedemann L.M., Francis G.E., Lamb R.F., Burns J.H., Winnie J.N., McKenzie E.D., Birnie G.D.
      Leukemia 3:227-234(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Inheritance of unequal numbers of the genes encoding the human neutrophil defensins HP-1 and HP-3."
      Mars W.M., Patmasiriwat P., Maity T., Huff V., Weil M.M., Saunders G.F.
      J. Biol. Chem. 270:30371-30376(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "The structure of neutrophil defensin genes."
      Linzmeier R., Michaelson D., Liu L., Ganz T.
      FEBS Lett. 321:267-273(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "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].
    7. "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].
      Tissue: Liver.
    8. Cited for: PROTEIN SEQUENCE OF 65-94.
    9. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-34.
    10. "Determination of the disulfide array in the human defensin HNP-2. A covalently cyclized peptide."
      Selsted M.E., Harwig S.S.L.
      J. Biol. Chem. 264:4003-4007(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    11. "The isolation and identification of multiple forms of the neutrophil granule peptides from human leukemic cells."
      Bateman A., Singh A., Shustik C., Mars W.M., Solomon S.
      J. Biol. Chem. 266:7524-7530(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING.
    12. "Posttranslational processing of defensins in immature human myeloid cells."
      Valore E.V., Ganz T.
      Blood 79:1538-1544(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING.
    13. "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.
    14. "Structural and functional consequences induced by post-translational modifications in alpha-Defensins."
      Balducci E., Bonucci A., Picchianti M., Pogni R., Talluri E.
      Int. J. Pept. 2011:594723-594723(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ADP-RIBOSYLATION AT ARG-78 AND ARG-88 BY ART1, PHOSPHORYLATION AT TYR-85.
    15. "NMR studies of defensin antimicrobial peptides. 1. Resonance assignment and secondary structure determination of rabbit NP-2 and human HNP-1."
      Zhang X.-L., Selsted M.E., Pardi A.
      Biochemistry 31:11348-11356(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF DEFENSIN 1.
    16. "NMR studies of defensin antimicrobial peptides. 2. Three-dimensional structures of rabbit NP-2 and human HNP-1."
      Pardi A., Zhang X.-L., Selsted M.E., Skalicky J.J., Yip P.F.
      Biochemistry 31:11357-11364(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF DEFENSIN 1.
    17. "Toward understanding the cationicity of defensins. Arg and Lys versus their noncoded analogs."
      Zou G., de Leeuw E., Li C., Pazgier M., Li C., Zeng P., Lu W.-Y., Lubkowski J., Lu W.
      J. Biol. Chem. 282:19653-19665(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 65-94, FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiDEF1_HUMAN
    AccessioniPrimary (citable) accession number: P59665
    Secondary accession number(s): P11479, Q14125, Q6EZF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 30, 2003
    Last sequence update: April 30, 2003
    Last modified: October 1, 2014
    This is version 124 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. 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