Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Neutrophil defensin 3

Gene

DEFA3

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

Functioni

Defensin 2 and defensin 3 have antibiotic, 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.4 Publications

GO - Biological processi

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

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Defensin, Fungicide

Keywords - Biological processi

Antiviral defense

Enzyme and pathway databases

ReactomeiREACT_115574. Alpha-defensins.
REACT_115846. Defensins.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutrophil defensin 3
Alternative name(s):
Defensin, alpha 3
HNP-3
Short name:
HP-3
Short name:
HP3
Cleaved into the following 2 chains:
Alternative name(s):
HNP-2
Short name:
HP-2
Short name:
HP2
Gene namesi
Name:DEFA3
Synonyms:DEF3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:2762. DEFA3.

Subcellular locationi

GO - Cellular componenti

  1. azurophil granule lumen Source: Reactome
  2. extracellular region Source: Reactome
  3. extracellular space Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. Golgi lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27239.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Propeptidei20 – 3819PRO_0000006777Add
BLAST
Chaini39 – 9456HP 3-56PRO_0000006778Add
BLAST
Peptidei65 – 9430Neutrophil defensin 3PRO_0000006779Add
BLAST
Peptidei66 – 9429Neutrophil defensin 2PRO_0000006780Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi66 ↔ 94
Disulfide bondi68 ↔ 83
Disulfide bondi73 ↔ 93

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP59666.
PRIDEiP59666.

PTM databases

PhosphoSiteiP59666.

Miscellaneous databases

PMAP-CutDBP59666.

Expressioni

Gene expression databases

BgeeiP59666.
CleanExiHS_DEFA3.
ExpressionAtlasiP59666. baseline.
GenevestigatoriP59666.

Organism-specific databases

HPAiHPA052517.

Interactioni

Subunit structurei

Dimer.2 Publications

Protein-protein interaction databases

IntActiP59666. 2 interactions.
MINTiMINT-1409240.
STRINGi9606.ENSP00000328359.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi67 – 715Combined sources
Beta strandi78 – 858Combined sources
Beta strandi88 – 947Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DFNX-ray1.90A/B65-94[»]
1ZMHX-ray1.50A/B/C/D66-94[»]
1ZMIX-ray1.15A/B/C/D66-94[»]
1ZMKX-ray1.30A/B66-94[»]
2PM4X-ray1.95A/B65-94[»]
2PM5X-ray2.40A/B65-94[»]
ProteinModelPortaliP59666.
SMRiP59666. Positions 66-94.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP59666.

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha-defensin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG86943.
HOGENOMiHOG000233351.
HOVERGENiHBG011703.
InParanoidiP59666.
KOiK05230.
OMAiQERDDEA.
OrthoDBiEOG75TMFQ.
PhylomeDBiP59666.
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.

P59666-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRTLAILAAI LLVALQAQAE PLQARADEVA AAPEQIAADI PEVVVSLAWD
60 70 80 90
ESLAPKHPGS RKNMDCYCRI PACIAGERRY GTCIYQGRLW AFCC
Length:94
Mass (Da):10,245
Last modified:April 30, 2003 - v1
Checksum:i0E0F8E957376C6AF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21131 mRNA. Translation: AAA35753.2.
M23281 mRNA. Translation: AAA52304.1.
L12691 Genomic DNA. Translation: AAB57722.1.
X13621 mRNA. Translation: CAA31952.1.
BC027917 mRNA. Translation: AAH27917.1.
CCDSiCCDS5962.1.
PIRiC40499.
RefSeqiNP_005208.1. NM_005217.3.
UniGeneiHs.654448.

Genome annotation databases

EnsembliENST00000327857; ENSP00000328359; ENSG00000239839.
GeneIDi1668.
KEGGihsa:1668.

Polymorphism databases

DMDMi30316323.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21131 mRNA. Translation: AAA35753.2.
M23281 mRNA. Translation: AAA52304.1.
L12691 Genomic DNA. Translation: AAB57722.1.
X13621 mRNA. Translation: CAA31952.1.
BC027917 mRNA. Translation: AAH27917.1.
CCDSiCCDS5962.1.
PIRiC40499.
RefSeqiNP_005208.1. NM_005217.3.
UniGeneiHs.654448.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DFNX-ray1.90A/B65-94[»]
1ZMHX-ray1.50A/B/C/D66-94[»]
1ZMIX-ray1.15A/B/C/D66-94[»]
1ZMKX-ray1.30A/B66-94[»]
2PM4X-ray1.95A/B65-94[»]
2PM5X-ray2.40A/B65-94[»]
ProteinModelPortaliP59666.
SMRiP59666. Positions 66-94.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP59666. 2 interactions.
MINTiMINT-1409240.
STRINGi9606.ENSP00000328359.

PTM databases

PhosphoSiteiP59666.

Polymorphism databases

DMDMi30316323.

Proteomic databases

PaxDbiP59666.
PRIDEiP59666.

Protocols and materials databases

DNASUi1668.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327857; ENSP00000328359; ENSG00000239839.
GeneIDi1668.
KEGGihsa:1668.

Organism-specific databases

CTDi1668.
GeneCardsiGC08M006875.
HGNCiHGNC:2762. DEFA3.
HPAiHPA052517.
MIMi604522. gene.
neXtProtiNX_P59666.
PharmGKBiPA27239.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG86943.
HOGENOMiHOG000233351.
HOVERGENiHBG011703.
InParanoidiP59666.
KOiK05230.
OMAiQERDDEA.
OrthoDBiEOG75TMFQ.
PhylomeDBiP59666.
TreeFamiTF338414.

Enzyme and pathway databases

ReactomeiREACT_115574. Alpha-defensins.
REACT_115846. Defensins.

Miscellaneous databases

EvolutionaryTraceiP59666.
GeneWikiiDEFA3.
GenomeRNAii1668.
NextBioi6864.
PMAP-CutDBP59666.
PROiP59666.
SOURCEiSearch...

Gene expression databases

BgeeiP59666.
CleanExiHS_DEFA3.
ExpressionAtlasiP59666. baseline.
GenevestigatoriP59666.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "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].
  3. "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].
  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].
    Tissue: Pancreas and Spleen.
  5. Cited for: PROTEIN SEQUENCE OF 65-94.
  6. "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.
  7. "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.
  8. "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.
  9. "Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization."
    Hill C.P., Yee J., Selsted M.E., Eisenberg D.
    Science 251:1481-1485(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF DEFENSIN 3, SUBUNIT, FUNCTION.
  10. "Reconstruction of the conserved beta-bulge in mammalian defensins using D-amino acids."
    Xie C., Prahl A., Ericksen B., Wu Z., Zeng P., Li X., Lu W.-Y., Lubkowski J., Lu W.
    J. Biol. Chem. 280:32921-32929(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 66-94, DISULFIDE BONDS, FUNCTION.
  11. "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 (2.4 ANGSTROMS) OF 65-94, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiDEF3_HUMAN
AccessioniPrimary (citable) accession number: P59666
Secondary accession number(s): P11479, Q14125
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: January 7, 2015
This is version 110 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.